Difference between revisions of "Sandbox"

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−
* '''Description:''' trigger enzyme: major glucose permease of the PTS, EIICBA(Glc) <br/><br/>
+
* '''Description:''' repressor of the glycolytic ''[[gapA]]'' operon<br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
−
|''ptsG''
+
|''cggR''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ptsX, crr''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yvbQ ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || glucose-specific enzyme IICBA component
+
|style="background:#ABCDEF;" align="center"| '''Product''' || central glycolytic genes regulator
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || glucose transport and phosphorylation, control of [[GlcT]] activity
+
|style="background:#ABCDEF;" align="center"|'''Function''' || transcriptional regulator
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 75,3 kDa, 5.40
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 37,2 kDa,5.68
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 2097 bp, 699 amino acids
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1020 bp, 340 amino acids
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glcT]]'', ''[[ptsH]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[araE]]'', ''[[gapA]]''
 
|-
 
|-
−
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ptsG_nucleotide.txt    Gene sequence      (+200bp)  ]'''  
+
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/cggR_nucleotide.txt    Gene sequence      (+200bp)  ]'''  
−
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ptsG_protein.txt Protein sequence]'''
+
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/cggR_protein.txt Protein sequence]'''
 
|-
 
|-
−
|colspan="2" style="background:#FAF8CC;color:#FF0000" align="center" | '''Caution: The sequence for this gene in SubtiList contains errors
+
|colspan="2" | '''Genetic context''' <br/> [[Image:cggR_context.gif]]
−
|-
 
−
|colspan="2" | '''Genetic context''' <br/> [[Image:ptsG_context.gif]]
 
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
Line 33: Line 31:
  
 
<br/><br/>
 
<br/><br/>
 +
  
 
=The gene=
 
=The gene=
Line 38: Line 37:
 
=== Basic information ===
 
=== Basic information ===
  
−
* '''Coordinates:''' 1456496 - 1458592
+
* '''Coordinates:''' 3481786 - 3482805
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
Line 44: Line 43:
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cggR-gapA-pgk-tpiA-pgm-eno.html]
  
−
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10198]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG14085]
  
 
=== Additional information===
 
=== Additional information===
Line 54: Line 53:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
−
* '''Catalyzed reaction/ biological activity:''' transport and phosphorylation of glucose, receives a phosphate from [[PtsH |HPr]] at the IIA domain (His-620), the phosphate group is then transferred to the IIB domain (Cys-461) an finally to the incoming glucose. In the absence of glucose, PtsG phosphorylates and thereby inactivates the transcriptional antiterminator [[GlcT]].
+
* '''Catalyzed reaction/ biological activity:''' transcription repression of the glycolytic ''[[gapA]]'' operon
  
−
* '''Protein family:''' PTS enzyme II, glucose family
+
* '''Protein family:'''
  
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
Line 65: Line 64:
  
 
* '''Domains:'''  
 
* '''Domains:'''  
−
** 11x transmembrane domain (16–36, 89–109, 139–159, 180–200, 233–253, 283–303, 313–333, 338–358, 365–385, 388–408)
+
** DNA binding domain (H-T-H motif) (37–56)
−
** PTS EIIC domain (  1-424)
 
−
** PTS EIIB domain (439–520)
 
−
** PTS EIIA domain (568–672)
 
  
−
* '''Modification:''' transient  phosphorylation ([[PtsH |HPr]]-dependent) on His-620, then internal phosphotransfer from His-620 to Cys-461
+
* '''Modification:'''
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:'''
+
* '''Effectors of protein activity:''' fructose 1.6-bisphosphate [http://www.ncbi.nlm.nih.gov/sites/entrez/12622823 PubMed] and dihydroxyacetone phosphate, glucose-6-phosphate and fructose-6-phosphate [http://www.ncbi.nlm.nih.gov/sites/entrez/18554327 PubMed] act as inducer and result in release of CggR from the DNA
  
−
* '''Interactions:''' PtsG-[[PtsH |HPr]], PtsG-[[GlcT]] (for phosphorylation of [[GlcT]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/14527945 PubMed]
+
* '''Interactions:'''
  
