Identification and Transcriptional Control of the Genes Encoding the Caulobacter crescentus ClpXP Protease

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 & Commer...

Full description

Saved in:
Bibliographic Details
Published inJournal of Bacteriology Vol. 181; no. 10; pp. 3039 - 3050
Main Authors Østerås, Magne, Stotz, Agathe, Nuoffer, Stefanie Schmid, Jenal, Urs
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.05.1999
Subjects
Online AccessGet full text
ISSN0021-9193
1067-8832
1098-5530
DOI10.1128/JB.181.10.3039-3050.1999

Cover

Abstract 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       
AbstractList 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 region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of the C. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram-negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP).
The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of the C. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram-negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP). The C. crescentus clpX gene was shown by complementation analysis to be functional in Escherichia coli . However, clpX from E. coli was not able to substitute for the essential nature of the clpX gene in C. crescentus . The clpP and clpX genes are separated on the C. crescentus chromosome by an open reading frame pointing in the opposite direction from the clp genes, and transcription of clpP and clpX was found to be uncoupled. clpP is transcribed as a monocistronic unit with a promoter (P P1 ) located immediately upstream of the 5′ end of the gene and a terminator structure following its 3′ end. P P1 is under heat shock control and is induced upon entry of the cells into the stationary phase. At least three promoters for clpX (P X1 , P X2 , and P X3 ) were mapped in the clpP-clpX intergenic region. In contrast to P P1 , the clpX promoters were found to be downregulated after heat shock but were also subject to growth phase control. In addition, the clpP and clpX promoters showed different activity patterns during the cell cycle. Together, these results demonstrate that the genes coding for the peptidase and the regulatory subunits of the ClpXP protease are under independent transcriptional control in C. crescentus . Determination of the numbers of ClpP and ClpX molecules per cell suggested that ClpX is the limiting component compared with ClpP.
The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of the C. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram- negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP). The C. crescentus clpX gene was shown by complementation analysis to be functional in Escherichia coli. However, clpX from E. coli was not able to substitute for the essential nature of the clpX gene in C. crescentus. The clpP and clpX genes are separated on the C. crescentus chromosome by an open reading frame pointing in the opposite direction from the clp genes, and transcription of clpP and clpX was found to be uncoupled. clpP is transcribed as a monocistronic unit with a promoter (P sub(P1)) located immediately upstream of the 5' end of the gene and a terminator structure following its 3' end. P sub(P1) is under heat shock control and is induced upon entry of the cells into the stationary phase. At least three promoters for clpX (P sub(X1), P sub(X2), and P sub(X3)) were mapped in the clpP-clpX intergenic region. In contrast to P sub(P1), the clpX promoters were found to be downregulated after heat shock but were also subject to growth phase control. In addition, the clpP and clpX promoters showed different activity patterns during the cell cycle. Together, these results demonstrate that the genes coding for the peptidase and the regulatory subunits of the ClpXP protease are under independent transcriptional control in C. crescentus. Determination of the numbers of ClpP and ClpX molecules per cell suggested that ClpX is the limiting component compared with ClpP.
The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of the C. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram-negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP). The C. crescentus clpX gene was shown by complementation analysis to be functional in Escherichia coli. However, clpX from E. coli was not able to substitute for the essential nature of the clpX gene in C. crescentus. The clpP and clpX genes are separated on the C. crescentus chromosome by an open reading frame pointing in the opposite direction from the clp genes, and transcription of clpP and clpX was found to be uncoupled. clpP is transcribed as a monocistronic unit with a promoter (PP1) located immediately upstream of the 5' end of the gene and a terminator structure following its 3' end. PP1 is under heat shock control and is induced upon entry of the cells into the stationary phase. At least three promoters for clpX (PX1, PX2, and PX3) were mapped in the clpP-clpX intergenic region. In contrast to PP1, the clpX promoters were found to be downregulated after heat shock but were also subject to growth phase control. In addition, the clpP and clpX promoters showed different activity patterns during the cell cycle. Together, these results demonstrate that the genes coding for the peptidase and the regulatory subunits of the ClpXP protease are under independent transcriptional control in C. crescentus. Determination of the numbers of ClpP and ClpX molecules per cell suggested that ClpX is the limiting component compared with ClpP.
