The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface
The Agrobacterium tumefaciens virB7 gene product contains a typical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of bacterial lipoproteins. VirB7 was shown to be processed as a lipoprotein by (i) in vivo labeling of native VirB7 and a VirB7::PhoA fusion wi...
Saved in:
Published in | Journal of Bacteriology Vol. 178; no. 11; pp. 3156 - 3167 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Microbiology
01.06.1996
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The Agrobacterium tumefaciens virB7 gene product contains a typical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of bacterial lipoproteins. VirB7 was shown to be processed as a lipoprotein by (i) in vivo labeling of native VirB7 and a VirB7::PhoA fusion with [3H]palmitic acid and (ii) inhibition of VirB7 processing by globomycin, a known inhibitor of signal peptidase II. A VirB7 derivative sustaining a Ser substitution for the invariant Cys-15 residue within the signal peptidase II cleavage site could not be visualized immunologically and failed to complement a (delta)virB7 mutation, establishing the importance of this putative lipid attachment site for VirB7 maturation and function. VirB7 partitioned predominantly with outer membrane fractions from wild-type A348 cells as well as a (delta)virB operon derivative transformed with a virB7 expression plasmid. Expression of virB7 fused to phoA, the alkaline phosphatase gene of Escherichia coli, gave rise to high alkaline phosphatase activities in E. coli and A. tumefaciens cells, providing genetic evidence for the export of VirB7 in these hosts. VirB7 was shown to be intrinsically resistant to proteinase K; by contrast, a VirB7::PhoA derivative was degraded by proteinase K treatment of A. tumefaciens spheroplasts and remained intact upon treatment of whole cells. Together, the results of these studies favor a model in which VirB7 is topologically configured as a monotopic protein with its amino terminus anchored predominantly to the outer membrane and with its hydrophilic carboxyl domain located in the periplasmic space. Parallel studies of VirB5, VirB8, VirB9, and VirB10 established that each of these membrane-associated proteins also contains a large periplasmic domain whereas VirB11 resides predominantly or exclusively within the interior of the cell |
---|---|
AbstractList | The Agrobacterium tumefaciens virB7 gene product contains a typical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of bacterial lipoproteins. VirB7 was shown to be processed as a lipoprotein by (i) in vivo labeling of native VirB7 and a VirB7::PhoA fusion with [3H]palmitic acid and (ii) inhibition of VirB7 processing by globomycin, a known inhibitor of signal peptidase II. A VirB7 derivative sustaining a Ser substitution for the invariant Cys-15 residue within the signal peptidase II cleavage site could not be visualized immunologically and failed to complement a delta virB7 mutation, establishing the importance of this putative lipid attachment site for VirB7 maturation and function. VirB7 partitioned predominantly with outer membrane fractions from wild-type A348 cells as well as a delta virB operon derivative transformed with a virB7 expression plasmid. Expression of virB7 fused to phoA, the alkaline phosphatase gene of Escherichia coli, gave rise to high alkaline phosphatase activities in E. coli and A. tumefaciens cells, providing genetic evidence for the export of VirB7 in these hosts. VirB7 was shown to be intrinsically resistant to proteinase K; by contrast, a VirB7::PhoA derivative was degraded by proteinase K treatment of A. tumefaciens spheroplasts and remained intact upon treatment of whole cells. Together, the results of these studies favor a model in which VirB7 is topologically configured as a monotopic protein with its amino terminus anchored predominantly to the outer membrane and with its hydrophilic carboxyl domain located in the periplasmic space. Parallel studies of VirB5, VirB8, VirB9, and VirB10 established that each of these membrane-associated proteins also contains a large periplasmic domain whereas VirB11 resides predominantly or exclusively within the interior of the cell. Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: JB The Agrobacterium tumefaciens virB7 gene product contains a typical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of bacterial lipoproteins. VirB7 was shown to be processed as a lipoprotein by (i) in vivo labeling of native VirB7 and a VirB7::PhoA fusion with [ super(3)H]palmitic acid and (ii) inhibition of VirB7 processing by globomycin, a known inhibitor of signal peptidase II. A VirB7 derivative sustaining a Ser substitution for the invariant Cys-15 residue within the signal peptidase II cleavage site could not be visualized immunologically and failed to complement a Delta virB7 mutation, establishing the importance of this putative lipid attachment site for VirB7 maturation and function. VirB7 partitioned predominantly with outer membrane fractions from wild-type A348 cells as well as a Delta virB operon derivative transformed with a virB7 expression plasmid. Expression of virB7 fused to phoA, the alkaline phosphatase gene of Escherichia coli gave rise to high alkaline phosphatase activities in E. coli and A. tumefaciens cells, providing genetic evidence for the export of VirB7 in these hosts. VirB7 was shown to be intrinsically resistant to proteinase K; by contrast, a VirB7::PhoA derivative was degraded by proteinase K treatment of A. tumefaciens spheroplasts and remained intact upon treatment of whole cells. Together, the results of these studies favor a model in which VirB7 is topologically configured as a monotopic protein with its amino