−
* '''Localization:''' membrane protein [http://www.ncbi.nlm.nih.gov/sites/entrez/18763711 NCBI]
+
* '''Localization:'''
  
 
=== Database entries ===
 
=== Database entries ===
−
 
−
* '''Structure:''' IIA domain [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=56258 NCBI], NMR IIA domain [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=55395 NCBI]
 
  
−
* '''Swiss prot entry:''' [http://www.expasy.ch/cgi-bin/sprot-search-ac?P20166]
+
* '''Structure:''' complex with Fructose-6-Phosphate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=65242 NCBI], effector binding domain [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=44226 NCBI]
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13890]
+
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O32253]
  
−
* '''E.C. number:''' [http://www.expasy.ch/cgi-bin/get-enzyme-entry?2.7.1.69]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU33950]
  
 
=== Additional information===
 
=== Additional information===
 +
  
 
=Expression and regulation=
 
=Expression and regulation=
  
 
* '''Operon:'''  
 
* '''Operon:'''  
−
**''[[ptsG]]-[[ptsH]]-[[ptsI]]''  
+
** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]''
−
**''[[ptsH]]-[[ptsI]]''
+
** ''[[cggR]]-[[gapA]]''
 +
 
 +
The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the ''[[cggR]]'' open reading frame. This results in stable mature ''[[gapA]]'' and ''[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' mRNAs. The processing event requires the [[Rny]] protein.
 +
 
 +
* '''Sigma factor:''' [[SigA]]
 +
 
 +
* '''Regulation:''' expression activated by glucose (76.76) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  [[CggR]] represses the operon in the absence of glycolytic sugars [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+12622823 PubMed]
  
−
* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
+
* '''Regulatory mechanism:''' repression
  
−
* '''Regulation:''' expression activated by glucose (31.83) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose
+
* '''Database entries:''' [http://dbtbs.hgc.jp/COG/prom/cggR-gapA-pgk-tpiA-pgm-eno.html DBTBS]
  
−
* '''Regulatory mechanism:''' transcriptional antitermination via the [[GlcT]]-dependent RNA-switch [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+9765562 PubMed]
 
 
* '''Additional information:'''
 
* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =
  
−
* '''Mutant:''' GP474 (cat), QB5436 (spc), QB5445 (erm), available in [[Stülke]] lab
+
* '''Mutant:''' GP311 (in frame deletion), available in [[Stülke]] lab
  
−
* '''Expression vector:''' pGP123 (domains BA, in [[pWH844]]), pGP123 (domains BA, mut: H620D, in [[pWH844]]), pGP428 (EIIB, in [[pWH844]]), pGP437(EIIA in [[pWH844]], with thrombin cleavage site), available in [[Stülke]] lab
+
* '''Expression vector:''' pGP705 (N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab
 
 
−
* '''lacZ fusion:''' pGP34 ([[pAC5]]), pGP66 ([[pAC7]]), pGP606 (mutant terminator, [[pAC6]]), pGP532 ([[pAC7]]), series of promoter deletions are available in [[pAC5]] and [[pAC6]], series of RAT mutants are available in [[pAC6]], available in [[Stülke]] lab
+
* '''lacZ fusion:''' pGP504 (in [[pAC7]]), pGP509 (in [[pAC6]]), available in [[Stülke]] lab
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
−
* '''Antibody:'''
+
* '''Antibody:''' available in [[Stülke]] lab
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
  
−
[[Stülke|Jörg Stülke]], University of Göttingen, Germany
+
[[Stephane Aymerich |Stephane Aymerich]], Microbiology and Molecular Genetics, INRA Paris-Grignon, France
−
[http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 126: Line 125:
 