The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of the C. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram-negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP). The C. crescentus clpX gene was shown by complementation analysis to be functional in Escherichia coli. However, clpX from E. coli was not able to substitute for the essential nature of the clpX gene in C. crescentus. The clpP and clpX genes are separated on the C. crescentus chromosome by an open reading frame pointing in the opposite direction from the clp genes, and transcription of clpP and clpX was found to be uncoupled. clpP is transcribed as a monocistronic unit with a promoter (PP1) located immediately upstream of the 5' end of the gene and a terminator structure following its 3' end. PP1 is under heat shock control and is induced upon entry of the cells into the stationary phase. At least three promoters for clpX (PX1, PX2, and PX3) were mapped in the clpP-clpX intergenic region. In contrast to PP1, the clpX promoters were found to be downregulated after heat shock but were also subject to growth phase control. In addition, the clpP and clpX promoters showed different activity patterns during the cell cycle. Together, these results demonstrate that the genes coding for the peptidase and the regulatory subunits of the ClpXP protease are under independent transcriptional control in C. crescentus. Determination of the numbers of ClpP and ClpX molecules per cell suggested that ClpX is the limiting component compared with ClpP.The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino acid sequences of the C. crescentus ClpP and ClpX proteins with those of their homologues from several gram-positive and gram-negative bacteria revealed stronger conservation for the ATPase regulatory subunit (ClpX) than for the peptidase subunit (ClpP). The C. crescentus clpX gene was shown by complementation analysis to be functional in Escherichia coli. However, clpX from E. coli was not able to substitute for the essential nature of the clpX gene in C. crescentus. The clpP and clpX genes are separated on the C. crescentus chromosome by an open reading frame pointing in the opposite direction from the clp genes, and transcription of clpP and clpX was found to be uncoupled. clpP is transcribed as a monocistronic unit with a promoter (PP1) located immediately upstream of the 5' end of the gene and a terminator structure following its 3' end. PP1 is under heat shock control and is induced upon entry of the cells into the stationary phase. At least three promoters for clpX (PX1, PX2, and PX3) were mapped in the clpP-clpX intergenic region. In contrast to PP1, the clpX promoters were found to be downregulated after heat shock but were also subject to growth phase control. In addition, the clpP and clpX promoters showed different activity patterns during the cell cycle. Together, these results demonstrate that the genes coding for the peptidase and the regulatory subunits of the ClpXP protease are under independent transcriptional control in C. crescentus. Determination of the numbers of ClpP and ClpX molecules per cell suggested that ClpX is the limiting component compared with ClpP.
Author Magne Østerås
Stefanie Schmid Nuoffer
Urs Jenal
Agathe Stotz
AuthorAffiliation Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
AuthorAffiliation_xml – name: Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
Author_xml – sequence: 1
  givenname: Magne
  surname: Østerås
  fullname: Østerås, Magne
  organization: <!--label omitted: 1-->Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
– sequence: 2
  givenname: Agathe
  surname: Stotz
  fullname: Stotz, Agathe
  organization: <!--label omitted: 1-->Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
– sequence: 3
  givenname: Stefanie Schmid
  surname: Nuoffer
  fullname: Nuoffer, Stefanie Schmid
  organization: <!--label omitted: 1-->Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
– sequence: 4
  givenname: Urs
  surname: Jenal
  fullname: Jenal, Urs
  organization: <!--label omitted: 1-->Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
BackLink https://www.ncbi.nlm.nih.gov/pubmed/10322004$$D View this record in MEDLINE/PubMed
BookMark eNqFkk1v1DAQhq2qiG4Lf6GyOHDL4o8ktiWERKNSWlWih1bqzZo4zq5XWXuxExD_HqddoPTS02hmnhnPeN5jdOiDtwhhSpaUMvnh6mxJJV1mlxOuCk6qnFBKHaAFJbUopOTsEC0IYbRQVPEjdJzShhBalhV7jY4o4YwRUi7Q5rKzfnS9MzC64DH4Dt9G8MlEt5sjMOAm-DGGAYcej2uLL6y3CZ97EzrnVw-hBqYhtGBGG7GJNpncc0q4GXb3N_gmhtFCsm_Qqx6GZN_u7Qm6-3J-23wtrr9dXDafrwtTKjUW0Fay63lvy5YqCR0IqFtgFfQt4VATyZhhdckFhbLtSCtUzmZDheFKyI6foI-PfXdTu7XdPEuEQe-i20L8pQM4_X_Gu7VehR9acVHJXP5-Xx7D98mmUW9dXmgYwNswJV0rUUpB2IsgFYzTshIZfPcM3IQp5p9NmjFB6nwmlaHTp1P_HffPqTLw6REwMaQUba-NGx-OlpdwQwb1rA19daazNmZ31oaetaFnbeQG8lmDf2-8WLrfYO1W658uWg1pqzftU5z_Biewyr0
CODEN JOBAAY
CitedBy_id crossref_primary_10_1128_JB_184_6_1794_1795_2002
crossref_primary_10_1128_JB_186_15_4960_4971_2004
crossref_primary_10_3389_fmolb_2017_00028
crossref_primary_10_1016_S1369_5274_00_00071_0
