In:
Journal of Bacteriology, American Society for Microbiology, Vol. 182, No. 20 ( 2000-10-15), p. 5799-5806
Kurzfassung:
Inactivation of ccpA in Enterococcus faecalis leads to reduction of the growth rate, derepression of the galKETR operon in the presence of a mixture of glucose and galactose, and reduction of transcription of ldh in the presence of glucose. Moreover, the E. faecalis ccpA gene fully complements a Bacillus subtilis ccpA mutant, arguing for similar functions of these two homologous proteins. Protein comparison on two-dimensional gels from the wild-type cells and the ccpA mutant cells revealed a pleiotropic effect of the mutation on gene expression. The HPr protein of the carbohydrate-phosphotransferase system was identified by microsequencing, and a modification of its phosphorylation state was observed between the wild-type and the mutant strains. Moreover, at least 16 polypeptides are overexpressed in the mutant, and 6 are repressed. Interestingly, 13 of the 16 polypeptides whose synthesis is enhanced in the mutant were also identified as glucose starvation proteins. The N-terminal amino acid sequences of four of them match sequences deduced from genes coding for l -serine dehydratase, dihydroxyacetone kinase (two genes), and a protein of unknown function from Deinococcus radiodurans.
Materialart:
Online-Ressource
ISSN:
0021-9193
,
1098-5530
DOI:
10.1128/JB.182.20.5799-5806.2000
Sprache:
Englisch
Verlag:
American Society for Microbiology
Publikationsdatum:
2000
ZDB Id:
1481988-0
SSG:
12
