Difference between revisions of "Sandbox"

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−
* '''Description:''' HPr, General component of the sugar phosphotransferase system (PTS).  <br/><br/>
+
* '''Description:''' transcriptional antiterminator of the ''bglPH'' 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'''
−
|''ptsH''
+
|''licT''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
 
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
Line 10: Line 10:
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || histidine-containing phosphocarrier <br/>protein HPr of the PTS
+
|style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional antiterminator (BglG family)
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || PTS-dependent sugar transport <br/>and carbon catabolite repression
+
|style="background:#ABCDEF;" align="center"|'''Function''' || required for substrate-dependent induction of ''bglPH''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 9,1 kDa, 4.58
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 32 kDa, 5.944 
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 264 bp, 88 amino acids
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 831 bp, 277 aa
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ptsG]]'', ''[[ptsI]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[bglS]]'', ''[[yxiP]]''
 
|-
 
|-
−
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13263&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
+
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15944&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
−
|colspan="2" | '''Genetic context''' <br/> [[Image:ptsH_context.gif]]
+
|-
 +
|-
 +
|colspan="2" | '''Genetic context''' <br/> [[Image:licT_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 30: Line 32:
  
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
−
 
  
 
=The gene=
 
=The gene=
Line 36: Line 37:
 
=== Basic information ===
 
=== Basic information ===
  
−
* '''Coordinates:''' 1458693 - 1458956
+
* '''Coordinates:'''
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
 +
no expression of the ''[[bglP]]-[[bglH]]'' operon
  
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/licT-bglS.html]
  
−
* '''SubtiList entry:'''[http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10200]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10474]
  
 
=== Additional information===
 
=== Additional information===
 +
  
 
=The protein=
 
=The protein=
Line 52: Line 56:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
−
* '''Catalyzed reaction/ biological activity:''' Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein [[PtsH|HPr]] + protein EIIA N(tau)-phospho-L-histidine
+
* '''Catalyzed reaction/ biological activity:''' binding to the mRNAs of ''[[bglS]]'' and the ''[[bglP]]-[[bglH]]'' operon, causes transcription antitermination (in presence of salicin and absence of glucose)
  
−
* '''Protein family:''' HPr family
+
* '''Protein family:''' BglG family of antiterminators
  
−
* '''Paralogous protein(s):''' [[Crh]]
+
* '''Paralogous protein(s):''' [[SacY]], [[GlcT]], [[SacT]]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
Line 62: Line 66:
 
* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
−
* '''Domains:''' HPr Domain (2–88)
+
* '''Domains:'''  
  
−
* '''Modification:''' phosphorylations: transient phosphorylation by [[PtsI |Enzyme I]] of the PTS on His-15, regulatory phosphorylation on Ser-46 by [[HprK]] [http://www.ncbi.nlm.nih.gov/sites/entrez/2507315 PubMed], weak phosphorylation on Ser-12 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], an extensive study on ''in vivo'' HPr phosphorylation can be found in Singh et al. (2008) [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537  PubMed]
+
* '''Modification:'''
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
Line 70: Line 74:
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
−
* '''Interactions:''' GapA-PtsH, PtsH-MtlR, PtsH-LicR, PtsH-LevR, PtsH-ManR, PtsH -RbsR, HprK- PtsH, PtsH-GlpK, PtsH-GlcT, PtsH-SacT, PtsH-SacY, PtsH-LicT [[GapA]]-[[PtsH|HPr]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17142398 PubMed], [[PtsH|HPr]]-[[MtlR]], [[PtsH|HPr]]-[[LicR]], [[PtsH|HPr]]-[[LevR]],[[PtsH|HPr]]-[[ManR]], [[YesS]]-[[PtsH|HPr]] (HPr-His-P), [[PtsH|HPr]]-[[CcpA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12432959 PubMed], [[PtsH|HPr]]-[[RbsR]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16519689 PubMed], [[HprK]]-[[PtsH|HPr]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12009882 PubMed]
+
* '''Interactions:''' PtsH-LicT
  