crossref_primary_10_1128_JB_186_7_2200_2205_2003
crossref_primary_10_1093_nar_gkw843
crossref_primary_10_1016_j_jprot_2016_04_004
crossref_primary_10_1111_j_1574_6976_2000_tb00538_x
crossref_primary_10_1128_JB_186_1_179_191_2004
crossref_primary_10_1073_pnas_0701776104
crossref_primary_10_1007_s00438_002_0783_1
crossref_primary_10_1111_mmi_12241
crossref_primary_10_1016_j_cell_2005_12_033
crossref_primary_10_1101_gad_222679_113
crossref_primary_10_1046_j_1365_2958_2002_02887_x
crossref_primary_10_1177_10454411010120030101
crossref_primary_10_1128_IAI_73_8_4864_4878_2005
crossref_primary_10_1128_AEM_00275_18
crossref_primary_10_3389_fmolb_2021_682967
crossref_primary_10_1046_j_1365_2958_2001_02238_x
crossref_primary_10_1038_nbt1294
crossref_primary_10_1111_j_1751_1097_2008_00444_x
crossref_primary_10_1371_journal_pgen_1004831
crossref_primary_10_1007_s00284_020_02093_1
crossref_primary_10_1371_journal_pcbi_1000463
crossref_primary_10_1016_j_jmb_2009_08_076
crossref_primary_10_1038_ncomms8005
crossref_primary_10_1046_j_1365_2958_2000_02155_x
crossref_primary_10_1016_S1369_5274_00_00145_4
crossref_primary_10_1099_00221287_148_7_2255
Cites_doi 10.1016/S0092-8674(00)80485-7
10.1016/S0092-8674(00)80431-6
10.1002/j.1460-2075.1982.tb01276.x
10.1128/jb.178.7.2094-2101.1996
10.1101/gad.12.6.880
10.1016/S0021-9258(19)38379-6
10.1128/jb.132.1.294-301.1977
10.1002/j.1460-2075.1996.tb00597.x
10.1038/32831
10.1038/nbt1183-784
10.1126/science.7542800
10.1016/S0968-0004(96)10038-4
10.1073/pnas.92.8.3274
10.1128/JB.180.5.1154-1158.1998
10.1093/emboj/17.19.5658
10.1128/jb.177.15.4372-4376.1995
10.1101/gad.10.12.1532
10.1006/jmbi.1995.0400
10.1006/jmbi.1994.1007
10.1016/0076-6879(91)04019-K
10.1128/jb.177.7.1662-1669.1995
10.1128/jb.172.10.6026-6034.1990
10.1099/00221287-138-10-2125
10.1073/pnas.74.12.5463
10.1093/emboj/17.22.6730
10.1101/gad.11.12.1561
10.1128/jb.178.7.1919-1927.1996
10.1128/jb.178.7.1829-1841.1996
10.1016/S0092-8674(00)80502-4
10.1091/mbc.3.8.913
10.1038/31159
10.1038/215588a0
10.1128/br.28.3.231-295.1964
10.1073/pnas.93.3.1210
10.1074/jbc.273.20.12476
10.1093/genetics/136.3.721
10.1002/j.1460-2075.1996.tb00374.x
10.1046/j.1365-2958.1996.396932.x
10.1038/41483
10.1128/JB.180.7.1632-1641.1998
10.1016/S0021-9258(19)38378-4
10.1093/dnares/3.3.109
10.1016/S0021-9258(18)41573-6
10.1101/gad.12.9.1338
10.1038/36786
10.1006/jmbi.1993.1521
10.1002/j.1460-2075.1995.tb07179.x
10.1128/jb.179.3.592-600.1997
10.1126/science.8456303
10.1128/jb.179.2.514-521.1997
10.1101/gad.11.7.815
ContentType Journal Article
Copyright Copyright American Society for Microbiology May 1999
Copyright © 1999, American Society for Microbiology 1999
Copyright_xml – notice: Copyright American Society for Microbiology May 1999
– notice: Copyright © 1999, American Society for Microbiology 1999
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7QL
7TM
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
7X8
5PM
DOI 10.1128/JB.181.10.3039-3050.1999
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
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 CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
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
Genetics Abstracts
CrossRef
Genetics Abstracts
MEDLINE
MEDLINE - Academic

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
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1067-8832
1098-5530
EndPage 3050
ExternalDocumentID PMC93758
42026455
10322004
10_1128_JB_181_10_3039_3050_1999
jb_181_10_3039
Genre Research Support, Non-U.S. Gov't
Journal Article
Feature
GroupedDBID ---
-DZ
-~X
.55
.GJ
0R~
186
18M
1VV
29J
2WC
39C
3O-
4.4
53G
5GY
5RE
5VS
79B
85S
AAGFI
AAYXX
ABPPZ
ACGFO
ACGOD
ACNCT
ACPRK
ADBBV
ADXHL
AENEX
AFFDN
AFFNX
AFRAH
AGVNZ
AI.
AIDAL
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BKOMP
BTFSW
C1A
CITATION
CJ0
CS3
DIK
DU5
E3Z
EBS
EJD
F5P
FRP
GX1
H13
HYE
HZ~
IH2
KQ8
L7B
MVM
NHB
O9-
OHT
OK1
P-S
P2P
PQQKQ
RHI
RNS
RPM
RSF
RXW
TAE
TR2
UHB
UKR
UPT
VH1
W8F
WH7
WOQ
X7M
Y6R
YQT
YR2
YZZ
ZCA
ZCG
ZGI
ZXP
~02
~KM
8WZ
9M8
A6W
ABTAH
AGCDD
AJUXI
CGR
CUY
CVF
ECM
EIF
NPM
P-O
PKN
QZG
RHF
UCJ
VQA
WHG
YIN
ZY4
7QL
7TM
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
7X8
5PM
ID FETCH-LOGICAL-c499t-ab58df3fe4b198ada7a6ba25afb03a60822c264371a4bd0b79ba20b717c3978d3
ISSN 0021-9193
IngestDate Thu Aug 21 18:31:24 EDT 2025
Fri Sep 05 13:49:51 EDT 2025
Fri Sep 05 04:05:31 EDT 2025
Mon Jun 30 08:30:31 EDT 2025
Wed Feb 19 01:18:30 EST 2025
Tue Jul 01 02:56:38 EDT 2025
Thu Apr 24 22:56:20 EDT 2025
Wed May 18 15:54:50 EDT 2016
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 10
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c499t-ab58df3fe4b198ada7a6ba25afb03a60822c264371a4bd0b79ba20b717c3978d3
Notes SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 14
ObjectType-Article-2
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
Corresponding author. Mailing address: Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland. Phone: 41-61-267-21-35. Fax: 41-61-267-21-18. E-mail: jenal@ubaclu.unibas.ch.
