Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis

The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigma(A)-dependent promoter and is inducible by lichenan,...

Full description

Saved in:
Bibliographic Details
Published inJournal of bacteriology Vol. 181; no. 16; pp. 4995 - 5003
Main Authors Tobisch, S, Stülke, J, Hecker, M
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.08.1999
Subjects
Online AccessGet full text

Cover

Loading…
Abstract The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigma(A)-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. Induction of the operon requires a DNA sequence with dyad symmetry located immediately upstream of the licBCAH promoter. Expression of the lic operon is positively controlled by the LicR regulator protein, which contains two potential helix-turn-helix motifs, two phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulation domains (PRDs), and a domain similar to PTS enzyme IIA (EIIA). The activity of LicR is stimulated by modification (probably phosphorylation) of both PRD-I and PRD-II by the general PTS components and is negatively regulated by modification (probably phosphorylation) of its EIIA domain by the specific EII(Lic) in the absence of oligomeric beta-glucosides. This was shown by the analysis of licR mutants affected in potential phosphorylation sites. Moreover, the lic operon is subject to carbon catabolite repression (CCR). CCR takes place via a CcpA-dependent mechanism and a CcpA-independent mechanism in which the general PTS enzyme HPr is involved.
AbstractList The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric β-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a ς A -dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. Induction of the operon requires a DNA sequence with dyad symmetry located immediately upstream of the licBCAH promoter. Expression of the lic operon is positively controlled by the LicR regulator protein, which contains two potential helix-turn-helix motifs, two phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulation domains (PRDs), and a domain similar to PTS enzyme IIA (EIIA). The activity of LicR is stimulated by modification (probably phosphorylation) of both PRD-I and PRD-II by the general PTS components and is negatively regulated by modification (probably phosphorylation) of its EIIA domain by the specific EII Lic in the absence of oligomeric β-glucosides. This was shown by the analysis of licR mutants affected in potential phosphorylation sites. Moreover, the lic operon is subject to carbon catabolite repression (CCR). CCR takes place via a CcpA-dependent mechanism and a CcpA-independent mechanism in which the general PTS enzyme HPr is involved.
The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigmaA-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose.
The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta -glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigma super(A)-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. Induction of the operon requires a DNA sequence with dyad symmetry located immediately upstream of the licBCAH promoter. Expression of the lic operon is positively controlled by the LicR regulator protein, which contains two potential helix-turn-helix motifs, two phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulation domains (PRDs), and a domain similar to PTS enzyme IIA (EIIA). The activity of LicR is stimulated by modification (probably phosphorylation) of both PRD-I and PRD-II by the general PTS components and is negatively regulated by modification (probably phosphorylation) of its EIIA domain by the specific EII super(Lic) in the absence of oligomeric beta -glucosides. This was shown by the analysis of licR mutants affected in potential phosphorylation sites. Moreover, the lic operon is subject to carbon catabolite repression (CCR). CCR takes place via a CcpA-dependent mechanism and a CcpA-independent mechanism in which the general PTS enzyme HPr is involved.
The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigma(A)-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. Induction of the operon requires a DNA sequence with dyad symmetry located immediately upstream of the licBCAH promoter. Expression of the lic operon is positively controlled by the LicR regulator protein, which contains two potential helix-turn-helix motifs, two phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulation domains (PRDs), and a domain similar to PTS enzyme IIA (EIIA). The activity of LicR is stimulated by modification (probably phosphorylation) of both PRD-I and PRD-II by the general PTS components and is negatively regulated by modification (probably phosphorylation) of its EIIA domain by the specific EII(Lic) in the absence of oligomeric beta-glucosides. This was shown by the analysis of licR mutants affected in potential phosphorylation sites. Moreover, the lic operon is subject to carbon catabolite repression (CCR). CCR takes place via a CcpA-dependent mechanism and a CcpA-independent mechanism in which the general PTS enzyme HPr is involved.