terminus anchored predominantly to the outer membrane and with its hydrophilic carboxyl domain located in the periplasmic space. Parallel studies of VirB5, VirB8, VirB9, and VirB10 established that each of these membrane-associated proteins also contains a large periplasmic domain whereas VirB11 resides predominantly or exclusively within the interior of the cell. The Agrobacterium tumefaciens virB7 gene product is topologically configured as a monotopic protein, with its amino terminus anchored predominantly to the outer membrane. The Agrobacterium tumefaciens virB7 gene product contains a typical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of bacterial lipoproteins. VirB7 was shown to be processed as a lipoprotein by (i) in vivo labeling of native VirB7 and a VirB7::PhoA fusion with [3H]palmitic acid and (ii) inhibition of VirB7 processing by globomycin, a known inhibitor of signal peptidase II. A VirB7 derivative sustaining a Ser substitution for the invariant Cys-15 residue within the signal peptidase II cleavage site could not be visualized immunologically and failed to complement a (delta)virB7 mutation, establishing the importance of this putative lipid attachment site for VirB7 maturation and function. VirB7 partitioned predominantly with outer membrane fractions from wild-type A348 cells as well as a (delta)virB operon derivative transformed with a virB7 expression plasmid. Expression of virB7 fused to phoA, the alkaline phosphatase gene of Escherichia coli, gave rise to high alkaline phosphatase activities in E. coli and A. tumefaciens cells, providing genetic evidence for the export of VirB7 in these hosts. VirB7 was shown to be intrinsically resistant to proteinase K; by contrast, a VirB7::PhoA derivative was degraded by proteinase K treatment of A. tumefaciens spheroplasts and remained intact upon treatment of whole cells. Together, the results of these studies favor a model in which VirB7 is topologically configured as a monotopic protein with its amino terminus anchored predominantly to the outer membrane and with its hydrophilic carboxyl domain located in the periplasmic space. Parallel studies of VirB5, VirB8, VirB9, and VirB10 established that each of these membrane-associated proteins also contains a large periplasmic domain whereas VirB11 resides predominantly or exclusively within the interior of the cell |
Author | Christie, P.J Spudich, G.M Zhou, X.R Fernandez, D. (The University of Texas Health Science Center at Houston, Houston, TX.) Dang, T.A.T Berger, B.R |
AuthorAffiliation | Department of Microbiology and Molecular Genetics, The University of Texas Health Science Center at Houston, 77030, USA |
AuthorAffiliation_xml | – name: Department of Microbiology and Molecular Genetics, The University of Texas Health Science Center at Houston, 77030, USA |
Author_xml | – sequence: 1 fullname: Fernandez, D. (The University of Texas Health Science Center at Houston, Houston, TX.) – sequence: 2 fullname: Dang, T.A.T – sequence: 3 fullname: Spudich, G.M – sequence: 4 fullname: Zhou, X.R – sequence: 5 fullname: Berger, B.R – sequence: 6 fullname: Christie, P.J |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8655494$$D View this record in MEDLINE/PubMed |
BookMark | eNqFUstu1DAUjVBRmRZ-AAnJYsGqGfyIHXvBolS8pEosmK4tx3FmPEriYDtt-S8-kBtmVKAbVr7yPef4XN9zVpyMYXRFgQheE0Ll232zJrWEes0IFyUjol4TpcSTYkWwkiXnDJ8UK4wpKRVR7FlxltIeY1JVnJ4Wp1JwXqlqVfzc7By63MbQGJtd9POA8jy4zljvxoRufXxfo60bHZpiaGebL5BZyikk1yIbhgmMjRmFDmVQ2pTLVe_uUY5mTFOIGZlpMtHkOV0gn4A9uKGBpitNSsF6k0Go91MA1ez8iNz9Qdzk35ITuJp6kwZvUZojOHPPi6ed6ZN7cTzPi5uPHzZXn8vrr5--XF1el5bXLJdNRXkLeGy61jSdrK2lFeNWCMuwZG0rOoUloS1hppLAIY603HSC8lo1mLLz4t1Bd5qbwbUWBo2m11P0g4k_dDBe_9sZ_U5vw62G3WAhgP_myI_h--xS1oNP1vU9TB_mpAHFq5pX_wXCjrGsxOLo9SPgPsxxhE_QlNZY1LWSAJIHkI0hpei6B8cE6yU-et8sFqHWS3z0Eh-9xAeor_6e-IF4zMuf93d-u7vz0WlYzCM5AL08gDoTtNlGn_TNNyWoZEqxX5l_3CU |
CODEN | JOBAAY |
CitedBy_id | crossref_primary_10_1128_JB_183_12_3642_3651_2001 crossref_primary_10_1080_07352689709701951 crossref_primary_10_1128_JB_00557_10 crossref_primary_10_1111_j_1365_2958_2004_04378_x crossref_primary_10_1016_j_plasmid_2012_09_002 crossref_primary_10_1128_jb_179_3_583_591_1997 crossref_primary_10_1111_j_1758_2229_2009_00110_x crossref_primary_10_1046_j_1364_3703_2003_00163_x crossref_primary_10_1046_j_1365_2958_1998_00908_x crossref_primary_10_1016_j_tim_2015_02_012 crossref_primary_10_1111_j_1574_6976_1998_tb00355_x crossref_primary_10_1128_JB_181_14_4342_4352_1999 crossref_primary_10_1128_JB_187_10_3486_3495_2005 crossref_primary_10_1021_bi902201y crossref_primary_10_1073_pnas_0408927102 crossref_primary_10_1128_jb_179_10_3085_3094_1997 crossref_primary_10_1016_S1369_5274_99_80004_6 crossref_primary_10_1016_j_plasmid_2005_02_001 crossref_primary_10_1016_j_tibs_2010_06_002 crossref_primary_10_1126_science_1166101 crossref_primary_10_1042_BJ20091518 crossref_primary_10_1128_JB_00038_11 crossref_primary_10_1128_JB_186_5_1415_1422_2004 crossref_primary_10_1046_j_1365_2958_2001_02502_x crossref_primary_10_1128_JB_183_20_5813_5825_2001 crossref_primary_10_1016_S0966_842X_02_02314_4 crossref_primary_10_1128_JB_182_15_4137_4145_2000 crossref_primary_10_1128_AEM_70_12_7497_7510_2004 crossref_primary_10_1038_s41467_022_28058_5 crossref_primary_10_1128_jb_179_18_5835_5842_1997 crossref_primary_10_1371_journal_ppat_1002031 crossref_primary_10_1128_jb_179_1_78_89_1997 crossref_primary_10_1073_pnas_172390699 crossref_primary_10_1096_fj_15_270843 crossref_primary_10_1128_jb_178_11_3168_3176_1996 crossref_primary_10_1128_JB_185_16_4983_4991_2003 crossref_primary_10_1016_j_jmb_2004_06_052 crossref_primary_10_1371_journal_pone_0004833 crossref_primary_10_1046_j_1462_5822_2003_00286_x crossref_primary_10_1111_1574_6976_12085 crossref_primary_10_1128_JB_187_13_4306_4314_2005 