−
* '''Localization:''' Cytoplasm  [http://www.ncbi.nlm.nih.gov/sites/entrez/16395550 PubMed]
+
* '''Localization:'''
  
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2HID 2HID], complex of ''L. casei'' HprK with ''B. subtilis'' HPr [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=20417 NCBI], complex of L. Casei HprK with B. Subtilis HPr-Ser-P [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=20418 NCBI]
+
* '''Structure:'''
  
−
* '''Swiss prot entry:''' [http://www.expasy.ch/cgi-bin/sprot-search-ac?P08877]
+
* '''Swiss prot entry:'''
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13900]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU39080]
  
−
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.11.- 2.7.11.-]
+
* '''E.C. number:'''
  
 
=== Additional information===
 
=== Additional information===
−
 
  
 
=Expression and regulation=
 
=Expression and regulation=
  
−
* '''Operon:'''  
+
* '''Operon:''' ''[[licT]]-[[bglS]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8606172 PubMed]
−
**''[[ptsG]]-[[ptsH]]-[[ptsI]]''
 
−
**''ptsH-[[ptsI]]''
 
  
−
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
+
* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8606172 PubMed]
  
−
* '''Regulation:''' expression activated by glucose (2-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose (''[[ptsG]]''), constitutive (''[[ptsH]]'')
+
* '''Regulation:'''  
  
−
* '''Regulatory mechanism:''' ''[[ptsG]]'': transcriptional antitermination via the [[GlcT]]-dependent RNA-switch
+
* '''Regulatory mechanism:'''  
  
 
* '''Additional information:'''
 
* '''Additional information:'''
Line 103: Line 104:
 
=Biological materials =
 
=Biological materials =
  
−
* '''Mutant:''' MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), available in [[Stülke]] lab
+
* '''Mutant:'''
  
−
* '''Expression vector:''' pGP438 (with N-terminal Strep-tag, in [[pGP172]]), pAG2 (His-tag) pGP371(ptsH-S46A, with His-tag, in [[pWH844]]), available in [[Stülke]]
+
* '''Expression vector:'''
−
+
       
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
−
* '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Boris Görke| Görke]] lab
+
* '''two-hybrid system:'''  
  
−
* '''Antibody:''' available in [[Stülke]] lab
+
* '''Antibody:'''
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
  
−
[[Josef Deutscher]], Paris-Grignon, France
+
[[Stephane Aymerich |Stephane Aymerich]], Microbiology and Molecular Genetics, INRA Paris-Grignon, France
−
 
 
−
[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 
−
 
 
−
[[Wolfgang Hillen]], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
 
−
 
 
−
[[Richard Brennan]], Houston, Texas, USA [http://www.mdanderson.org/departments/biochem/display.cfm?id=556ef368-6c81-4043-b74f350d41dd06cb&method=displayfull&pn=a8427ebd-d0ff-11d4-80fd00508b603a14 Homepage]
 
  
−
[[Boris Görke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/goerke.html Homepage]
+
[[Josef Deutscher]], Microbiology and Molecular Genetics, INRA Paris-Grignon, France
  
−
[[Anne Galinier]], University of Marseille, France
+
[[Michael Hecker]], Greifswald, Germany [http://www.mikrobiologie.uni-greifswald.de/index.php?id=20 Homepage]
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 133: Line 128:
 
=References=
 
=References=
  
−
# Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in ''Bacillus subtilis'': regulation of the central metabolic pathways. ''Metab Eng.'' '''5:''' 133-149 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
+
'''Original description'''
−
# Macek B, Mijakovic I, Olsen JV (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. ''Mol Cell Proteomics'' '''6(4):''' 697-707. [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
+
# Schnetz, K., Stülke, J., Gertz, S., Krüger, S., Krieg, M., Hecker, M. & Rak, B. (1996) LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family. J. Bacteriol. 178: 1971-1979. [http://www.ncbi.nlm.nih.gov/sites/entrez/8606172 PubMed]
−
# Müller W, Horstmann N, Hillen W (2006) The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr-Ser46-P in Bacillus subtilis ''FEBS J.'' '''273(6):''' 1251-61. [http://www.ncbi.nlm.nih.gov/sites/entrez/16519689 PubMed]
+
 