The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigma(A)-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. Induction of the operon requires a DNA sequence with dyad symmetry located immediately upstream of the licBCAH promoter. Expression of the lic operon is positively controlled by the LicR regulator protein, which contains two potential helix-turn-helix motifs, two phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulation domains (PRDs), and a domain similar to PTS enzyme IIA (EIIA). The activity of LicR is stimulated by modification (probably phosphorylation) of both PRD-I and PRD-II by the general PTS components and is negatively regulated by modification (probably phosphorylation) of its EIIA domain by the specific EII(Lic) in the absence of oligomeric beta-glucosides. This was shown by the analysis of licR mutants affected in potential phosphorylation sites. Moreover, the lic operon is subject to carbon catabolite repression (CCR). CCR takes place via a CcpA-dependent mechanism and a CcpA-independent mechanism in which the general PTS enzyme HPr is involved.The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on substrates such as lichenan or barley glucan. The lic operon is transcribed from a sigma(A)-dependent promoter and is inducible by lichenan, lichenan hydrolysate, and cellobiose. Induction of the operon requires a DNA sequence with dyad symmetry located immediately upstream of the licBCAH promoter. Expression of the lic operon is positively controlled by the LicR regulator protein, which contains two potential helix-turn-helix motifs, two phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulation domains (PRDs), and a domain similar to PTS enzyme IIA (EIIA). The activity of LicR is stimulated by modification (probably phosphorylation) of both PRD-I and PRD-II by the general PTS components and is negatively regulated by modification (probably phosphorylation) of its EIIA domain by the specific EII(Lic) in the absence of oligomeric beta-glucosides. This was shown by the analysis of licR mutants affected in potential phosphorylation sites. Moreover, the lic operon is subject to carbon catabolite repression (CCR). CCR takes place via a CcpA-dependent mechanism and a CcpA-independent mechanism in which the general PTS enzyme HPr is involved.
Author Tobisch, S
Hecker, M
Stülke, J
AuthorAffiliation Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald, D-17487 Greifswald, 1 and Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik, Friedrich-Alexander-Universität Erlangen-Nürnberg, D-91058 Erlangen, 2 Germany
AuthorAffiliation_xml – name: Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald, D-17487 Greifswald, 1 and Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik, Friedrich-Alexander-Universität Erlangen-Nürnberg, D-91058 Erlangen, 2 Germany
Author_xml – sequence: 1
  givenname: S
  surname: Tobisch
  fullname: Tobisch, S
  organization: Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald, D-17487 Greifswald, Germany
– sequence: 2
  givenname: J
  surname: Stülke
  fullname: Stülke, J
– sequence: 3
  givenname: M
  surname: Hecker
  fullname: Hecker, M
BackLink https://www.ncbi.nlm.nih.gov/pubmed/10438772$$D View this record in MEDLINE/PubMed
BookMark eNqFkc2KFDEUhYOMOD2jryDBhbsq81uVgBtn8JcGYdB1kUpud2dIJ2WSGmifxwe1tHsGdeMiXEi-c-7JvRfoLKYICGFKWkqZevXpqqWKtrRrhdaykYTwlmqtH6EVJVo1UnJyhlaEMNpoqvk5uijllhAqhGRP0Dklgqu-Zyv04wa2czDVp4jTBtcd4OAtThPk482VsT6EueAyj9UHX7CJDtudycZWyP77g3ZKFWL1JuBpl8py8uFkXHyFcm-_9vYG52PXlPGUF5mPeDz8xhrnMyzGDu_narYQofjyFD3emFDg2aleoq_v3n65_tCsP7__eP1m3Uycqtqojjim3chH54xmYLkDIXtQhruN09JysGqErhPWKtIrIwUQ6bjtN0x3QvBL9ProO83jHpxdvpNNGKbs9yYfhmT88PdL9Lthm-4GzbXSi_zlSZ7TtxlKHfa-WAjBREhzGbplV0L17L8g7ZnilMkFfPEPeJvmHJcZDIz1RCrV_YKe_5n6Ie79kvlPrAiy1A
CODEN JOBAAY
ContentType Journal Article
Copyright Copyright American Society for Microbiology Aug 1999
Copyright © 1999, American Society for Microbiology 1999
Copyright_xml – notice: Copyright American Society for Microbiology Aug 1999
– notice: Copyright © 1999, American Society for Microbiology 1999
DBID CGR
CUY
CVF
ECM
EIF
NPM
7QL
7TM
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
7X8
5PM
DOI 10.1128/JB.181.16.4995-5003.1999
DatabaseName 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 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
Bacteriology Abstracts (Microbiology B)
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 1098-5530
EndPage 5003
ExternalDocumentID PMC93989
44662312
10438772
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
8WZ
9M8
A6W
ABPPZ
ABTAH
ACGFO
ACGOD
ACNCT
ACPRK
ADBBV
AENEX
AFFDN
AFFNX
AFRAH
AGCDD
AGVNZ
AI.