crossref_primary_10_1128_JB_185_9_2867_2878_2003 crossref_primary_10_1073_pnas_0505290102 crossref_primary_10_1128_IAI_01207_09 crossref_primary_10_1128_JB_182_3_758_763_2000 crossref_primary_10_1128_JB_00029_09 crossref_primary_10_1128_JB_180_24_6597_6606_1998 crossref_primary_10_1128_IAI_73_11_7578_7587_2005 crossref_primary_10_1128_JB_01331_09 crossref_primary_10_1128_JB_185_3_760_771_2003 crossref_primary_10_1016_S1369_5274_98_80110_0 crossref_primary_10_1046_j_1364_3703_2000_00026_x crossref_primary_10_1128_jb_179_11_3404_3409_1997 crossref_primary_10_1128_jb_179_4_1203_1210_1997 crossref_primary_10_1042_BST20120332 crossref_primary_10_1128_MMBR_00023_09 crossref_primary_10_1099_00221287_147_12_3201 crossref_primary_10_1046_j_1365_2958_2003_03669_x crossref_primary_10_1016_j_plasmid_2013_03_006 crossref_primary_10_1128_JB_180_4_885_891_1998 crossref_primary_10_1038_nrmicro2218 crossref_primary_10_1128_JB_182_12_3437_3445_2000 crossref_primary_10_1016_j_bbamcr_2004_02_013 crossref_primary_10_1128_IAI_01384_09 crossref_primary_10_1016_S0955_0674_00_00111_3 crossref_primary_10_1146_annurev_biochem_062911_102821 crossref_primary_10_1016_S0966_842X_00_01792_3 crossref_primary_10_1046_j_1365_2958_1998_00688_x crossref_primary_10_1128_JB_183_12_3636_3641_2001 crossref_primary_10_1139_o06_148 crossref_primary_10_1146_annurev_micro_58_030603_123630 crossref_primary_10_1371_journal_pone_0175273 crossref_primary_10_1111_mpp_12159 crossref_primary_10_1046_j_1365_2958_1999_01436_x crossref_primary_10_1128_jb_179_2_453_462_1997 crossref_primary_10_1128_jb_179_4_1211_1218_1997 crossref_primary_10_1128_JB_184_20_5572_5582_2002 crossref_primary_10_1128_JB_183_13_3855_3865_2001 crossref_primary_10_1128_JB_00945_08 |
Cites_doi | 10.1073/pnas.86.24.9677 10.1146/annurev.py.32.090194.001105 10.1128/jb.123.1.255-264.1975 10.1016/S0021-9258(18)42771-8 10.1128/jb.174.23.7661-7669.1992 10.1128/jb.171.3.1616-1622.1989 10.1128/IAI.63.8.3227-3230.1995 10.1073/pnas.90.7.2970 10.1146/annurev.pp.43.060192.002341 10.1126/science.256.5061.1324 10.1016/0966-842X(96)81513-7 10.1128/JB.175.16.5233-5241.1993 10.1104/pp.107.4.1041 10.1038/318624a0 10.1128/mr.57.4.995-1017.1993 10.1016/0092-8674(94)90146-5 10.1016/S0091-679X(08)61676-3 10.1073/pnas.90.24.11538 10.1128/jb.171.11.5830-5839.1989 10.1073/pnas.82.23.8129 10.1038/328172a0 10.1111/j.1365-2958.1990.tb00690.x 10.1128/JB.176.12.3646-3660.1994 10.1002/j.1460-2075.1995.tb07342.x 10.1007/BF00297277 10.1073/pnas.90.7.2925 10.1128/JB.173.3.1139-1144.1991 10.1016/S0021-9258(18)55322-9 10.1128/jb.174.7.2095-2101.1992 10.1128/jb.175.6.1723-1734.1993 10.1006/plas.1994.1057 10.1128/JB.172.9.5187-5199.1990 10.1128/jb.171.1.511-520.1989 10.1128/JB.178.11.3168-3176.1996 10.1128/JB.169.12.5692-5699.1987 10.1016/S0021-9258(18)60637-4 10.1128/JB.177.17.4881-4889.1995 10.1007/BF00332739 10.1073/pnas.88.21.9603 10.1128/JB.173.17.5523-5531.1991 10.1111/j.1365-2958.1994.tb00990.x 10.1016/S0021-9258(19)84474-5 10.1128/JB.161.1.402-410.1985 10.1111/j.1365-2958.1990.tb02015.x 10.1111/j.1365-2958.1993.tb01587.x 10.1016/S0021-9258(19)85762-9 10.1016/0003-2697(87)90587-2 10.1128/jb.170.6.2659-2667.1988 10.1128/JB.167.3.1083-1085.1986 10.1128/jb.175.5.1543-1547.1993 10.1128/JB.177.10.2892-2900.1995 10.1128/MR.58.2.162-210.1994 10.1128/JB.177.16.4779-4791.1995 10.1111/j.1365-2958.1994.tb01304.x 10.1128/mr.57.1.50-108.1993 10.1093/nar/16.10.4621 10.1016/S0021-9258(19)88726-4 10.1128/jb.174.24.7982-7988.1992 10.1002/j.1460-2075.1986.tb04381.x 10.1128/JB.176.6.1711-1717.1994 10.1128/JB.172.9.5200-5210.1990 10.1007/978-1-4757-9357-4_9 10.1007/BF00261729 10.1002/j.1460-2075.1987.tb02679.x 10.1128/JB.177.17.4890-4899.1995 10.1111/j.1574-6968.1993.tb06400.x 10.1128/JB.175.20.6415-6425.1993 10.1128/jb.177.1.27-36.1995 10.1007/BF00763177 10.1016/S0021-9258(19)39628-0 10.1002/j.1460-2075.1987.tb04831.x 10.1016/0092-8674(81)90368-8 10.1111/j.1365-2958.1993.tb01235.x |
ContentType | Journal Article |
Copyright | Copyright American Society for Microbiology Jun 1996 |
Copyright_xml | – notice: Copyright American Society for Microbiology Jun 1996 |
DBID | FBQ CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7TM 7U9 8FD C1K FR3 H94 M7N P64 RC3 7X8 5PM |
DOI | 10.1128/jb.178.11.3156-3167.1996 |
DatabaseName | AGRIS Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Bacteriology Abstracts (Microbiology B) Nucleic Acids Abstracts Virology and AIDS Abstracts Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database AIDS and Cancer Research Abstracts Algology Mycology and Protozoology Abstracts (Microbiology C) Biotechnology and BioEngineering Abstracts Genetics Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Genetics Abstracts Virology and AIDS Abstracts Technology Research Database Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) Nucleic Acids Abstracts AIDS and Cancer Research Abstracts Engineering Research Database Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management MEDLINE - Academic |
DatabaseTitleList | MEDLINE - Academic MEDLINE Bacteriology Abstracts (Microbiology B) Genetics Abstracts CrossRef |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1098-5530 1067-8832 |
EndPage | 3167 |
ExternalDocumentID | 9734300 10_1128_jb_178_11_3156_3167_1996 8655494 jb_178_11_3156 US9628399 |
Genre | Research Support, U.S. Gov't, P.H.S Journal Article Feature |
GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM048746 – fundername: NIGMS NIH HHS grantid: GM48746 |