−
# Pompeo ''et al.'' (2007) Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in ''Bacillus subtilis''? J Bacteriol 189, 1154-1157.[http://www.ncbi.nlm.nih.gov/sites/entrez/17142398 PubMed]
+
'''Control of LicT activity'''
−
# Fieulaine, S., Morera, S., Poncet, S., Mijakovic, I., Galinier, A., Janin, J., Deutscher, J., and Nessler, S. (2002) X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc Natl Acad Sci U S A 99: 13437-13441. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359875 PubMed]
 
−
# Arnaud M, Vary P, Zagorec M, Klier A, Débarbouillé M, Postma P, Rapoport G (1992) Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity. J Bacteriol 174:3161-3170. [http://www.ncbi.nlm.nih.gov/sites/entrez/1577686 PubMed]
 
−
# Deutscher, J., Kessler, U., Alpert, C. A., and Hengstenberg, W. (1984) Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-ser-HPr and its possible regulatory function. Biochemistry 23: 4455-4460. [http://pubs.acs.org/doi/abs/10.1021/bi00314a033 DOI:10.1021/bi00314a033]
 
−
# Deutscher, J., Küster, E., Bergstedt, U., Charrier, V., and Hillen, W. (1995) Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol. Microbiol. 15: 1049-1053. [http://www.ncbi.nlm.nih.gov/sites/entrez/7623661  PubMed]
 
−
# Eisermann, R., Deutscher, J., Gonzy-Tréboul, G., and Hengstenberg, W. (1988) Site-directed mutagenesis with the ptsH gene of Bacillus subtilis. J Biol Chem 263: 17050-17054. [http://www.ncbi.nlm.nih.gov/sites/entrez/2846556  PubMed]
 
−
# Frisby, D., and Zuber, P. 1994. Mutations in pts cause catabolite-resistant sporulation and altered regulation of spo0H in Bacillus subtilis. J. Bacteriol. 176: 2587-2595. [http://www.ncbi.nlm.nih.gov/sites/entrez/8169206  PubMed]
 
−
# Galinier A, Deutscher J, Martin-Verstraete I: (1999) Phosphorylation of either Crh or HPr mediates binding of CcpA to the Bacillus subtilis xyn cre and catabolite repression of the xyn operon. J Mol Biol , 286:307-314. [http://www.ncbi.nlm.nih.gov/sites/entrez/9973552  PubMed]
 
−
# Görke, B., Fraysse, L. & Galinier, A. (2004) Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis. J. Bacteriol. 186, 2992-2995 . [http://www.ncbi.nlm.nih.gov/sites/entrez/15126459  PubMed]
 
 
# Lindner, C., Galinier, A., Hecker, M. & Deutscher, J. (1999) Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31, 995-1006 . [http://www.ncbi.nlm.nih.gov/sites/entrez/10048041  PubMed]
 
# Lindner, C., Galinier, A., Hecker, M. & Deutscher, J. (1999) Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31, 995-1006 . [http://www.ncbi.nlm.nih.gov/sites/entrez/10048041  PubMed]
 
# Lindner, C., Hecker, M., Le Coq, D. & Deutscher, J. (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184, 4819-4828 . [http://www.ncbi.nlm.nih.gov/sites/entrez/12169607  PubMed]
 