OpenAccessLink https://jb.asm.org/content/jb/181/10/3039.full.pdf
PMID 10322004
PQID 227060029
PQPubID 40724
PageCount 12
ParticipantIDs proquest_journals_227060029
proquest_miscellaneous_69748702
crossref_citationtrail_10_1128_JB_181_10_3039_3050_1999
crossref_primary_10_1128_JB_181_10_3039_3050_1999
pubmed_primary_10322004
pubmedcentral_primary_oai_pubmedcentral_nih_gov_93758
proquest_miscellaneous_17231457
highwire_asm_jb_181_10_3039
ProviderPackageCode CITATION
AAYXX
PublicationCentury 1900
PublicationDate 1999-05-01
PublicationDateYYYYMMDD 1999-05-01
PublicationDate_xml – month: 05
  year: 1999
  text: 1999-05-01
  day: 01
PublicationDecade 1990
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: Washington
PublicationTitle Journal of Bacteriology
PublicationTitleAlternate J Bacteriol
PublicationYear 1999
Publisher American Society for Microbiology
Publisher_xml – name: American Society for Microbiology
References e_1_3_2_49_2
Jenal U. (e_1_3_2_20_2) 1995; 71
Wright R. (e_1_3_2_56_2) 1996; 10
e_1_3_2_41_2
e_1_3_2_43_2
Wang J. (e_1_3_2_53_2) 1997; 91
e_1_3_2_24_2
Salser W. (e_1_3_2_42_2) 1967; 215
Levchenko I. (e_1_3_2_29_2) 1997; 91
Kelly A. J. (e_1_3_2_22_2) 1998; 12
Kessel M. (e_1_3_2_23_2) 1995; 250
Domian I. J. (e_1_3_2_7_2) 1997; 90
e_1_3_2_9_2
e_1_3_2_37_2
e_1_3_2_39_2
Gottesman S. (e_1_3_2_13_2) 1998; 12
Wawrzynow A. (e_1_3_2_54_2) 1995; 14
Lehnherr H. (e_1_3_2_27_2) 1993; 233
Jenal U. (e_1_3_2_18_2) 1998; 17
Deckert G. (e_1_3_2_6_2) 1998; 392
Gottesman S. (e_1_3_2_14_2) 1997; 11
e_1_3_2_10_2
e_1_3_2_31_2
e_1_3_2_52_2
e_1_3_2_5_2
e_1_3_2_12_2
Grimaud R. (e_1_3_2_15_2) 1998; 273
e_1_3_2_58_2
e_1_3_2_3_2
e_1_3_2_35_2
Simon R. (e_1_3_2_46_2) 1983; 1
Levchenko I. (e_1_3_2_30_2) 1997; 11
e_1_3_2_48_2
Lehnherr H. (e_1_3_2_28_2) 1995; 92
e_1_3_2_40_2
e_1_3_2_25_2
Laachouch J. E. (e_1_3_2_26_2) 1996; 15
Volker U. (e_1_3_2_51_2) 1992; 138
Stephens C. (e_1_3_2_47_2) 1996; 93
Gober J. W. (e_1_3_2_11_2) 1992; 3
e_1_3_2_38_2
e_1_3_2_8_2
e_1_3_2_17_2
e_1_3_2_59_2
e_1_3_2_19_2
Hecker M. (e_1_3_2_16_2) 1996; 19
Maurizi M. R. (e_1_3_2_33_2) 1990; 265
Maurizi M. R. (e_1_3_2_32_2) 1990; 265
e_1_3_2_34_2
e_1_3_2_57_2
e_1_3_2_4_2
e_1_3_2_36_2
e_1_3_2_55_2
Zweiger G. (e_1_3_2_60_2) 1994; 235
Kaneko T. (e_1_3_2_21_2) 1996; 3
Schirmer E. C. (e_1_3_2_45_2) 1996; 21
Alley M. R. K. (e_1_3_2_2_2) 1993; 259
Sanger F. (e_1_3_2_44_2) 1977; 74
Turgay K. (e_1_3_2_50_2) 1998; 17
7543475 - J Bacteriol. 1995 Aug;177(15):4372-6
8411153 - J Mol Biol. 1993 Oct 5;233(3):414-28
1362210 - J Gen Microbiol. 1992 Oct;138(10):2125-35
7623377 - J Mol Biol. 1995 Jul 28;250(5):587-94
9006009 - J Bacteriol. 1997 Feb;179(3):592-600
14220656 - Bacteriol Rev. 1964 Sep;28:231-95
271968 - Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7
8226770 - J Biol Chem. 1993 Oct 25;268(30):22618-26
7724551 - Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3274-7
9573050 - Genes Dev. 1998 May 1;12(9):1338-47
8617219 - EMBO J. 1996 Jan 15;15(2):437-44
8772382 - Trends Biochem Sci. 1996 Aug;21(8):289-96
9390554 - Cell. 1997 Nov 14;91(4):447-56
9203582 - Genes Dev. 1997 Jun 15;11(12):1561-72
8830234 - Mol Microbiol. 1996 Feb;19(3):417-28
9267022 - Cell. 1997 Aug 8;90(3):415-24
8577742 - Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1210-4
9428517 - Cell. 1997 Dec 26;91(7):939-47
9537357 - J Bacteriol. 1998 Apr;180(7):1632-41
1658564 - Methods Enzymol. 1991;204:372-84
8606166 - J Bacteriol. 1996 Apr;178(7):1919-27
334726 - J Bacteriol. 1977 Oct;132(1):294-301
9537320 - Nature. 1998 Mar 26;392(6674):353-8
9512521 - Genes Dev. 1998 Mar 15;12(6):880-93
7542800 - Science. 1995 Jul 28;269(5223):496-512
9575205 - J Biol Chem. 1998 May 15;273(20):12476-81
8666236 - Genes Dev. 1996 Jun 15;10(12):1532-42
7896686 - J Bacteriol. 1995 Apr;177(7):1662-9
7911771 - Genetics. 1994 Mar;136(3):721-30
2197276 - J Biol Chem. 1990 Jul 25;265(21):12546-52
8665847 - EMBO J. 1996 May 15;15(10):2393-406
7743994 - EMBO J. 1995 May 1;14(9):1867-77
8456303 - Science. 1993 Mar 19;259(5102):1754-7
8905231 - DNA Res. 1996 Jun 30;3(3):109-36
9755166 - EMBO J. 1998 Oct 1;17(19):5658-69
9384377 - Nature. 1997 Nov 20;390(6657):249-56
9252185 - Nature. 1997 Aug 7;388(6642):539-47
9495753 - J Bacteriol. 1998 Mar;180(5):1154-8
6329717 - EMBO J. 1982;1(8):945-51
9106654 - Genes Dev. 1997 Apr 1;11(7):815-23
2197275 - J Biol Chem. 1990 Jul 25;265(21):12536-45
2211522 - J Bacteriol. 1990 Oct;172(10):6026-34
9890793 - EMBO J. 1998 Nov 16;17(22):6730-8
8606189 - J Bacteriol. 1996 Apr;178(7):2094-101
8644489 - Adv Enzymol Relat Areas Mol Biol. 1995;71:1-39
1392079 - Mol Biol Cell. 1992 Aug;3(8):913-26
8606155 - J Bacteriol. 1996 Apr;178(7):1829-41
9634230 - Nature. 1998 Jun 11;393(6685):537-44
6050209 - Nature. 1967 Aug 5;215(5101):588-91
8289276 - J Mol Biol. 1994 Jan 14;235(2):472-85
8990305 - J Bacteriol. 1997 Jan;179(2):514-21
References_xml – volume: 91
  start-page: 939
  year: 1997
  ident: e_1_3_2_29_2
  article-title: PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80485-7
– volume: 91
  start-page: 447
  year: 1997
  ident: e_1_3_2_53_2
  article-title: The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80431-6
– ident: e_1_3_2_52_2
  doi: 10.1002/j.1460-2075.1982.tb01276.x
– ident: e_1_3_2_43_2
– ident: e_1_3_2_58_2
  doi: 10.1128/jb.178.7.2094-2101.1996
– volume: 12
  start-page: 880
  year: 1998
  ident: e_1_3_2_22_2
  article-title: Cell cycle-dependent transcriptional and proteolytic regulation of FtsZ in Caulobacter
  publication-title: Genes Dev.
  doi: 10.1101/gad.12.6.880
– volume: 265
  start-page: 12546
  year: 1990
  ident: e_1_3_2_33_2
  article-title: Clp P represents a unique family of serine proteases
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)38379-6
– ident: e_1_3_2_9_2
  doi: 10.1128/jb.132.1.294-301.1977
– ident: e_1_3_2_19_2
  doi: 10.1002/j.1460-2075.1996.tb00597.x
– volume: 392
  start-page: 353
  year: 1998
  ident: e_1_3_2_6_2
  article-title: The complete genome of the hyperthermophilic bacterium Aquifex aeolicus
  publication-title: Nature
  doi: 10.1038/32831
– volume: 1
  start-page: 784
  year: 1983
  ident: e_1_3_2_46_2
  article-title: A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria
  publication-title: Bio/Technology
  doi: 10.1038/nbt1183-784
– ident: e_1_3_2_10_2
  doi: 10.1126/science.7542800
– volume: 21
  start-page: 289
  year: 1996
  ident: e_1_3_2_45_2
  article-title: HSP100/Clp proteins: a common mechanism explains diverse functions
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/S0968-0004(96)10038-4
– volume: 92
  start-page: 3274
  year: 1995
  ident: e_1_3_2_28_2
  article-title: Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.92.8.3274
– ident: e_1_3_2_59_2
  doi: 10.1128/JB.180.5.1154-1158.1998
– volume: 17
  start-page: 5658
  year: 1998
  ident: e_1_3_2_18_2
  article-title: An essential protease involved in bacterial cell cycle control
  publication-title: EMBO J.
  doi: 10.1093/emboj/17.19.5658
– ident: e_1_3_2_31_2
  doi: 10.1128/jb.177.15.4372-4376.1995
– volume: 10
  start-page: 1532
  year: 1996
  ident: e_1_3_2_56_2
  article-title: Caulobacter Lon protease has a critical role in cell-cycle control of DNA methylation
  publication-title: Genes Dev.
  doi: 10.1101/gad.10.12.1532
– volume: 250
  start-page: 587
  year: 1995
  ident: e_1_3_2_23_2
  article-title: Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1995.0400
– ident: e_1_3_2_39_2
– volume: 235
  start-page: 472
  year: 1994
  ident: e_1_3_2_60_2
  article-title: A Caulobacter DNA methyltransferase that functions only in the predivisional cell
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1994.1007
– ident: e_1_3_2_8_2
  doi: 10.1016/0076-6879(91)04019-K
– ident: e_1_3_2_48_2
  doi: 10.1128/jb.177.7.1662-1669.1995
– ident: e_1_3_2_24_2
  doi: 10.1128/jb.172.10.6026-6034.1990
– ident: e_1_3_2_17_2
– volume: 138
  start-page: 2125
  year: 1992
  ident: e_1_3_2_51_2
  article-title: Stress proteins and cross-protection by heat shock and salt stress in Bacillus subtilis
  publication-title: J. Gen. Microbiol.
  doi: 10.1099/00221287-138-10-2125
– ident: e_1_3_2_55_2
– volume: 74
  start-page: 5463
  year: 1977
  ident: e_1_3_2_44_2
  article-title: DNA sequencing with chain-terminating inhibitors
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.74.12.5463
– volume: 17
  start-page: 6730
  year: 1998
  ident: e_1_3_2_50_2
  article-title: Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
  publication-title: EMBO J.
  doi: 10.1093/emboj/17.22.6730
– volume: 11
  start-page: 1561
  year: 1997
  ident: e_1_3_2_30_2
  article-title: ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway
  publication-title: Genes Dev.
  doi: 10.1101/gad.11.12.1561
– ident: e_1_3_2_40_2
  doi: 10.1128/jb.178.7.1919-1927.1996
– ident: e_1_3_2_41_2
  doi: 10.1128/jb.178.7.1829-1841.1996
– volume: 90
  start-page: 415
  year: 1997
  ident: e_1_3_2_7_2
  article-title: Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80502-4
– volume: 3
  start-page: 913
  year: 1992
  ident: e_1_3_2_11_2
  article-title: A developmentally regulated Caulobacter flagellar promoter is activated by 3′ enhancer and IHF binding elements
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.3.8.913
– volume: 71
  start-page: 1
  year: 1995
  ident: e_1_3_2_20_2
  article-title: Regulation of asymmetry and polarity during the Caulobacter cell cycle
  publication-title: Adv. Enzymol.
– ident: e_1_3_2_5_2
  doi: 10.1038/31159
– volume: 215
  start-page: 588
  year: 1967
  ident: e_1_3_2_42_2
  article-title: In vitro synthesis of bacteriophage lysozyme
  publication-title: Nature
  doi: 10.1038/215588a0
– ident: e_1_3_2_38_2
  doi: 10.1128/br.28.3.231-295.1964
– volume: 93
  start-page: 1210
  year: 1996
  ident: e_1_3_2_47_2
  article-title: A cell cycle-regulated bacterial DNA methyltransferase is essential for viability
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.93.3.1210
– volume: 273
  start-page: 12476
  year: 1998
  ident: e_1_3_2_15_2
  article-title: Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.20.12476
– ident: e_1_3_2_3_2
– ident: e_1_3_2_36_2
  doi: 10.1093/genetics/136.3.721
– volume: 15
  start-page: 437
  year: 1996
  ident: e_1_3_2_26_2
  article-title: Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp protease
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1996.tb00374.x
– volume: 19
  start-page: 417
  year: 1996
  ident: e_1_3_2_16_2
  article-title: Heat-shock and general stress response in Bacillus subtilis
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.1996.396932.x
– ident: e_1_3_2_49_2
  doi: 10.1038/41483
– ident: e_1_3_2_37_2
– ident: e_1_3_2_4_2
  doi: 10.1128/JB.180.7.1632-1641.1998
– volume: 265
  start-page: 12536
  year: 1990
  ident: e_1_3_2_32_2
  article-title: Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)38378-4
– volume: 3
  start-page: 109
  year: 1996
  ident: e_1_3_2_21_2
  article-title: Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
  publication-title: DNA Res.
  doi: 10.1093/dnares/3.3.109
– ident: e_1_3_2_12_2
  doi: 10.1016/S0021-9258(18)41573-6
– volume: 12
  start-page: 1338
  year: 1998
  ident: e_1_3_2_13_2
  article-title: The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
  publication-title: Genes Dev.