=References=
 
=References=
 
hier steht Paper  
 
hier steht Paper  
−
# Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing ''Bacillus subtilis'' by divergent approaches. Proteomics '''8:''' 4123-4136 [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
+
# Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. subm.
−
# Stülke J, Martin-Verstraete I, Zagorec M (1997) Induction of the ''Bacillus subtilis ptsGHI'' operon by glucose is controlled by a novel antiterminator, ''GlcT Mol Microbiol.''  '''25:''' 65-78. [http://www.ncbi.nlm.nih.gov/sites/entrez/11902727 PubMed]
+
# Doan, T., and S. Aymerich. 2003. Regulation of the central glycolytic pathways in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol. Microbiol. 47: 1709-1721. [http://www.ncbi.nlm.nih.gov/sites/entrez/12622823 PubMed]
−
# Bachem S, Stülke J. (1998)    Regulation of the ''Bacillus subtilis'' GlcT antiterminator protein by components of the phosphotransferase system. ''J Bacteriol.'' '''180:''' 5319-26 [http://www.ncbi.nlm.nih.gov/sites/entrez/9765562 PubMed]
+
# Doan et al. (2008) A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor. Proteins 71:2038-2050. [http://www.ncbi.nlm.nih.gov/sites/entrez/18186488 PubMed]
−
# Bachem, S., Faires, N., & Stülke, J. (1997) Characterization of the presumptive phosphorylation sites of the ''Bacillus subtilis'' glucose permease by site-directed mutagenesis: Implication in glucose transport and catabolite repression. FEMS Microbiol. L. 156: 233-238. [http://www.ncbi.nlm.nih.gov/sites/entrez/9513271 PubMed]
+
# Fillinger, S., Boschi-Muller, S., Azza, S., Dervyn, E., Branlant, G., and Aymerich, S. (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275, 14031-14037. [http://www.ncbi.nlm.nih.gov/sites/entrez/10799476 PubMed]
−
# Gonzy-Tréboul, G., de Waard, J. H., Zagorec, M., and Postma, P.W. (1991). The glucose permease of the phosphotransferase system of ''Bacillus subtilis'': Evidence for IIGlc and IIIGlc domains. Mol. Microbiol. 5, 1241-1249. [http://www.ncbi.nlm.nih.gov/sites/entrez/1956301 PubMed]
+
# Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in ''Bacillus subtilis'': evidence for the presence of multiple levels of control of the ''gapA'' operon. Mol Microbiol 41, 409-422.[http://www.ncbi.nlm.nih.gov/sites/entrez/11489127 PubMed]
−
# Langbein, I., Bachem, S. & Stülke, J. (1999) Specific interaction of the RNA binding domain of the ''Bacillus subtilis'' transcriptional antiterminator GlcT with its RNA target, RAT. J. Mol. Biol. 293: 795-805. [http://www.ncbi.nlm.nih.gov/sites/entrez/10543968 PubMed]
+
# Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002). Control of the glycolytic ''gapA'' operon by the catabolite control protein A in ''Bacillus subtilis'': a novel mechanism of CcpA-mediated regulation. Mol Microbiol 45, 543-553.[http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
−
# Schilling, O., Herzberg, C., Hertrich, T., Vörsmann, H., Jessen, D., Hübner, S., Titgemeyer, F. & Stülke, J. (2006) Keeping signals straight in transcription regulation: specificity determinants for the interaction of a family of conserved bacterial RNA-protein couples. Nucl. Acids Res. 34: 6102-6115. [http://www.ncbi.nlm.nih.gov/sites/entrez/17074746 PubMed]
+
# Meinken, C., Blencke, H. M., Ludwig, H., and Stülke, J. (2003) Expression of the glycolytic ''gapA'' operon in ''Bacillus subtilis'': differential synthesis of proteins encoded by the operon. Microbiology 149, 751-761. [http://www.ncbi.nlm.nih.gov/sites/entrez/12634343 PubMed]
−
# Schilling, O., Langbein, I., Müller, M., Schmalisch, M. & Stülke, J. (2004) A protein-dependent riboswitch controlling ''ptsGHI'' operon expression in ''Bacillus subtilis'': RNA structure rather than sequence provides interaction specificity. Nucl. Acids Res. 32: 2853-2864. [http://www.ncbi.nlm.nih.gov/sites/entrez/15155854 PubMed]
+
# Rezacova et al. (2008) Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates. Mol. Microbiol. 69:895-910. [http://www.ncbi.nlm.nih.gov/sites/entrez/18554327 PubMed]
−
# Schmalisch, M., Bachem, S. & Stülke, J. (2003) Control of the ''Bacillus subtilis'' antiterminator protein GlcT by phosphorylation: Elucidation of the phosphorylation chain leading to inactivation of GlcT. J. Biol. Chem. 278: 51108-51115. [http://www.ncbi.nlm.nih.gov/sites/entrez/14527945 PubMed]
+
# Zorilla et al. (2007) Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR). Biochemistry 46:14996-15008. [http://www.ncbi.nlm.nih.gov/sites/entrez/18052209 PubMed]
−
# Zagorec, M. & Postma, P. (1992). Cloning and nucleotide sequence of the ''ptsG'' gene of ''Bacillus subtilis''. Mol Gen Genet 234, 325-328. [http://www.ncbi.nlm.nih.gov/sites/entrez/1508157 PubMed]
+
# Zorilla et al. (2007) Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA. Biophys. J. 92: 3215-3227. [http://www.ncbi.nlm.nih.gov/sites/entrez/17293407 PubMed]
−
# Sutrina, S. L., Reddy, P., Saier, M. H., Jr & Reizer, J. (1990). The glucose permease of ''Bacillus subtilis'' is a single polypeptide chain that functions to energize the sucrose permease. J Biol Chem 265, 18581-18589. [http://www.ncbi.nlm.nih.gov/sites/entrez/2120236 PubMed]
 