# Lindner, C., Hecker, M., Le Coq, D. & Deutscher, J. (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184, 4819-4828 . [http://www.ncbi.nlm.nih.gov/sites/entrez/12169607  PubMed]
−
# Martin-Verstraete, I., Charrier, V., Stülke, J., Galinier, A., Erni, B., Rapoport, G., & Deutscher, J. (1998) Antagonistic effects of dual PTS catalyzed phosphorylation on the Bacillus subtilis transcriptional activator LevR. Mol. Microbiol. 28: 293-303. [http://www.ncbi.nlm.nih.gov/sites/entrez/9622354  PubMed]
+
# Krüger, S., Gertz, S. & Hecker, M. Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression. J. Bacteriol. 178, 2637-2644 (1996). [http://www.ncbi.nlm.nih.gov/sites/entrez/8626332 PubMed]
−
# Martin-Verstraete, I., Deutscher, J., and Galinier, A. (1999) Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon. J Bacteriol 181: 2966-2969. [http://www.ncbi.nlm.nih.gov/sites/entrez/10217795  PubMed]
+
# Tortosa, P., Declerck, N., Dutartre, H., Lindner, C., Deutscher, J., and Le Coq, D. (2001) Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY. Mol Microbiol 41: 1381-1393. [http://www.ncbi.nlm.nih.gov/sites/entrez/11580842 PubMed]
−
# Reizer, J., Sutrina, S. L., Saier, Jr., M. H., Stewart, G. C., Peterkofsky, A., and Reddy, P. (1989) Mechanistic and physiological consequences of HPr(Ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: studies with site-specific mutants of HPr. EMBO J 8: 2111-2120. [http://www.ncbi.nlm.nih.gov/sites/entrez/2507315  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]
+
'''Structural analysis of LicT'''
−
# Schumacher, M. A. et al. (2004) Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118, 731-741 . [http://www.ncbi.nlm.nih.gov/sites/entrez/15369672  PubMed]
+
# Declerck N, Dutartre H, Receveur V, Dubois V, Royer C, Aymerich S, van Tilbeurgh H (2001) Dimer stabilization upon activation of the transcriptional antiterminator LicT. J Mol Biol 314:671-681. [http://www.ncbi.nlm.nih.gov/sites/entrez/11733988 PubMed]
−
# Singh, K. D., Halbedel, S., Görke, B. & Stülke, J. (2007) Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: implication of the protein phosphatase PrpC. J. Mol. Microbiol. Biotechnol. 13: 165-171. [http://www.ncbi.nlm.nih.gov/sites/entrez/17693724  PubMed]
+
# Graille, M. et al. Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J. Biol. Chem. 280, 14780-14789 (2005). [http://www.ncbi.nlm.nih.gov/sites/entrez/15699035 PubMed]
−
# Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537  PubMed]
+
# van Tilbeurgh H, Le Coq D, Declerck N (2001) Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator. EMBO J 20:3789-3799. [http://www.ncbi.nlm.nih.gov/sites/entrez/11447120 PubMed]
−
# Stülke, J., Martin-Verstraete, I., Charrier, V., Klier, A., Deutscher, J. & Rapoport, G. (1995) The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon. J. Bacteriol. 177: 6928-6936. [http://www.ncbi.nlm.nih.gov/sites/entrez/7592487  PubMed]
+
# Déméné H, Ducat T, De Guillen K, Birck C, Aymerich S, Kochoyan M, Declerck N.(2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.''J. Biol. Chem.'' '''283:''' 30838-30849. [http://www.ncbi.nlm.nih.gov/sites/entrez/18682383 PubMed]
−
# Tortosa, P., Aymerich, S., Lindner, C., Saier, M.H., Jr., Reizer, J. and Le Coq, D. (1997) Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system. J. Biol. Chem. 272, 17230-17237. [http://www.ncbi.nlm.nih.gov/sites/entrez/9202047  PubMed]
+
 