GroupedDBID | --- -DZ -~X .55 .GJ 0R~ 186 18M 1VV 29J 2WC 39C 3O- 4.4 53G 5GY 5RE 5VS 79B 85S 8WZ 9M8 A6W ABPPZ ABPTK ABTAH ACGFO ACGOD ACNCT ACPRK ADBBV AENEX AEQTP AFDAS AFFDN AFFNX AFMIJ AFRAH AGCDD AI. AIDAL AJUXI ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BKOMP BTFSW C1A CJ0 CS3 DIK DU5 E3Z EBS EJD F20 F5P FBQ FRP GX1 HYE HZ~ IH2 KQ8 L7B MVM NHB O9- OHT OK1 P-S P2P PQQKQ QZG RHF RHI RNS RPM RSF RXW TAE TR2 UCJ UHB UKR UPT VH1 VQA W8F WH7 WHG WOQ X7M XFK Y6R YQT YR2 YZZ ZA5 ZCA ZCG ZGI ZXP ZY4 ~02 ~KM AGVNZ CGR CUY CVF ECM EIF H13 NPM AAYXX CITATION 7QL 7TM 7U9 8FD C1K FR3 H94 M7N P64 RC3 7X8 5PM |
ID | FETCH-LOGICAL-c573t-b425dfac0afdabf87cc2435c66c3083dd6f90812d13a48c571e1d5af62579b023 |
IEDL.DBID | RPM |
ISSN | 0021-9193 |
IngestDate | Tue Sep 17 21:09:02 EDT 2024 Fri Aug 16 05:30:44 EDT 2024 Sat Aug 17 04:01:33 EDT 2024 Fri Sep 13 07:57:43 EDT 2024 Thu Sep 12 18:51:26 EDT 2024 Sat Sep 28 08:40:39 EDT 2024 Wed May 18 15:26:16 EDT 2016 Wed Dec 27 19:29:16 EST 2023 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 11 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c573t-b425dfac0afdabf87cc2435c66c3083dd6f90812d13a48c571e1d5af62579b023 |
Notes | 9628399 H20 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
OpenAccessLink | https://europepmc.org/articles/pmc178066?pdf=render |
PMID | 8655494 |
PQID | 227067798 |
PQPubID | 40724 |
PageCount | 12 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_178066 pubmed_primary_8655494 highwire_asm_jb_178_11_3156 fao_agris_US9628399 proquest_miscellaneous_78054754 proquest_miscellaneous_15608462 proquest_journals_227067798 crossref_primary_10_1128_jb_178_11_3156_3167_1996 |
PublicationCentury | 1900 |
PublicationDate | 1996-06-01 |
PublicationDateYYYYMMDD | 1996-06-01 |
PublicationDate_xml | – month: 06 year: 1996 text: 1996-06-01 day: 01 |
PublicationDecade | 1990 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: Washington |
PublicationTitle | Journal of Bacteriology |
PublicationTitleAlternate | J Bacteriol |
PublicationYear | 1996 |
Publisher | American Society for Microbiology |
Publisher_xml | – name: American Society for Microbiology |
References | Matsuyama S. (p_44) 1995; 14 Weiss A. A. (p_76) 1993; 90 Gennity J. M. (p_24) 1991; 266 Hayashi S. (p_27) 1990; 22 Finberg K. E. (p_20) 1995; 177 p_45 Takase I. (p_65) 1987; 169 Binns A. N. (p_6) 1995; 177 Beijersbergen A. (p_2) 1992; 256 Haase J. (p_26) 1995; 177 Bouvier J. (p_7) 1991; 173 Gennity J. M. (p_25) 1992; 174 Poquet I. (p_51) 1993; 9 Ward J. E. (p_74) 1990; 172 Winans S. C. (p_77) 1996; 4 Thorstenson Y. R. (p_68) 1994; 176 Hooykaas P. J. J. (p_28) 1994; 32 Shirasu K. (p_58) 1990; 4 Stachel S. E. (p_62) 1987; 6 Hussain M. (p_29) 1980; 255 Margolin W. (p_43) 1995; 177 Winans S. C. (p_78) 1989; 171 Kuldau G. A. (p_35) 1990; 221 Leduc M. (p_37) 1992; 174 Schagger H. (p_56) 1987; 166 Sugiyama J. E. (p_64) 1991; 88 p_36 Choi D. (p_10) 1986; 261 Pansegrau W. (p_48) 1993; 90 Thorstenson Y. R. (p_67) 1993; 175 Ward J. E. (p_72) 1990; 265 Shirasu K. (p_57) 1993; 111 Kado C. I. (p_33) 1994; 12 Enfert C. (p_15) 1987; 6 Buchanan-Wollaston V. (p_8) 1987; 328 Manoil C. (p_41) 1991; 34 Christie P. J. (p_12) 1988; 170 Fullner K. J. (p_22) 1994; 245 Zupan J. R. (p_81) 1995; 107 p_30 p_32 Thompson D. V. (p_66) 1988; 16 de Maagd R. A. (p_17) 1986; 167 Oudega B. (p_47) 1993; 175 Jung J. U. (p_31) 1989; 171 Pansegrau W. (p_49) 1993; 90 Frost L. S. (p_21) 1994; 58 Pugsley A. P. (p_52) 1993; 57 Garfinkel D. J. (p_23) 1981; 27 Beijersbergen A. (p_3) 1994; 32 Stachel S. E. (p_61) 1986; 5 Lessl M. (p_38) 1992; 267 Traxler B. (p_69) 1992; 267 Pohlman R. F. (p_50) 1994; 14 Zambryski P. C. (p_80) 1992; 43 De Graaf F. K. (p_16) 1986; 125 Manoil C. (p_42) 1985; 82 Otten L. (p_46) 1984; 195 Berger B. R. (p_4) 1993; 175 Fath M. J. (p_18) 1993; 57 Lessl M. (p_39) 1993; 175 Pugsley A. P. (p_53) 1990; 4 Ward J. E. (p_71) 1988; 263 p_14 p_59 Ward J. E. (p_73) 1990; 172 Chen C. (p_9) 1991; 173 Watson B. (p_75) 1975; 123 Christie P. J. (p_11) 1989; 86 Varga A. R. (p_70) 1989; 171 Fernandez D. (p_19) 1996; 178 Kotob S. I. (p_34) 1995; 63 Berger B. R. (p_5) 1994; 176 Stephens K. M. (p_63) 1995; 177 Covacci A. (p_13) 1993; 8 Lessl M. (p_40) 1994; 77 p_54 p_55 Stachel S. E. (p_60) 1985; 318 Allaoui A. (p_1) 1992; 174 Winans S. C. (p_79) 1985; 161 |
References_xml | – volume: 86 start-page: 9677 year: 1989 ident: p_11 article-title: A gene required for transfer of T-DNA to plants encodes an ATPase with autophosphorylating activity publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.86.24.9677 contributor: fullname: Christie P. J. – volume: 32 start-page: 157 year: 1994 ident: p_28 article-title: The virulence system of Agrobacterium tumefaciens. Annu publication-title: Rev. Phytopathol. doi: 10.1146/annurev.py.32.090194.001105 contributor: fullname: Hooykaas P. J. J. – volume: 123 start-page: 255 year: 1975 ident: p_75 article-title: Plasmid required for virulence of Agrobacterium tumefaciens publication-title: J. Bacteriol. doi: 10.1128/jb.123.1.255-264.1975 contributor: fullname: Watson B. – volume: 267 start-page: 5339 year: 1992 ident: p_69 article-title: The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)42771-8 contributor: fullname: Traxler B. – volume: 174 start-page: 7661 year: 1992 ident: p_1 article-title: MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins publication-title: J. Bacteriol. doi: 10.1128/jb.174.23.7661-7669.1992 contributor: fullname: Allaoui A. – volume: 171 start-page: 1616 year: 1989 ident: p_78 article-title: A protein required for transcriptional regulation of Agrobacterium virulence genes spans the cytoplasmic membrane publication-title: J. Bacteriol. doi: 10.1128/jb.171.3.1616-1622.1989 contributor: fullname: Winans S. C. – volume: 63 start-page: 3227 year: 1995 ident: p_34 article-title: Localization of the promoter for the ptl genes of Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin publication-title: Infect. Immun. doi: 10.1128/IAI.63.8.3227-3230.1995 contributor: fullname: Kotob S. I. – volume: 90 start-page: 2970 year: 1993 ident: p_76 article-title: Molecular characterization of an operon required for pertussis toxin secretion publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.90.7.2970 contributor: fullname: Weiss A. A. – volume: 43 start-page: 465 year: 1992 ident: p_80 article-title: Chronicles from the Agrobacterium-plant cell DNA transfer story. Annu publication-title: Rev. Plant Physiol. Plant Mol. Biol. doi: 10.1146/annurev.pp.43.060192.002341 contributor: fullname: Zambryski P. C. – volume: 256 start-page: 1324 year: 1992 ident: p_2 article-title: Conjugative transfer by the virulence system of Agrobacterium tumefaciens publication-title: Science doi: 10.1126/science.256.5061.1324 contributor: fullname: Beijersbergen A. – volume: 4 start-page: 1616 year: 1996 ident: p_77 article-title: Adaptation of a conjugal transfer system for the export of pathogenic macromolecules publication-title: Trends Microbiol. doi: 10.1016/0966-842X(96)81513-7 contributor: fullname: Winans S. C. – volume: 175 start-page: 5233 year: 1993 ident: p_67 article-title: Subcellular localization of seven VirB proteins of Agrobacterium tumefaciens: implications for the formation of a T-DNA transport structure publication-title: J. Bacteriol. doi: 10.1128/JB.175.16.5233-5241.1993 contributor: fullname: Thorstenson Y. R. – volume: 107 start-page: 1041 year: 1995 ident: p_81 article-title: Transfer of T-DNA from Agrobacterium to the plant cell publication-title: Plant Physiol. (Bethesda) doi: 10.1104/pp.107.4.1041 contributor: fullname: Zupan J. R. – volume: 318 start-page: 624 year: 1985 ident: p_60 article-title: Identification of the signal molecules produced by wounded plant cells that activate T-DNA transfer in Agrobacterium tumefaciens publication-title: Nature (London) doi: 10.1038/318624a0 contributor: fullname: Stachel S. E. – volume: 57 start-page: 995 year: 1993 ident: p_18 article-title: ABC transporters: bacterial exporters publication-title: Microbiol. Rev. doi: 10.1128/mr.57.4.995-1017.1993 contributor: fullname: Fath M. J. – volume: 77 start-page: 321 year: 1994 ident: p_40 article-title: Common mechanisms in bacterial conjugation and Ti-mediated T-DNA transfer to plant cells publication-title: Cell doi: 10.1016/0092-8674(94)90146-5 contributor: fullname: Lessl M. – volume: 34 start-page: 61 year: 1991 ident: p_41 article-title: Analysis of membrane protein topology using alkaline phosphatase and ~-galactosidase gene fusions publication-title: Methods Cell Biol. doi: 10.1016/S0091-679X(08)61676-3 contributor: fullname: Manoil C. – volume: 90 start-page: 11538 year: 1993 ident: p_48 article-title: Site-specific cleavage and joining of single-stranded DNA by VirD2 protein of Agrobacterium tumefaciens Ti plasmids: analogy to bacterial conjugation publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.90.24.11538 contributor: fullname: Pansegrau W. – volume: 171 start-page: 5830 year: 1989 ident: p_70 article-title: Construction, expression, and localization of a CycA::PhoA fusion protein in Rhodobacter sphaeroides and Escherichia coli publication-title: J. Bacteriol. doi: 10.1128/jb.171.11.5830-5839.1989 contributor: fullname: Varga A. R. – volume: 82 start-page: 8129 year: 1985 ident: p_42 article-title: TnphoA: a transposon probe for protein export signals publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.82.23.8129 contributor: fullname: Manoil C. – volume: 328 start-page: 172 year: 1987 ident: p_8 article-title: The mob and oriT mobilization functions of a bacterial plasmid promote its transfer to plants publication-title: Nature (London) doi: 10.1038/328172a0 contributor: fullname: Buchanan-Wollaston V. – volume: 4 start-page: 1153 year: 1990 ident: p_58 article-title: Characterization of the virB operon of an Agrobacterium tumefaciens Ti plasmid: nucleotide sequence and protein analysis publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1990.tb00690.x contributor: fullname: Shirasu K. – volume: 176 start-page: 3646 year: 1994 ident: p_5 article-title: Genetic complementation analysis of the Agrobacterium tumefaciens virB operon: virB2 through virB11 are essential virulence genes publication-title: J. Bacteriol. doi: 10.1128/JB.176.12.3646-3660.1994 contributor: fullname: Berger B. R. – volume: 14 start-page: 3365 year: 1995 ident: p_44 article-title: A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane publication-title: EMBO J. doi: 10.1002/j.1460-2075.1995.tb07342.x contributor: fullname: Matsuyama S. – volume: 245 start-page: 704 year: 1994 ident: p_22 article-title: An essential virulence protein of Agrobacterium tumefaciens, VirB4, requires an intact mononucleotide binding domain to function in transfer of T-DNA publication-title: Mol. Gen. Genet. doi: 10.1007/BF00297277 contributor: fullname: Fullner K. J. – volume: 90 start-page: 2925 year: 1993 ident: p_49 article-title: Relaxase (TraI) of IncP~ plasmid RP4 catalyzes a site-specific cleaving-joining reaction of singlestranded DNA publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.90.7.2925 contributor: fullname: Pansegrau W. – volume: 173 start-page: 1139 year: 1991 ident: p_9 article-title: Controlled expression of the transcriptional activator gene virG in Agrobacterium tumefaciens by using the Escherichia coli lac promoter publication-title: J. Bacteriol. doi: 10.1128/JB.173.3.1139-1144.1991 contributor: fullname: Chen C. – volume: 266 start-page: 16458 year: 1991 ident: p_24 article-title: The protein sequence responsible for lipoprotein localization in Escherichia coli exhibits remarkable specificity publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)55322-9 contributor: fullname: Gennity J. M. – ident: p_54 – volume: 174 start-page: 2095 year: 1992 ident: p_25 article-title: Structural determinants in addition to the amino-terminal sorting sequence influence membrane localization of Escherichia coli lipoproteins publication-title: J. Bacteriol. doi: 10.1128/jb.174.7.2095-2101.1992 contributor: fullname: Gennity J. M. – volume: 175 start-page: 1723 year: 1993 ident: p_4 article-title: The Agrobacterium tumefaciens virB4 gene product is an essential virulence protein requiring an intact nucleoside triphosphate-binding domain publication-title: J. Bacteriol. doi: 10.1128/jb.175.6.1723-1734.1993 contributor: fullname: Berger B. R. – volume: 32 start-page: 212 year: 1994 ident: p_3 article-title: Localization and topology of VirB proteins of Agrobacterium tumefaciens publication-title: Plasmid doi: 10.1006/plas.1994.1057 contributor: fullname: Beijersbergen A. – volume: 125 start-page: 183 year: 1986 ident: p_16 article-title: Production and release of cloacin DF13 and related colicins publication-title: Curr. Top. Microbiol. Immunol. contributor: fullname: De Graaf F. K. – ident: p_30 – volume: 172 start-page: 5187 year: 1990 ident: p_73 article-title: Complementation analysis of Agrobacterium tumefaciens Ti plasmid virB genes by use of a vir promoter expression vector: virB9, virB10, and virB11 are essential virulence genes publication-title: J. Bacteriol. doi: 10.1128/JB.172.9.5187-5199.1990 contributor: fullname: Ward J. E. – volume: 171 start-page: 511 year: 1989 ident: p_31 article-title: Sequence of an osmotically inducible lipoprotein gene publication-title: J. Bacteriol. doi: 10.1128/jb.171.1.511-520.1989 contributor: fullname: Jung J. U. – volume: 178 start-page: 3168 year: 1996 ident: p_19 article-title: The Agrobacterium tumefaciens VirB7 lipoprotein is required for stabilization of VirB proteins during assembly of the T-complex transport apparatus publication-title: J. Bacteriol. doi: 10.1128/JB.178.11.3168-3176.1996 contributor: fullname: Fernandez D. – volume: 169 start-page: 5692 year: 1987 ident: p_65 article-title: Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome publication-title: J. Bacteriol. doi: 10.1128/JB.169.12.5692-5699.1987 contributor: fullname: Takase I. – volume: 263 start-page: 5804 year: 1988 ident: p_71 article-title: Characterization of the virB operon from an Agrobacterium tumefaciens Ti plasmid publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)60637-4 contributor: fullname: Ward J. E. – volume: 177 start-page: 4881 year: 1995 ident: p_20 article-title: Interactions of VirB9, -10, and -11 with the membrane fraction of Agrobacterium tumefaciens: solubility studies provide evidence for tight associations publication-title: J. Bacteriol. doi: 10.1128/JB.177.17.4881-4889.1995 contributor: fullname: Finberg K. E. – volume: 195 start-page: 159 year: 1984 ident: p_46 article-title: Restoration of virulence of vir region mutants of Agrobacterium tumefaciens strain B6S3 by coinfection with normal and mutant Agrobacterium strains publication-title: Mol. Gen. Genet. doi: 10.1007/BF00332739 contributor: fullname: Otten L. – volume: 88 start-page: 9603 year: 1991 ident: p_64 article-title: Membrane topology analysis of Escherichia coli mannitol permease by using a nesteddeletion method to create mtlA-phoA fusions publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.88.21.9603 contributor: fullname: Sugiyama J. E. – volume: 173 start-page: 5523 year: 1991 ident: p_7 article-title: A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome publication-title: J. Bacteriol. doi: 10.1128/JB.173.17.5523-5531.1991 contributor: fullname: Bouvier J. – volume: 12 start-page: 17 year: 1994 ident: p_33 article-title: Promiscuous DNA transfer system of Agrobacterium tumefaciens: role of the virB operon in sex pilus assembly and synthesis publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1994.tb00990.x contributor: fullname: Kado C. I. – volume: 261 start-page: 8953 year: 1986 ident: p_10 article-title: Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)84474-5 contributor: fullname: Choi D. – volume: 161 start-page: 402 year: 1985 ident: p_79 article-title: Conjugal transfer system of the IncN plasmid pKM101 publication-title: J. Bacteriol. doi: 10.1128/JB.161.1.402-410.1985 contributor: fullname: Winans S. C. – volume: 4 start-page: 59 year: 1990 ident: p_53 article-title: Analysis of the subcellular location of pullulanase produced by Escherichia coli carrying the pulA gene from Klebsiella pneumoniae strain UNF5023 publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1990.tb02015.x contributor: fullname: Pugsley A. P. – volume: 8 start-page: 429 year: 1993 ident: p_13 article-title: Pertussis toxin export requires accessory genes located downstream from the pertussis toxin operon publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1993.tb01587.x contributor: fullname: Covacci A. – volume: 255 start-page: 3707 year: 1980 ident: p_29 article-title: Accumulation of glyceride-containing precursors of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)85762-9 contributor: fullname: Hussain M. – volume: 166 start-page: 368 year: 1987 ident: p_56 article-title: Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa publication-title: Anal. Biochem. doi: 10.1016/0003-2697(87)90587-2 contributor: fullname: Schagger H. – ident: p_36 – ident: p_55 – ident: p_59 – volume: 170 start-page: 2659 year: 1988 ident: p_12 article-title: The Agrobacterium tumefaciens virE2 gene product is a single-stranded-DNAbinding protein that associates with T-DNA publication-title: J. Bacteriol. doi: 10.1128/jb.170.6.2659-2667.1988 contributor: fullname: Christie P. J. – volume: 167 start-page: 1083 year: 1986 ident: p_17 article-title: Fractionation of Rhizobium leguminosarum cells into outer membrane, cytoplasmic