  doi: 10.1101/gad.12.9.1338
– ident: e_1_3_2_25_2
  doi: 10.1038/36786
– volume: 233
  start-page: 414
  year: 1993
  ident: e_1_3_2_27_2
  article-title: Plasmid addiction genes of bacteriophage P1: doc, which causes cell death on curing of prophage, and phd, which prevents host death when prophage is retained
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1993.1521
– ident: e_1_3_2_35_2
– volume: 14
  start-page: 1867
  year: 1995
  ident: e_1_3_2_54_2
  article-title: The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1995.tb07179.x
– ident: e_1_3_2_34_2
  doi: 10.1128/jb.179.3.592-600.1997
– volume: 259
  start-page: 1754
  year: 1993
  ident: e_1_3_2_2_2
  article-title: Requirement of the carboxyl terminus of the bacterial chemoreceptor for its targeted proteolysis
  publication-title: Science
  doi: 10.1126/science.8456303
– ident: e_1_3_2_57_2
  doi: 10.1128/jb.179.2.514-521.1997
– volume: 11
  start-page: 815
  year: 1997
  ident: e_1_3_2_14_2
  article-title: Protein quality control: triage by chaperones and proteases
  publication-title: Genes Dev.
  doi: 10.1101/gad.11.7.815
– reference: 9267022 - Cell. 1997 Aug 8;90(3):415-24
– reference: 7543475 - J Bacteriol. 1995 Aug;177(15):4372-6
– reference: 9890793 - EMBO J. 1998 Nov 16;17(22):6730-8
– reference: 8606166 - J Bacteriol. 1996 Apr;178(7):1919-27
– reference: 9384377 - Nature. 1997 Nov 20;390(6657):249-56
– reference: 8617219 - EMBO J. 1996 Jan 15;15(2):437-44
– reference: 8990305 - J Bacteriol. 1997 Jan;179(2):514-21
– reference: 8456303 - Science. 1993 Mar 19;259(5102):1754-7
– reference: 8411153 - J Mol Biol. 1993 Oct 5;233(3):414-28
– reference: 7896686 - J Bacteriol. 1995 Apr;177(7):1662-9
– reference: 1392079 - Mol Biol Cell. 1992 Aug;3(8):913-26
– reference: 9634230 - Nature. 1998 Jun 11;393(6685):537-44
– reference: 9106654 - Genes Dev. 1997 Apr 1;11(7):815-23
– reference: 9495753 - J Bacteriol. 1998 Mar;180(5):1154-8
– reference: 2197276 - J Biol Chem. 1990 Jul 25;265(21):12546-52
– reference: 8606155 - J Bacteriol. 1996 Apr;178(7):1829-41
– reference: 7743994 - EMBO J. 1995 May 1;14(9):1867-77
– reference: 9512521 - Genes Dev. 1998 Mar 15;12(6):880-93
– reference: 6329717 - EMBO J. 1982;1(8):945-51
– reference: 8289276 - J Mol Biol. 1994 Jan 14;235(2):472-85
– reference: 8606189 - J Bacteriol. 1996 Apr;178(7):2094-101
– reference: 8226770 - J Biol Chem. 1993 Oct 25;268(30):22618-26
– reference: 2197275 - J Biol Chem. 1990 Jul 25;265(21):12536-45
– reference: 9428517 - Cell. 1997 Dec 26;91(7):939-47
– reference: 9537320 - Nature. 1998 Mar 26;392(6674):353-8
– reference: 8577742 - Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1210-4
– reference: 6050209 - Nature. 1967 Aug 5;215(5101):588-91
– reference: 8905231 - DNA Res. 1996 Jun 30;3(3):109-36
– reference: 9252185 - Nature. 1997 Aug 7;388(6642):539-47
– reference: 9573050 - Genes Dev. 1998 May 1;12(9):1338-47
– reference: 7542800 - Science. 1995 Jul 28;269(5223):496-512
– reference: 8665847 - EMBO J. 1996 May 15;15(10):2393-406
– reference: 8644489 - Adv Enzymol Relat Areas Mol Biol. 1995;71:1-39
– reference: 1658564 - Methods Enzymol. 1991;204:372-84
– reference: 8830234 - Mol Microbiol. 1996 Feb;19(3):417-28
– reference: 7623377 - J Mol Biol. 1995 Jul 28;250(5):587-94
– reference: 9537357 - J Bacteriol. 1998 Apr;180(7):1632-41
– reference: 14220656 - Bacteriol Rev. 1964 Sep;28:231-95
– reference: 9006009 - J Bacteriol. 1997 Feb;179(3):592-600
– reference: 271968 - Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7
– reference: 1362210 - J Gen Microbiol. 1992 Oct;138(10):2125-35
– reference: 7724551 - Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3274-7
– reference: 9575205 - J Biol Chem. 1998 May 15;273(20):12476-81
– reference: 9390554 - Cell. 1997 Nov 14;91(4):447-56
– reference: 9755166 - EMBO J. 1998 Oct 1;17(19):5658-69
– reference: 7911771 - Genetics. 1994 Mar;136(3):721-30
– reference: 334726 - J Bacteriol. 1977 Oct;132(1):294-301
– reference: 9203582 - Genes Dev. 1997 Jun 15;11(12):1561-72
– reference: 8666236 - Genes Dev. 1996 Jun 15;10(12):1532-42
– reference: 2211522 - J Bacteriol. 1990 Oct;172(10):6026-34
– reference: 8772382 - Trends Biochem Sci. 1996 Aug;21(8):289-96
SSID ssj0014452
Score 1.7373728
Snippet Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino...
