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Journal of Bacteriology, October 2000, p. 5799-5806, Vol. 182, No. 20
Unité de Microbiologie de
l'Environnement, Unité soutenue par l'INRA, IRBA,
Université de Caen, 14032 Caen Cedex, France
Received 30 May 2000/Accepted 26 July 2000
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.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Characterization of the ccpA Gene of
Enterococcus faecalis: Identification of
Starvation-Inducible Proteins Regulated by CcpA
*
Corresponding author. Mailing address: Unité de
Microbiologie de l'Environnement, Unité soutenue par l'INRA,
IRBA, Université de Caen, 14032 Caen Cedex, France. Phone:
(33)-2-31-56-59-30. Fax: (33)-2-31-56-53-11. E-mail:
phdlme{at}ibba.unicaen.fr.
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