Phosphorylation of either crh or HPr mediates binding of CcpA to the bacillus subtilis xyn cre and catabolite repression of the xyn operon - PubMed (original) (raw)
. 1999 Feb 19;286(2):307-14.
doi: 10.1006/jmbi.1998.2492.
Affiliations
- PMID: 9973552
- DOI: 10.1006/jmbi.1998.2492
Phosphorylation of either crh or HPr mediates binding of CcpA to the bacillus subtilis xyn cre and catabolite repression of the xyn operon
A Galinier et al. J Mol Biol. 1999.
Abstract
Carbon catabolite repression (CCR) of several Bacillus subtilis catabolic genes is mediated by ATP-dependent phosphorylation of Ser46 of the histidine-containing protein (HPr), a phosphocarrier protein of the phosphoenolpyruvate (PEP): sugar phosphotransferase system. A recently discovered HPr-like protein of B. subtilis, Crh, cannot be phosphorylated by PEP and enzyme I but becomes phosphorylated at Ser46 by the ATP-dependent, metabolite-activated HPr kinase. Genetic data suggested that Crh is also implicated in CCR. We here demonstrate that in a ptsH1 crh1 mutant, in which Ser46 of both HPr and Crh is replaced with an alanyl residue, expression of the beta-xylosidase-encoding xynB gene was completely relieved from CCR. No effect on CCR could be observed in strains carrying the crh1 allele, suggesting that under the experimental conditions P-Ser-HPr can substitute for P-Ser-Crh in CCR. By contrast, a ptsH1 mutant was slightly relieved from CCR of xynB, indicating that P-Ser-Crh can substitute only partly for P-Ser-HPr. Mapping experiments allowed us to identify the xyn promoter and a catabolite responsive element (cre) located 229 bp downstream of the transcription start point. Using DNase I footprinting experiments, we could demonstrate that similar to P-Ser-HPr, P-Ser-Crh stimulates binding of CcpA to the xyn cre. Fructose 1,6-bisphosphate was found to strongly enhance binding of the P-Ser-HPr/CcpA and P-Ser-Crh/CcpA complexes to the xyn cre, but had no effect on binding of CcpA alone.
Copyright 1999 Academic Press.
Similar articles
- Quantification of the influence of HPrSer46P on CcpA-cre interaction.
Aung-Hilbrich LM, Seidel G, Wagner A, Hillen W. Aung-Hilbrich LM, et al. J Mol Biol. 2002 May 24;319(1):77-85. doi: 10.1016/S0022-2836(02)00245-0. J Mol Biol. 2002. PMID: 12051938 - The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression.
Galinier A, Haiech J, Kilhoffer MC, Jaquinod M, Stülke J, Deutscher J, Martin-Verstraete I. Galinier A, et al. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8439-44. doi: 10.1073/pnas.94.16.8439. Proc Natl Acad Sci U S A. 1997. PMID: 9237995 Free PMC article. - Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals.
Gösseringer R, Küster E, Galinier A, Deutscher J, Hillen W. Gösseringer R, et al. J Mol Biol. 1997 Mar 7;266(4):665-76. doi: 10.1006/jmbi.1996.0820. J Mol Biol. 1997. PMID: 9102460 - Phosphotransfer functions mutated Bacillus subtilis HPr-like protein Crh carrying a histidine in the active site.
Darbon E, Galinier A, Le Coq D, Deutscher J. Darbon E, et al. J Mol Microbiol Biotechnol. 2001 Jul;3(3):439-44. J Mol Microbiol Biotechnol. 2001. PMID: 11361076 Review. - CcpA-independent carbon catabolite repression in Bacillus subtilis.
Dahl MK. Dahl MK. J Mol Microbiol Biotechnol. 2002 May;4(3):315-21. J Mol Microbiol Biotechnol. 2002. PMID: 11931564 Review.
Cited by
- Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa.
Daigle DM, Cao L, Fraud S, Wilke MS, Pacey A, Klinoski R, Strynadka NC, Dean CR, Poole K. Daigle DM, et al. J Bacteriol. 2007 Aug;189(15):5441-51. doi: 10.1128/JB.00543-07. Epub 2007 Jun 1. J Bacteriol. 2007. PMID: 17545281 Free PMC article. - Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis.
Görke B, Fraysse L, Galinier A. Görke B, et al. J Bacteriol. 2004 May;186(10):2992-5. doi: 10.1128/JB.186.10.2992-2995.2004. J Bacteriol. 2004. PMID: 15126459 Free PMC article. - Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.
Singh KD, Schmalisch MH, Stülke J, Görke B. Singh KD, et al. J Bacteriol. 2008 Nov;190(21):7275-84. doi: 10.1128/JB.00848-08. Epub 2008 Aug 29. J Bacteriol. 2008. PMID: 18757537 Free PMC article. - Phosphorylation of HPr by the bifunctional HPr Kinase/P-ser-HPr phosphatase from Lactobacillus casei controls catabolite repression and inducer exclusion but not inducer expulsion.
Dossonnet V, Monedero V, Zagorec M, Galinier A, Pérez-Martínez G, Deutscher J. Dossonnet V, et al. J Bacteriol. 2000 May;182(9):2582-90. doi: 10.1128/JB.182.9.2582-2590.2000. J Bacteriol. 2000. PMID: 10762262 Free PMC article. - Catabolite repression and activation in Bacillus subtilis: dependency on CcpA, HPr, and HprK.
Lorca GL, Chung YJ, Barabote RD, Weyler W, Schilling CH, Saier MH Jr. Lorca GL, et al. J Bacteriol. 2005 Nov;187(22):7826-39. doi: 10.1128/JB.187.22.7826-7839.2005. J Bacteriol. 2005. PMID: 16267306 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous