Difference between revisions of "Sandbox"

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* '''Description:''' synthesis of the modified ribonukleotide queuosine <br/><br/>
+
* '''Description:''' HPr, General component of the sugar phosphotransferase system (PTS).  <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'''
|''queF ''
+
|''ptsH''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ykvM''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
+
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || unknown
+
|style="background:#ABCDEF;" align="center"| '''Product''' || histidine-containing phosphocarrier <br/>protein HPr of the PTS
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || tRNA modification
+
|style="background:#ABCDEF;" align="center"|'''Function''' || PTS-dependent sugar transport <br/>and carbon catabolite repression
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 4.927 
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 9,1 kDa, 4.58
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 495 bp, 165 aa
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 264 bp, 88 amino acids
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[queE]]'', ''[[ykvN]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ptsG]]'', ''[[ptsI]]''
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13248&#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:CAB13263&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
|colspan="2" | '''Genetic context''' <br/> [[Image:ykvM_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:ptsH_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 29: Line 29:
 
__TOC__
 
__TOC__
  
<br/><br/>
+
<br/><br/><br/><br/>
 +
 
  
 
=The gene=
 
=The gene=
Line 35: Line 36:
 
=== Basic information ===
 
=== Basic information ===
  
* '''Coordinates:'''
+
* '''Coordinates:''' 1458693 - 1458956
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
Line 41: Line 42:
 
=== Database entries ===
 
=== Database entries ===
  
* '''DBTBS entry:''' no entry
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html]
  
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG13315]
+
* '''SubtiList entry:'''[http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10200]
  
 
=== Additional information===
 
=== Additional information===
 
  
 
=The protein=
 
=The protein=
Line 52: Line 52:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:'''  
+
* '''Catalyzed reaction/ biological activity:''' Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein [[PtsH|HPr]] + protein EIIA N(tau)-phospho-L-histidine
  
* '''Protein family:'''
+
* '''Protein family:''' HPr family
  
* '''Paralogous protein(s):'''
+
* '''Paralogous protein(s):''' [[Crh]]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
Line 62: Line 62:
 
* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
+
* '''Domains:''' HPr Domain (2–88)
  
* '''Modification:'''
+
* '''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]
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
Line 70: Line 70:
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:'''
+
* '''Interactions:'''[[PtsH|HPr]]-[[LicT]],  [[PtsH|HPr]]-[[SacY]],  [[PtsH|HPr]]-[[SacT]],  [[PtsH|HPr]]-[[GlcT]],  [[PtsH|HPr]]-[[GlpK]],  [[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]
  
* '''Localization:''' Cytoplasm
+
* '''Localization:''' Cytoplasm Cytoplasm  [http://www.ncbi.nlm.nih.gov/sites/entrez/16395550 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''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]
  
* '''Swiss prot entry:'''
+
* '''Swiss prot entry:''' [http://www.expasy.ch/cgi-bin/sprot-search-ac?P08877]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13750]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13900]
  
* '''E.C. number:'''
+
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.11.- 2.7.11.-]
  
 
=== Additional information===
 
=== Additional information===
 +
  
 
=Expression and regulation=
 
=Expression and regulation=
  
 
* '''Operon:'''  
 
* '''Operon:'''  
 +
**''[[ptsG]]-[[ptsH]]-[[ptsI]]''
 +
**''ptsH-[[ptsI]]''
  
* '''[[Sigma factor]]:'''  
+
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
  
* '''Regulation:'''  
+
* '''Regulation:''' expression activated by glucose (2-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose (''[[ptsG]]''), constitutive (''[[ptsH]]'')
  
* '''Regulatory mechanism:'''  
+
* '''Regulatory mechanism:''' ''[[ptsG]]'': transcriptional antitermination via the [[GlcT]]-dependent RNA-switch
  
* '''Additional information:'''  
+
* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:'''
+
* '''Mutant:''' MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), available in [[Stülke]] lab
  
* '''Expression vector:'''
+
* '''Expression vector:''' pGP438 (with N-terminal Strep-tag, in [[pGP172]]), pAG2 (His-tag) pGP371(ptsH-S46A, with His-tag, in [[pWH844]]), available in [[Stülke]]
       
+
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
* '''two-hybrid system:'''  
+
* '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Boris Görke| Görke]] lab
  
* '''Antibody:'''
+
* '''Antibody:''' available in [[Stülke]] lab
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
 +
 +
[[Josef Deutscher]], 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]
 +
 +
[[Anne Galinier]], University of Marseille, France
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 118: Line 133:
 
=References=
 
=References=
  
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
+
# 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]
 +
# 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]
 +
# 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]
 +
# 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., 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]
 +
# 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]

Revision as of 02:06, 30 April 2009

  • Description: HPr, General component of the sugar phosphotransferase system (PTS).

Gene name ptsH
Synonyms
Essential no
Product histidine-containing phosphocarrier
protein HPr of the PTS
Function PTS-dependent sugar transport
and carbon catabolite repression
MW, pI 9,1 kDa, 4.58
Gene length, protein length 264 bp, 88 amino acids
Immediate neighbours ptsG, ptsI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PtsH context.gif
This image was kindly provided by SubtiList






The gene

Basic information

  • Coordinates: 1458693 - 1458956

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine
  • Protein family: HPr family
  • Paralogous protein(s): Crh

Extended information on the protein

  • Kinetic information:
  • Domains: HPr Domain (2–88)
  • Modification: phosphorylations: transient phosphorylation by Enzyme I of the PTS on His-15, regulatory phosphorylation on Ser-46 by HprK PubMed, weak phosphorylation on Ser-12 PubMed, an extensive study on in vivo HPr phosphorylation can be found in Singh et al. (2008) PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: Cytoplasm Cytoplasm PubMed

Database entries

  • Structure: 2HID, complex of L. casei HprK with B. subtilis HPr NCBI, complex of L. Casei HprK with B. Subtilis HPr-Ser-P NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]

Additional information

Expression and regulation

  • Regulation: expression activated by glucose (2-fold) PubMed, induction by glucose (ptsG), constitutive (ptsH)
  • Regulatory mechanism: ptsG: transcriptional antitermination via the GlcT-dependent RNA-switch
  • Additional information:

Biological materials

  • Mutant: MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), available in Stülke lab
  • Expression vector: pGP438 (with N-terminal Strep-tag, in pGP172), pAG2 (His-tag) pGP371(ptsH-S46A, with His-tag, in pWH844), available in Stülke
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Görke lab
  • Antibody: available in Stülke lab

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

Wolfgang Hillen, Erlangen University, Germany Homepage

Richard Brennan, Houston, Texas, USA Homepage

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

Your additional remarks

References

  1. 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 PubMed
  2. 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. PubMed
  3. 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. PubMed
  4. 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.PubMed
  5. 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. PubMed
  6. 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. PubMed
  7. 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. DOI:10.1021/bi00314a033
  8. 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. PubMed
  9. 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. PubMed
  10. 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. PubMed
  11. 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. PubMed
  12. 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 . PubMed
  13. 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
  14. 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
  15. 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. PubMed
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