Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh

Journal of Molecular Microbiology and Biotechnology

Volumn 3, Issue 3, 2001, Pages 429-432

  Penin, F ^a   Favier, A ^a   Montserret, R ^a   Brutscher, B ^a   Deutscher, J ^a   Marion, D ^a   Galinier, A ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CYCLIC AMP BINDING PROTEIN; DIMER; HISTIDINE DERIVATIVE; MONOMER; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; REPRESSOR PROTEIN;

BACILLUS SUBTILIS; CATABOLITE REPRESSION; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONFERENCE PAPER; CONTROLLED STUDY; DIMERIZATION; DISSOCIATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; TEMPERATURE;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CIRCULAR DICHROISM; DIMERIZATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE SYSTEM; PHOSPHOPROTEINS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 0035015834     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper

References (23)

1. Natural abondance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
2. Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
3. ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes
4. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr
5. Phosphorylation of either Crh or HPr mediates binding of CcpA to the Bacillus subtilis xyn cre and catabolite repression of the xyn operon
6. The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression
7. New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression
8. Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals
9. Catabolite repression of α-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors
10. Protein secondary structure and circular dichroism: A practical guide
11. Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr
12. NADP, corepressor for the Bacillus catabolite control protein CcpA
13. The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
14. Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon
15. The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport
16. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
17. Catabolite regulation of the pta gene as part of carbon flow pathways in Bacillus subtilis
18. A novel protein kinase that controls carbon catabolite repression in bacteria
19. Transcriptional activation of the Bacillus subtilis ackA gene requires sequences upstream of the promoter
20. The structure and function of HPr
21. A family of bacterial regulators homologous to Gal and Lac repressors
22. Expression of the Bacillus subtilis acsA gene: Position and sequence context affect cremediated carbon catabolite repression
23. Trans-acting factors affecting carbon catabolite repression of the hut operon in Bacillus subtilis