−
# Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A (1997) Cloning and sequencing of two enterococcal ''glpK'' genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J Biol Chem 272:14166-14174. [http://www.ncbi.nlm.nih.gov/sites/entrez/9162046 PubMed]
+
'''LicT-RNA interaction'''
−
# Darbon E, Servant P, Poncet S, Deutscher J (2002) Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P~GlpK dephosphorylation control ''Bacillus subtilis glpFK'' expression. Mol Microbiol 43:1039-1052. [http://www.ncbi.nlm.nih.gov/sites/entrez/11929549 PubMed]
+
# Yang Y, Declerck N, Manival X, Aymerich S, Kochoyan M (2002) Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT. EMBO J 21:1987-1997. [http://www.ncbi.nlm.nih.gov/sites/entrez/11953318 PubMed]
−
# Jones, B.E., Rajagopal, P., and Klevit, R.E. (1997) Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis. Protein Sci 6: 2107-2119. [http://www.ncbi.nlm.nih.gov/sites/entrez/9336834 PubMed]
+
# Aymerich, S. and Steinmetz, M. (1992) Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family. Proc. Natl. Acad. Sci. USA 89, 10410-10414. [http://www.ncbi.nlm.nih.gov/sites/entrez/1279678 PubMed]
−
# Rajagopal, P., Waygood, E.B., and Klevit, R.E. (1994) Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. Biochemistry 33: 15271-15282. [http://www.ncbi.nlm.nih.gov/sites/entrez/7803390 PubMed]
+
# Declerck, N., Vincent, F., Hoh, F., Aymerich, S. and van Tilbeurgh, H. (1999) RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domains from SacY and LicT. J. Mol. Biol. 294, 389-402. [http://www.ncbi.nlm.nih.gov/sites/entrez/10610766 PubMed]
 +
# Déméné H, Ducat T, De Guillen K, Birck C, Aymerich S, Kochoyan M, Declerck N.(2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.''J. Biol. Chem.'' '''283:''' 30838-30849. [http://www.ncbi.nlm.nih.gov/sites/entrez/18682383 PubMed]
 +
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 15:53, 27 April 2009

  • Description: transcriptional antiterminator of the bglPH operon

Gene name licT
Synonyms
Essential no
Product transcriptional antiterminator (BglG family)
Function required for substrate-dependent induction of bglPH
MW, pI 32 kDa, 5.944
Gene length, protein length 831 bp, 277 aa
Immediate neighbours bglS, yxiP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LicT context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

no expression of the bglP-bglH operon

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: binding to the mRNAs of bglS and the bglP-bglH operon, causes transcription antitermination (in presence of salicin and absence of glucose)
  • Protein family: BglG family of antiterminators

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions: PtsH-LicT
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

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

Josef Deutscher, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

Michael Hecker, Greifswald, Germany Homepage

Your additional remarks

References

Original description

  1. Schnetz, K., Stülke, J., Gertz, S., Krüger, S., Krieg, M., Hecker, M. & Rak, B. (1996) LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family. J. Bacteriol. 178: 1971-1979. PubMed

Control of LicT activity

  1. Lindner, C., Galinier, A., Hecker, M. & Deutscher, J. (1999) Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31, 995-1006 . PubMed
  2. Lindner, C., Hecker, M., Le Coq, D. & Deutscher, J. (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184, 4819-4828 . PubMed
  3. Krüger, S., Gertz, S. & Hecker, M. Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression. J. Bacteriol. 178, 2637-2644 (1996). PubMed
  4. Tortosa, P., Declerck, N., Dutartre, H., Lindner, C., Deutscher, J., and Le Coq, D. (2001) Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY. Mol Microbiol 41: 1381-1393. PubMed

Structural analysis of LicT

  1. Declerck N, Dutartre H, Receveur V, Dubois V, Royer C, Aymerich S, van Tilbeurgh H (2001) Dimer stabilization upon activation of the transcriptional antiterminator LicT. J Mol Biol 314:671-681. PubMed
  2. Graille, M. et al. Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J. Biol. Chem. 280, 14780-14789 (2005). PubMed
  3. van Tilbeurgh H, Le Coq D, Declerck N (2001) Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator. EMBO J 20:3789-3799. PubMed
  4. Déméné H, Ducat T, De Guillen K, Birck C, Aymerich S, Kochoyan M, Declerck N.(2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.J. Biol. Chem. 283: 30838-30849. PubMed

LicT-RNA interaction

  1. Yang Y, Declerck N, Manival X, Aymerich S, Kochoyan M (2002) Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT. EMBO J 21:1987-1997. PubMed
  2. Aymerich, S. and Steinmetz, M. (1992) Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family. Proc. Natl. Acad. Sci. USA 89, 10410-10414. PubMed
  3. Declerck, N., Vincent, F., Hoh, F., Aymerich, S. and van Tilbeurgh, H. (1999) RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domains from SacY and LicT. J. Mol. Biol. 294, 389-402. PubMed
  4. Déméné H, Ducat T, De Guillen K, Birck C, Aymerich S, Kochoyan M, Declerck N.(2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.J. Biol. Chem. 283: 30838-30849. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
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