The region of the Caulobacter crescentus chromosome harboring the genes for the ClpXP protease was isolated and characterized. Comparison of the deduced amino...
SourceID pubmedcentral
proquest
pubmed
crossref
highwire
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 3039
SubjectTerms Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
Amino acids
ATPases Associated with Diverse Cellular Activities
Bacteria
Bacterial Proteins - metabolism
Bacteriology
Base Sequence
Blotting, Western
Caulobacter crescentus
Caulobacter crescentus - cytology
Caulobacter crescentus - enzymology
Caulobacter crescentus - genetics
Caulobacter crescentus - growth & development
Cell Division
Cloning, Molecular
Consensus Sequence
DNA-Binding Proteins
Endopeptidase Clp
Escherichia coli
Escherichia coli - genetics
Escherichia coli Proteins
Gene Expression Regulation, Bacterial
Genes
Genes, Bacterial - genetics
Genetic Complementation Test
Genetics and Molecular Biology
Heat-Shock Response
Microbiology
Molecular Chaperones
Molecular Sequence Data
Mutation
Promoter Regions, Genetic - genetics
Sequence Homology, Amino Acid
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Transcription Factors
Transcription, Genetic - genetics
Title Identification and Transcriptional Control of the Genes Encoding the Caulobacter crescentus ClpXP Protease
URI http://jb.asm.org/content/181/10/3039.abstract
https://www.ncbi.nlm.nih.gov/pubmed/10322004
https://www.proquest.com/docview/227060029
https://www.proquest.com/docview/17231457
https://www.proquest.com/docview/69748702
https://pubmed.ncbi.nlm.nih.gov/PMC93758
Volume 181
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3JbtswECXcFAV6KbrHTRcd2pMhV6Q26hgbKQIDDnqIAd8EUkvqIJaNSDo0X9rP6QxFypLrFGkvtiGKgqR5noUz80jIZ_BRAyokt13mu7bnpZkdBZ60M85ogrtcRSk2J88vgvOFN1v6y8HgV6dqqa7kOLk72FfyP1KFYyBX7JL9B8m2F4UD8BvkC58gYfh8kIybLttcL7upPICyPUYTqIWBphRdlwIgy3Q5OiuSTWr6pKaiRlIQJG0egQup2J3qcjS92S6_Yx9B1SZw_vRhJw3Xc29pfi6u0HGdul8iXppUvN-67qdX6HMiCXh11y7vVFmOre7ICbpepaOLeoPbtpjhxW2JVTj6baS6Zy_aFQR2ugJQXXUKUeerHdFUV0FjxQhtNk0cZ41OBoNqc-7uKW3aRafT0cFglKPDxoFhw8NsMobJY1yuwCw46DvVstmbAmLerhVokG9QQa41l6ZEYM-KtrWN1zKG68cQXOH1H5HHLAxVAYFaR9L5Lc_zNY9987imxozxr_fdH9Lb6pvp-1CG1_pQjLRf6tvxnS6fk2caMNZpg-AXZJAVL8mTZhvUn6_IdR_HFuDY2sOxpXFsbXIL4GMpHFsGx-pQB8fWDseWwrFlcPyaLL6dXU7Pbb0HiJ1ALF7ZQvo8zd088ySNuEhFKAIpmC9y6bgiwP0KEobJZyo8mToyjGAUvmiYgKfNU_cNOSo2RXYMLxhCf8pzx_UTCWGDE8kok6GTUFBiqZvQIQnNW40TTZCP-7TcxCpQZjyeTbqijVE0MYpmSGg7c9uQxDxgzokRXCzKddyHDYwaWcZa4ZQxY0h15TAY_dSOgjXAFJ8osk1dxhCOuNTzw_vPCKLQAxvNhuRtg4zOHTfoGhK_h5n2BGSi748Uqx-KkR5iHJ-_--sTnZCnO9XwnhxVt3X2Afz5Sn5Uf43fDszyWQ
linkProvider National Library of Medicine
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=Identification+and+Transcriptional+Control+of+the+Genes+Encoding+the+Caulobacter+crescentus+ClpXP+Protease&rft.jtitle=Journal+of+Bacteriology&rft.au=Magne+%C3%98ster%C3%A5s&rft.au=Agathe+Stotz&rft.au=Stefanie+Schmid+Nuoffer&rft.au=Urs+Jenal&rft.date=1999-05-01&rft.pub=American+Society+for+Microbiology&rft.issn=0021-9193&rft.eissn=1067-8832&rft.volume=181&rft.issue=10&rft.spage=3039&rft_id=info:doi/10.1128%2FJB.181.10.3039-3050.1999&rft_id=info%3Apmid%2F10322004&rft.externalDBID=n%2Fa&rft.externalDocID=jb_181_10_3039
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