membrane, periplasmic, and cytoplasmic components publication-title: J. Bacteriol. doi: 10.1128/JB.167.3.1083-1085.1986 contributor: fullname: de Maagd R. A. – volume: 175 start-page: 1543 year: 1993 ident: p_47 article-title: Escherichia coli SecB, SecA, and SecY proteins are required for expression and membrane insertion of the bacteriocin release protein, a small lipoprotein publication-title: J. Bacteriol. doi: 10.1128/jb.175.5.1543-1547.1993 contributor: fullname: Oudega B. – volume: 177 start-page: 2892 year: 1995 ident: p_43 article-title: The dnaA gene of Rhizobium meliloti lies within an unusual gene arrangement publication-title: J. Bacteriol. doi: 10.1128/JB.177.10.2892-2900.1995 contributor: fullname: Margolin W. – volume: 58 start-page: 162 year: 1994 ident: p_21 article-title: Analysis of the sequence and gene products of the transfer region of the F sex factor publication-title: Microbiol. Rev. doi: 10.1128/MR.58.2.162-210.1994 contributor: fullname: Frost L. S. – volume: 177 start-page: 4779 year: 1995 ident: p_26 article-title: Bacterial conjugation mediated by plasmid RP4: RSF1010 mobilization, donor-specific phage production, and pilus production require the same Tra2 core components of a proposed DNA transport complex publication-title: J. Bacteriol. doi: 10.1128/JB.177.16.4779-4791.1995 contributor: fullname: Haase J. – volume: 14 start-page: 655 year: 1994 ident: p_50 article-title: Common ancestry between IncN conjugal transfer genes and macromolecular export systems of plant and animal pathogens publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1994.tb01304.x contributor: fullname: Pohlman R. F. – volume: 57 start-page: 50 year: 1993 ident: p_52 article-title: The complete general secretory pathway in gram-negative bacteria publication-title: Microbiol. Rev. doi: 10.1128/mr.57.1.50-108.1993 contributor: fullname: Pugsley A. P. – volume: 16 start-page: 4621 year: 1988 ident: p_66 article-title: Analysis of the complete nucleotide sequence of the Agrobacterium tumefaciens virB operon publication-title: Nucleic Acids Res. doi: 10.1093/nar/16.10.4621 contributor: fullname: Thompson D. V. – volume: 267 start-page: 20471 year: 1992 ident: p_38 article-title: Sequence similarities between the RP4 Tra2 and the Ti VirB region strongly support the conjugation model for T-DNA transfer publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)88726-4 contributor: fullname: Lessl M. – ident: p_45 – volume: 174 start-page: 7982 year: 1992 ident: p_37 article-title: Interactions of Escherichia coli membrane lipoproteins with the murein sacculus publication-title: J. Bacteriol. doi: 10.1128/jb.174.24.7982-7988.1992 contributor: fullname: Leduc M. – volume: 5 start-page: 1445 year: 1986 ident: p_61 article-title: The genetic and transcriptional organization of the vir region of the A6 Ti-plasmid of Agrobacterium tumefaciens publication-title: EMBO J. doi: 10.1002/j.1460-2075.1986.tb04381.x contributor: fullname: Stachel S. E. – volume: 176 start-page: 1711 year: 1994 ident: p_68 article-title: The essential virulence protein VirB8 localizes to the inner membrane of Agrobacterium tumefaciens publication-title: J. Bacteriol. doi: 10.1128/JB.176.6.1711-1717.1994 contributor: fullname: Thorstenson Y. R. – ident: p_14 – volume: 172 start-page: 5200 year: 1990 ident: p_74 article-title: Identification of a VirB10 protein aggregate in the inner membrane of Agrobacterium tumefaciens publication-title: J. Bacteriol. doi: 10.1128/JB.172.9.5200-5210.1990 contributor: fullname: Ward J. E. – ident: p_32 doi: 10.1007/978-1-4757-9357-4_9 – volume: 221 start-page: 256 year: 1990 ident: p_35 article-title: The virB operon of Agrobacterium tumefaciens pTiC58 encodes 11 open reading frames publication-title: Mol. Gen. Genet. doi: 10.1007/BF00261729 contributor: fullname: Kuldau G. A. – volume: 6 start-page: 3531 year: 1987 ident: p_15 article-title: Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase publication-title: EMBO J. doi: 10.1002/j.1460-2075.1987.tb02679.x contributor: fullname: Enfert C. – volume: 177 start-page: 4890 year: 1995 ident: p_6 article-title: Inhibition of VirBmediated transfer of diverse substrates from Agrobacterium tumefaciens by the IncQ plasmid RSF1010 publication-title: J. Bacteriol. doi: 10.1128/JB.177.17.4890-4899.1995 contributor: fullname: Binns A. N. – volume: 111 start-page: 287 year: 1993 ident: p_57 article-title: Membrane location of the Ti plasmid VirB proteins involved in the biosynthesis of a pilin-like conjugative structure on Agrobacterium tumefaciens publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.1993.tb06400.x contributor: fullname: Shirasu K. – volume: 175 start-page: 6415 year: 1993 ident: p_39 article-title: The mating pair formation system of plasmid RP4 defined by RSF1010 mobilization and donor-specific phage propagation publication-title: J. Bacteriol. doi: 10.1128/JB.175.20.6415-6425.1993 contributor: fullname: Lessl M. – volume: 177 start-page: 27 year: 1995 ident: p_63 article-title: Agrobacterium tumefaciens VirB11 protein requires a consensus nucleotide binding site for function in virulence publication-title: J. Bacteriol. doi: 10.1128/jb.177.1.27-36.1995 contributor: fullname: Stephens K. M. – volume: 22 start-page: 451 year: 1990 ident: p_27 article-title: Lipoproteins in bacteria publication-title: J. Bioenerg. Biomembr. doi: 10.1007/BF00763177 contributor: fullname: Hayashi S. – volume: 265 start-page: 4768 year: 1990 ident: p_72 article-title: Characterization of the virB operon from an Agrobacterium tumefaciens Ti plasmid publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)39628-0 contributor: fullname: Ward J. E. – volume: 6 start-page: 857 year: 1987 ident: p_62 article-title: Activation of Agrobacterium tumefaciens vir gene expression generates multiple singlestranded T-strand molecules from the pTiA6 T-region: requirement for 5~ virD gene products publication-title: EMBO J. doi: 10.1002/j.1460-2075.1987.tb04831.x contributor: fullname: Stachel S. E. – volume: 27 start-page: 143 year: 1981 ident: p_23 article-title: Genetic analysis of crown gall: fine structure map of the T-DNA by site-directed mutagenesis publication-title: Cell doi: 10.1016/0092-8674(81)90368-8 contributor: fullname: Garfinkel D. J. – volume: 9 start-page: 1061 year: 1993 ident: p_51 article-title: The role of the lipoprotein sorting signal (aspartate ~2) in pullulanase secretion publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.1993.tb01235.x contributor: fullname: Poquet I. |
