PMID:8195089

Citation	Deutscher, J, Reizer, J, Fischer, C, Galinier, A, Saier, MH Jr and Steinmetz, M (1994) Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J. Bacteriol. 176:3336-44
Abstract	In gram-positive bacteria, HPr, a phosphocarrier protein of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), is phosphorylated by an ATP-dependent, metabolite-activated protein kinase on seryl residue 46. In a Bacillus subtilis mutant strain in which Ser-46 of HPr was replaced with a nonphosphorylatable alanyl residue (ptsH1 mutation), synthesis of gluconate kinase, glucitol dehydrogenase, mannitol-1-P dehydrogenase and the mannitol-specific PTS permease was completely relieved from repression by glucose, fructose, or mannitol, whereas synthesis of inositol dehydrogenase was partially relieved from catabolite repression and synthesis of alpha-glucosidase and glycerol kinase was still subject to catabolite repression. When the S46A mutation in HPr was reverted to give S46 wild-type HPr, expression of gluconate kinase and glucitol dehydrogenase regained full sensitivity to repression by PTS sugars. These results suggest that phosphorylation of HPr at Ser-46 is directly or indirectly involved in catabolite repression. A strain deleted for the ptsGHI genes was transformed with plasmids expressing either the wild-type ptsH gene or various S46 mutant ptsH genes (S46A or S46D). Expression of the gene encoding S46D HPr, having a structure similar to that of P-ser-HPr according to nuclear magnetic resonance data, caused significant reduction of gluconate kinase activity, whereas expression of the genes encoding wild-type or S46A HPr had no effect on this enzyme activity. When the promoterless lacZ gene was put under the control of the gnt promoter and was subsequently incorporated into the amyE gene on the B. subtilis chromosome, expression of beta-galactosidase was inducible by gluconate and repressed by glucose. However, we observed no repression of beta-galactosidase activity in a strain carrying the ptsH1 mutation. Additionally, we investigated a ccpA mutant strain and observed that all of the enzymes which we found to be relieved from carbon catabolite repression in the ptsH1 mutant strain were also insensitive to catabolite repression in the ccpA mutant. Enzymes that were repressed in the ptsH1 mutant were also repressed in the ccpA mutant.
Links	PubMed PMC205505
Keywords	Bacillus subtilis/enzymology; Bacillus subtilis/genetics; Bacterial Proteins; Base Sequence; Enzyme Repression; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes, Bacterial/genetics; Gluconates/metabolism; Mannitol/metabolism; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutation; Phosphoenolpyruvate Sugar Phosphotransferase System/analysis; Phosphoenolpyruvate Sugar Phosphotransferase System/genetics; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Phosphorylation; Phosphotransferases (Alcohol Group Acceptor)/analysis; Promoter Regions, Genetic/genetics; Protein Kinases/metabolism; Sorbitol/metabolism; Sugar Alcohol Dehydrogenases/analysis
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:PTHP		GO:0043610: regulation of carbohydrate utilization	ECO:0000315:		P		Table 2 shows enzyme activity for gluconate kinase not repressed in mutant	complete CACAO 2000
BACSU:PTHP	involved_in	GO:0043610: regulation of carbohydrate utilization	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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