AIDAL
AJUXI
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BKOMP
BTFSW
C1A
CGR
CJ0
CS3
CUY
CVF
DIK
DU5
E3Z
EBS
ECM
EIF
EJD
F5P
FRP
GX1
H13
HYE
HZ~
IH2
KQ8
L7B
MVM
NHB
NPM
O9-
OHT
OK1
P-O
P-S
P2P
PKN
PQQKQ
QZG
RHF
RHI
RNS
RPM
RSF
RXW
TAE
TR2
UCJ
UHB
UKR
UPT
VH1
VQA
W8F
WH7
WHG
WOQ
X7M
Y6R
YIN
YQT
YR2
YZZ
ZCA
ZCG
ZGI
ZXP
ZY4
~02
~KM
7QL
7TM
7U9
8FD
AAGFI
ADXHL
C1K
FR3
H94
M7N
P64
RC3
7X8
5PM
ID FETCH-LOGICAL-p318t-860d29db3bdda92ec3de457e8a3dfd95c3ec8be664cc8078a54e05d3c7f296443
ISSN 0021-9193
IngestDate Thu Aug 21 14:04:21 EDT 2025
Fri Jul 11 12:12:00 EDT 2025
Thu Jul 10 23:21:00 EDT 2025
Fri Aug 22 20:36:49 EDT 2025
Wed Feb 19 01:22:28 EST 2025
IsPeerReviewed true
IsScholarly true
Issue 16
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-p318t-860d29db3bdda92ec3de457e8a3dfd95c3ec8be664cc8078a54e05d3c7f296443
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: Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald, Friedrich-Ludwig-Jahn-Strasse 15, D-17487 Greifswald, Germany. Phone: 49(0)3834-864200. Fax: 49(0)3834-864202. E-mail: hecker@microbio7.biologie.uni-greifswald.de.
PMID 10438772
PQID 227058865
PQPubID 40724
PageCount 9
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_93989
proquest_miscellaneous_69954872
proquest_miscellaneous_17283125
proquest_journals_227058865
pubmed_primary_10438772
PublicationCentury 1900
PublicationDate 1999-08-01
PublicationDateYYYYMMDD 1999-08-01
PublicationDate_xml – month: 08
  year: 1999
  text: 1999-08-01
  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 9882680 - J Bacteriol. 1999 Jan;181(2):632-41
2651862 - Microbiol Rev. 1989 Mar;53(1):109-20
6274841 - J Bacteriol. 1982 Jan;149(1):114-22
8245830 - J Gen Microbiol. 1993 Sep;139(9):2041-5
11902727 - Mol Microbiol. 1997 Jul;25(1):65-78
2265750 - Gene. 1990 Nov 30;96(1):125-8
6359157 - Proc Natl Acad Sci U S A. 1983 Nov;80(22):6790-4
8606172 - J Bacteriol. 1996 Apr;178(7):1971-9
2163394 - J Bacteriol. 1990 Jul;172(7):3966-73
9663674 - Mol Microbiol. 1998 Jun;28(5):865-74
8195089 - J Bacteriol. 1994 Jun;176(11):3336-44
7540244 - Mol Microbiol. 1995 Feb;15(3):395-401
3064811 - Biochemistry. 1988 Aug 23;27(17):6512-6
9384377 - Nature. 1997 Nov 20;390(6657):249-56
271968 - Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7
9622354 - Mol Microbiol. 1998 Apr;28(2):293-303
7592486 - J Bacteriol. 1995 Dec;177(23):6919-27
9765562 - J Bacteriol. 1998 Oct;180(20):5319-26
9162046 - J Biol Chem. 1997 May 30;272(22):14166-74
7730271 - J Bacteriol. 1995 May;177(9):2403-7
10941796 - J Mol Microbiol Biotechnol. 1999 Aug;1(1):141-8
7704253 - Microbiology. 1995 Feb;141 ( Pt 2):261-8
1738313 - Mol Microbiol. 1992 Jan;6(1):35-46
1577686 - J Bacteriol. 1992 May;174(10):3161-70
7623661 - Mol Microbiol. 1995 Mar;15(6):1049-53
8245831 - J Gen Microbiol. 1993 Sep;139(9):2047-54
7855437 - Res Microbiol. 1994 Sep;145(7):503-18
2105292 - J Bacteriol. 1990 Feb;172(2):1043-50
7592487 - J Bacteriol. 1995 Dec;177(23):6928-36
8246840 - Microbiol Rev. 1993 Sep;57(3):543-94
9570401 - Mol Microbiol. 1998 Mar;27(6):1157-69
7559347 - J Bacteriol. 1995 Oct;177(19):5590-7
2117666 - J Mol Biol. 1990 Aug 5;214(3):657-71
10048041 - Mol Microbiol. 1999 Feb;31(3):995-1006
7883710 - J Bacteriol. 1995 Mar;177(6):1527-35
8990303 - J Bacteriol. 1997 Jan;179(2):496-506
