Abstract:
: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.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Leboeuf C,Leblanc L,Auffray Y,Hartke Adoi
10.1128/jb.182.20.5799-5806.2000keywords:
subject
Has Abstractpub_date
2000-10-01 00:00:00pages
5799-806issue
20eissn
0021-9193issn
1098-5530journal_volume
182pub_type
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更新日期:1985-01-01 00:00:00
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journal_title:Journal of bacteriology
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pub_type: 杂志文章
doi:10.1128/JB.154.1.41-49.1983
更新日期:1983-04-01 00:00:00
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pub_type: 杂志文章
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更新日期:1982-03-01 00:00:00