SSID | ssj0014452 |
Score | 1.8445264 |
Snippet | The Agrobacterium tumefaciens virB7 gene product contains a typical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of... Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... The Agrobacterium tumefaciens virB7 gene product is topologically configured as a monotopic protein, with its amino terminus anchored predominantly to the... |
SourceID | pubmedcentral proquest crossref pubmed highwire fao |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 3156 |
SubjectTerms | ACIDE PALMITIQUE ACIDO PALMITICO ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE AGROBACTERIUM TUMEFACIENS Agrobacterium tumefaciens - chemistry BACTERIA Bacterial Proteins - analysis Bacterial Proteins - metabolism Bacteriology Base Sequence BIOCHIMIE Biological Transport BIOQUIMICA Flowers & plants FOSFATASA ALCALINA GENE GENES GENIE BIOCHIMIQUE INGENIERIA BIOQUIMICA LIPOPROTEINAS LIPOPROTEINE Lipoproteins - analysis MEMBRANAS CELULARES MEMBRANE CELLULAIRE Membrane Proteins - analysis Membranes Molecular Sequence Data Nucleoproteins - metabolism PEPTIDASAS PEPTIDASE PHOSPHATASE ALCALINE PROTEASAS PROTEASE PROTEINAS PROTEINE Proteins PROTEOLISIS PROTEOLYSE REACCIONES QUIMICAS REACTION CHIMIQUE Recombinant Fusion Proteins - metabolism Virulence Factors |
Title | The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface |
URI | http://jb.asm.org/content/178/11/3156.abstract https://www.ncbi.nlm.nih.gov/pubmed/8655494 https://www.proquest.com/docview/227067798/abstract/ https://search.proquest.com/docview/15608462 https://search.proquest.com/docview/78054754 https://pubmed.ncbi.nlm.nih.gov/PMC178066 |
Volume | 178 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwELXYSpV6QVCoSAvFB47N7iZx7PhYKkqFVIREV9qbZTt2SdV8aJOg8r_4gYydZNWt4MLN0mSceGcmfrOZeUboAzOa53xpQ8CqJiTMpiE3JguNdPxoCnZg3y52_ZVerciXdboem8Lasayy0qqYV_flvCp--NrKptSLqU5s8e36ImIZ7JSLGZqxJJky9PHLASHpyBAeQSDzZKreibPFnZqDJowhUU1p6HrAXbMePUD7rj2TcLKzOc2srB_RBv8Ngj6tpHy0NV2-QM9HTInPh2d_iZ6Z6hDtD6dM_nqFfoMr4PPbDUSuZ2buS9zBG8lKF9Yt_llsPjIMfmRwM9C_nmHphk3dmhy7mvO6ghvj2mJAi_gm9GXo5gF3EzE6lo2nEO_bM1y0oF2aErLwyoRytD5MdF80tWeFKCpsHobJZeendGzLDcD4stC47TfwZOY1Wl1-urm4CsfDGkKdsqQLFQR_DvKltLlUNmNaxwDFNKU6AZiX59RygB9xHiWSZKATmShPpYX8i3EFyOEI7VWwnDcIcyOZBdxJydISzSynmVWcWRtbZSixAYomK4lm4OQQPpeJM3GnBNgYxsLZWDgbC2fjAB2COYW8hVenWH3nFGAV5wE6mcwrYJFPtEE6WVyMkd2KOGaOdI9nAXq_lUJIuu8s8LvWfStcczrAuvjfV7iDJAhLSYCOBv_ZrmN0xADRHcfayh0b-K4EgsSzgg9Bcfy_iifoYChId38wvUV73aY37wBvdeoUzT6vo1MfZn8AweQsvQ |
link.rule.ids | 230,315,733,786,790,891,27957,27958,53827,53829 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFLbY0MReuAwmwoD5gcelXVLHjh_HxFRgnZBopb1ZtmNvGctFTYIGv4sfyHEu1VrBA7xZOrXVk34-_k5zzmeE3jGjecKPrQ9c1fiE2cjnxsS-kU4fTcEJ3LaLzS7odEE-XUaXfVNY1ZdV5lqlo_w2G-XpdVtbWWZ6PNSJjb_MTgMWw0k53kIPYbuGbMjR-3cHhES9RngAW5lPhvqdMB7fqBHMhTGkqhH1XRe4a9eju2jHNWgSTtaOpy0ri3vCwX8ioZu1lPcOp7MnaDG41dWkfBs1tRrpnxuKj__q91P0uGer-KSzPkMPTL6Hdrr7K388R78AZPjkagkxodV8bjJcQ6yz0gWMCn9Pl-8ZBoQaXHbCskdYumFZVCbBrpq9yMEhXFgMPBTP_bbA3dzhepBcx7Jsxcmb6ginFczOTAb5fW582eMKFrpNy6LVm0hzbO66xWXdLul0nEtIELJU46pZwjczL9Di7MP8dOr310D4OmKT2lcQVhKwH0ubSGVjpnUIJE9TqidAIJOEWg7EJkyCiSQxzAlMkETSQmbHuAJOso-2c3DnJcLcSGaB0VJybIlmltPYKs6sDa0ylFgPBcOvL8pO7UO0WVIYixsl4PnDWDjsCIcd4bDjoT2AiZBXEJTF4iunQNg499DBABsBTm7MBuuAJNHHjEqEIXNyfjz20OHKCpvdvcGB51o0lXBt70AYw79_wl1RQVhEPLTf4XLlRw9wD9E1wK7sTmd83QIwbPXGO9i9-t-Jh-jRdD47F-cfLz4foN2u7N39jfUabdfLxrwBVlert-0m_g2X_U2P |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELbaoqJeeBQqQoH6wLHZ3WQdOz6Wwqo8WlWiK5WTZSd2SWke2iSo8Lv4gYydZNVdwaU3SxNbO7ufx99sZj4j9JbphKd8YnzgqtonzEQ-1zr2tbT6aApOYNcudnpGT-bk02V0uYHioRfGFe0nKhsVN_moyL672soqT8ZDndj4_PQ4YDGclOMqNeNN9AC2bMiHPL1_f0BI1OuEB7Cd-XSo4Qnj8bUawXwYQ7oaUd92gtuWPbqDtm2TJuFk5YjaNLK8Ix78LyK6Xk9554CaPUbfBte6upQfo7ZRo-T3murjfXx_gh71rBUfdU88RRu62EXb3T2Wv56hPwA2fHS1gNjgtJ_bHDcQ84y0gaPGP7PFO4YBqRpXncDsIZZ2WJW1TrGtai8LcAqXBgMfxRe-K3TXt7gZpNexrJxIeVsf4qyG2bnOIc8vtC97fMFCN1lVOt2JrMD6tltcNm5Jq-dcQaKQZwmu2wV8Mv0czWcfLo5P_P46CD-J2LTxFYSXFOwTaVKpTMySJASyl1CaTIFIpik1HAhOmAZTSWKYE-ggjaSBDI9xBdxkD20V4M4LhLmWzACzpWRiSMIMp7FRnBkTGqUpMR4KBgSIqlP9EC5bCmNxrQT8BjAWFj_C4kdY_HhoF6Ai5BUEZzH_yikQN849tD9AR4CTa7PBOqBJ9LGjFmHIrKwfjz10sLTCprdvcuB7Ldta2PZ3II7h_5-wV1UQFhEP7XXYXPrRg9xDdAW0S7vVG1-1ABSd7ngHvZf3nXiAHp6_n4kvH88-76Odrvrd_pv1Cm01i1a_BnLXqDduH_8F24dQDw |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+Agrobacterium+tumefaciens+virB7+gene+product%2C+a+proposed+component+of+the+T-complex+transport+apparatus%2C+is+a+membrane-associated+lipoprotein+exposed+at+the+periplasmic+surface&rft.jtitle=Journal+of+bacteriology&rft.au=Fernandez%2C+D&rft.au=Dang%2C+T+A&rft.au=Spudich%2C+G+M&rft.au=Zhou%2C+X+R&rft.date=1996-06-01&rft.issn=0021-9193&rft.volume=178&rft.issue=11&rft.spage=3156&rft.epage=3167&rft_id=info:doi/10.1128%2Fjb.178.11.3156-3167.1996&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9193&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9193&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9193&client=summon |