1619665 - J Mol Biol. 1992 Jul 5;226(1):85-99
3098288 - Biochemistry. 1986 Oct 21;25(21):6543-51
8626332 - J Bacteriol. 1996 May;178(9):2637-44
9465101 - Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1823-8
1537788 - J Bacteriol. 1992 Mar;174(5):1433-8
1904524 - Mol Microbiol. 1991 Mar;5(3):575-84
9202047 - J Biol Chem. 1997 Jul 4;272(27):17230-7
8132469 - J Bacteriol. 1994 Mar;176(6):1738-45
References_xml – reference: 2651862 - Microbiol Rev. 1989 Mar;53(1):109-20
– reference: 7855437 - Res Microbiol. 1994 Sep;145(7):503-18
– reference: 2163394 - J Bacteriol. 1990 Jul;172(7):3966-73
– reference: 2265750 - Gene. 1990 Nov 30;96(1):125-8
– reference: 9570401 - Mol Microbiol. 1998 Mar;27(6):1157-69
– reference: 2117666 - J Mol Biol. 1990 Aug 5;214(3):657-71
– reference: 9162046 - J Biol Chem. 1997 May 30;272(22):14166-74
– reference: 2105292 - J Bacteriol. 1990 Feb;172(2):1043-50
– reference: 8990303 - J Bacteriol. 1997 Jan;179(2):496-506
– reference: 7883710 - J Bacteriol. 1995 Mar;177(6):1527-35
– reference: 7559347 - J Bacteriol. 1995 Oct;177(19):5590-7
– reference: 8132469 - J Bacteriol. 1994 Mar;176(6):1738-45
– reference: 11902727 - Mol Microbiol. 1997 Jul;25(1):65-78
– reference: 9384377 - Nature. 1997 Nov 20;390(6657):249-56
– reference: 1537788 - J Bacteriol. 1992 Mar;174(5):1433-8
– reference: 7704253 - Microbiology. 1995 Feb;141 ( Pt 2):261-8
– reference: 9465101 - Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1823-8
– reference: 7540244 - Mol Microbiol. 1995 Feb;15(3):395-401
– reference: 7592487 - J Bacteriol. 1995 Dec;177(23):6928-36
– reference: 8245831 - J Gen Microbiol. 1993 Sep;139(9):2047-54
– reference: 7592486 - J Bacteriol. 1995 Dec;177(23):6919-27
– reference: 9622354 - Mol Microbiol. 1998 Apr;28(2):293-303
– reference: 3064811 - Biochemistry. 1988 Aug 23;27(17):6512-6
– reference: 8195089 - J Bacteriol. 1994 Jun;176(11):3336-44
– reference: 271968 - Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7
– reference: 9663674 - Mol Microbiol. 1998 Jun;28(5):865-74
– reference: 10048041 - Mol Microbiol. 1999 Feb;31(3):995-1006
– reference: 8245830 - J Gen Microbiol. 1993 Sep;139(9):2041-5
– reference: 6359157 - Proc Natl Acad Sci U S A. 1983 Nov;80(22):6790-4
– reference: 8626332 - J Bacteriol. 1996 May;178(9):2637-44
– reference: 7623661 - Mol Microbiol. 1995 Mar;15(6):1049-53
– reference: 1904524 - Mol Microbiol. 1991 Mar;5(3):575-84
– reference: 6274841 - J Bacteriol. 1982 Jan;149(1):114-22
– reference: 1577686 - J Bacteriol. 1992 May;174(10):3161-70
– reference: 9882680 - J Bacteriol. 1999 Jan;181(2):632-41
– reference: 10941796 - J Mol Microbiol Biotechnol. 1999 Aug;1(1):141-8
– reference: 3098288 - Biochemistry. 1986 Oct 21;25(21):6543-51
– reference: 1738313 - Mol Microbiol. 1992 Jan;6(1):35-46
– reference: 8606172 - J Bacteriol. 1996 Apr;178(7):1971-9
– reference: 7730271 - J Bacteriol. 1995 May;177(9):2403-7
– reference: 9202047 - J Biol Chem. 1997 Jul 4;272(27):17230-7
– reference: 8246840 - Microbiol Rev. 1993 Sep;57(3):543-94
– reference: 1619665 - J Mol Biol. 1992 Jul 5;226(1):85-99
– reference: 9765562 - J Bacteriol. 1998 Oct;180(20):5319-26
SSID ssj0014452
Score 1.8253444
Snippet The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta-glucosides, which are produced by extracellular enzymes on...
