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CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus.

CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Research Abstract Details 

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  • CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Abstract Text:

    asiya a gusaAsiya A Gusa,barbara j froehlichBarbara J Froehlich,devak desaiDevak Desai,virginia stringerVirginia Stringer,june r scottJune R Scott,

    CovR, the two-component response regulator of Streptococcus pyogenes (group A streptococcus [GAS]) directly or indirectly represses about 15% of the genome, including genes encoding many virulence factors and itself. Transcriptome analyses also showed that some genes are activated by CovR. We asked whether the regulation by CovR of one of these genes, dppA, the first gene in an operon encoding a dipeptide permease, is direct or indirect. Direct regulation by CovR was suggested by the presence of five CovR consensus binding sequences (CBs) near the putative promoter. In this study, we identified the 5' end of the dppA transcript synthesized in vivo and showed that the start of dppA transcription in vitro is the same. We found that CovR binds specifically to the dppA promoter region (PdppA) in vitro with an affinity similar to that at which it binds to other CovR-regulated promoters. Disruption of any of the five CBs by a substitution of GG for TT inhibited CovR binding to that site in vitro, and binding at two of the CBs appeared cooperative. In vivo, CovR activation of transcription was not affected by individual mutations of any of the four CBs that we could study. This suggests that the binding sites are redundant in vivo. In vitro, CovR did not activate transcription from PdppA in experiments using purified GAS RNA polymerase and either linear or supercoiled DNA template. Therefore, we propose that in vivo, CovR may interfere with the binding of a repressor of PdppA.

    CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Publishing Authors By Initials

    aa gusaAA Gusa,bj froehlichBJ Froehlich,d desaiD Desai,v stringerV Stringer,jr scottJR Scott,

    For similar bacteria: gram-positive bacteria: gram-positive cocci: streptococcaceae: streptococcus: streptococcus pyogenes research abstracts see: bacteria: gram-positive bacteria: gram-positive cocci: streptococcaceae: streptococcus: streptococcus pyogenes research

    PUBMED ID PMID:

    MEDLINE DATE:

    CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of bacteriology

    VOLUME: 189

    Page Numbers: 1407-16

    Journal Abbreviation: J. Bacteriol.

    ISSN: 0021-9193

    DAY: 22

    MONTH: 09

    YEAR: 2006

    CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985120

    CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Keywords Mesh Terms:

    KEYWORDS: Streptococcus pyogenes

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus. Information

    Substance Name: oligopeptide permease, Bacteria

    Registry Number: 39335-07-4

    Grant and Affiliation Information for CovR activation of the dipeptide permease promoter (PdppA) in Group A Streptococcus.

    AFFILIATION: Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIAID

    GRANT: T32-AI07470

    ACRONYM: AI

    MEDLINETA: J Bacteriol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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