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PMID: 9352913 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Catabolite repression in Lactobacillus casei ATCC 393 is mediated by CcpA.

Journal of bacteriology ·Vol. 179 ·No. 21 ·1997-11-00 ·Pages 6657-64

Monedero V, Gosalbes MJ, Pérez-Martínez G

Abstract

The chromosomal ccpA gene from Lactobacillus casei ATCC 393 has been cloned and sequenced. It encodes the CcpA protein, a central catabolite regulator belonging to the LacI-GalR family of bacterial repressors, and shows 54% identity with CcpA proteins from Bacillus subtilis and Bacillus megaterium. The L. casei ccpA gene was able to complement a B. subtilis ccpA mutant. An L. casei ccpA mutant showed increased doubling times and a relief of the catabolite repression of some enzymatic activities, such as N-acetylglucosaminidase and phospho-beta-galactosidase. Detailed analysis of CcpA activity was performed by using the promoter region of the L. casei chromosomal lacTEGF operon which is subject to catabolite repression and contains a catabolite responsive element (cre) consensus sequence. Deletion of this cre site or the presence of the ccpA mutation abolished the catabolite repression of a lacp::gusA fusion. These data support the role of CcpA as a common regulatory element mediating catabolite repression in low-GC-content gram-positive bacteria.

MeSH Terms
Acetylglucosaminidase/biosynthesis Amino Acid Sequence Bacillus subtilis/genetics Bacterial Proteins Base Sequence Cloning, Molecular DNA-Binding Proteins/genetics Enzyme Repression Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic Genetic Complementation Test Glycoside Hydrolases Gram-Positive Bacteria/genetics Lac Operon/genetics Lactobacillus casei/genetics Molecular Sequence Data Mutagenesis Repressor Proteins/genetics Sequence Analysis, DNA Sequence Homology, Amino Acid Transcription, Genetic beta-Galactosidase/biosynthesis
Chemicals
Bacterial Proteins DNA-Binding Proteins Repressor Proteins catabolite control proteins, bacteria Glycoside Hydrolases beta-Galactosidase Acetylglucosaminidase 6-phospho-beta-galactosidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Monedero V
Departamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos, Burjassot, Valencia, Spain.
Gosalbes M J
Pérez-Martínez G
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1997-11-00
Pages
6657-64
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC179592
Subset
IM
Databases
GENBANK
AJ003194, U28137
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