The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric beta -glucosides, which are produced by extracellular enzymes...
The lic operon of Bacillus subtilis is required for the transport and degradation of oligomeric β-glucosides, which are produced by extracellular enzymes on...
SourceID pubmedcentral
proquest
pubmed
SourceType Open Access Repository
Aggregation Database
Index Database
StartPage 4995
SubjectTerms Bacillus subtilis
Bacillus subtilis - genetics
Bacillus subtilis - metabolism
Bacteria
Bacterial Proteins
Bacteriology
Cellular biology
Chromosome Mapping
DNA-Binding Proteins - genetics
DNA-Directed RNA Polymerases - genetics
Gene Expression Regulation, Bacterial - drug effects
Gene Expression Regulation, Enzymologic - drug effects
Genetic Complementation Test
Genetics and Molecular Biology
Glucans - pharmacology
Glycoside Hydrolases - genetics
Glycoside Hydrolases - metabolism
Lac Operon
Mutagenesis, Site-Directed
Mutation
Operon - genetics
Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry
Phosphoenolpyruvate Sugar Phosphotransferase System - genetics
Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism
Phosphorylation
Plasmids
Promoter Regions, Genetic
Protein Structure, Tertiary
Proteins
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Regulation
Repressor Proteins - genetics
Sigma Factor - genetics
Trans-Activators - genetics
Trans-Activators - metabolism
Title Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis
URI https://www.ncbi.nlm.nih.gov/pubmed/10438772
https://www.proquest.com/docview/227058865
https://www.proquest.com/docview/17283125
https://www.proquest.com/docview/69954872
https://pubmed.ncbi.nlm.nih.gov/PMC93989
Volume 181
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3JbtswECXSFAV6KbrHTRceegvk2iIpUccmSBAEdhKkNuCbQEkULMCwDEs6ONf-Sj-0M6I2Gza6XASDoijB72k4pGbeEPKVcVeqeKAsJVxtcSdklnIVt2CyjuNYehErs97Ht871lN_MxOzo6GcnaqnIg374uDev5H9QhTbAFbNk_wHZZlBogN-ALxwBYTj-FcYPppB85fOhC4mS1Xeo_V22nKswWSyK7CwrgjxZJEaP-aLRaH5srr1PcwwbArzu52m2mqfrTTXwjyQ3urQ4_CgJH86qu6ZrzDLAYpnowmI3y9hPcGHHRQ52Cqxokh3wfgPzBFub-pM0SDJTmqotDpYXelGJgrb7tnUsyLjdtDBCB7LetKiTCIZgZ01xxNYQD7uM69pVWJeJzhwtBqUwwh77b2NOw815H8bqD50-Xmdhb8zK9No5r_7Of3vnX01HI39yOZs8IU9tWGuUGeOzJk4IFpyikpw3T1yHg9ny26H77Fut7AbddryYyUvyogKAfjdcekWO9PI1eWYKkm7ekF8to2gaU4CcAqOoYRS21IyiNaMoMIruMgp7NoyiO4yiJaPq4ZFRtGEUrRhFgw3dYhTtMOotmV5dTi6uraqOh7WCGSO3pDOIbC8KWBBFyrN1yCLNwTRIxaI48kTIdCgD7Tg8DLH8gRJcD0TEQjfGoADO3pHjZbrUJ4TGIrSFhjW-HGquEA47dsFpVoyziAvVI6f1P-9XL2rm27Y7EFI6oke-NGfBiuKnMbXUaZH5WKWNga9_uIeDwonStXvkvcHRXxk5GH-IH9NdPCO2EG46oIL79pllMi-V3D3mSe_DH5_qlDxvX6KP5DhfF_oT-MJ58Lnk6m857bzP
linkProvider Geneva Foundation for Medical Education and Research
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=Regulation+of+the+lic+Operon+of+Bacillus+subtilis+and+Characterization+of+Potential+Phosphorylation+Sites+of+the+LicR+Regulator+Protein+by+Site-Directed+Mutagenesis&rft.jtitle=Journal+of+bacteriology&rft.au=Tobisch%2C+S&rft.au=Stuelke%2C+J&rft.au=Hecker%2C+M&rft.date=1999-08-01&rft.issn=0021-9193&rft.volume=181&rft.issue=16&rft.spage=4995&rft.epage=5003&rft_id=info:doi/10.1128%2FJB.181.16.4995-5003.1999&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