−
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 

Revision as of 18:08, 1 April 2009

  • Description: repressor of the glycolytic gapA operon

Gene name cggR
Synonyms yvbQ
Essential no
Product central glycolytic genes regulator
Function transcriptional regulator
MW, pI 37,2 kDa,5.68
Gene length, protein length 1020 bp, 340 amino acids
Immediate neighbours araE, gapA
Gene sequence (+200bp) Protein sequence
Genetic context
CggR context.gif
This image was kindly provided by SubtiList




The gene

Basic information

  • Coordinates: 3481786 - 3482805

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcription repression of the glycolytic gapA operon
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • DNA binding domain (H-T-H motif) (37–56)
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: fructose 1.6-bisphosphate PubMed and dihydroxyacetone phosphate, glucose-6-phosphate and fructose-6-phosphate PubMed act as inducer and result in release of CggR from the DNA
  • Interactions:
  • Localization:

Database entries

  • Structure: complex with Fructose-6-Phosphate NCBI, effector binding domain NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]

Additional information

Expression and regulation

The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the cggR open reading frame. This results in stable mature gapA and gapA-pgk-tpiA-pgm-eno mRNAs. The processing event requires the Rny protein.

  • Sigma factor: SigA
  • Regulation: expression activated by glucose (76.76) PubMed, CggR represses the operon in the absence of glycolytic sugars PubMed
  • Regulatory mechanism: repression
  • Additional information:

Biological materials

  • Mutant: GP311 (in frame deletion), available in Stülke lab
  • Expression vector: pGP705 (N-terminal His-tag, in pWH844), available in Stülke lab
  • GFP fusion:
  • Antibody: available in Stülke lab

Labs working on this gene/protein

Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

Your additional remarks

References

hier steht Paper

  1. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. subm.
  2. Doan, T., and S. Aymerich. 2003. Regulation of the central glycolytic pathways in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol. Microbiol. 47: 1709-1721. PubMed
  3. Doan et al. (2008) A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor. Proteins 71:2038-2050. PubMed
  4. Fillinger, S., Boschi-Muller, S., Azza, S., Dervyn, E., Branlant, G., and Aymerich, S. (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275, 14031-14037. PubMed
  5. Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422.PubMed
  6. Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002). Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol Microbiol 45, 543-553.PubMed
  7. Meinken, C., Blencke, H. M., Ludwig, H., and Stülke, J. (2003) Expression of the glycolytic gapA operon in Bacillus subtilis: differential synthesis of proteins encoded by the operon. Microbiology 149, 751-761. PubMed
  8. Rezacova et al. (2008) Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates. Mol. Microbiol. 69:895-910. PubMed
  9. Zorilla et al. (2007) Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR). Biochemistry 46:14996-15008. PubMed
  10. Zorilla et al. (2007) Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA. Biophys. J. 92: 3215-3227. PubMed
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