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Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus.

Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Research Abstract Details 

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  • Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Abstract Text:

    li zhengLi Zheng,chuanxin yuChuanxin Yu,kenneth baylesKenneth Bayles, lasa Lasa,yinduo jiYinduo Ji,

    Our previous studies demonstrated that a putative Staphylococcus aureus glycoprotease (Gcp) is essential for bacterial survival, indicating that Gcp may be a novel target for developing antibacterial agents. However, the biological function of Gcp is unclear. In order to elucidate the reason that Gcp is required for growth, we examined the role of Gcp in bacterial autolysis, which is an important biological process for bacterial growth. Using both a spacp-regulated gcp expression strain and a TetR-regulated gcp antisense expression strain, we found that the down-regulation of gcp expression can effectively inhibit Triton X-100-induced lysis, eliminate penicillin- and vancomycin-caused cell lysis, and dramatically increase tolerance to hydrolases. Moreover, we determined whether resistance to lysis is due to a defect in murein hydrolase activity by using a zymogram analysis. The results showed that the cell lysate of a down-regulated gcp expression mutant displayed several bands of decreased murein hydrolytic activity. Furthermore, we explored the potential mechanism of Gcp's involvement in autolysis and demonstrated that Gcp may function independently from several key autolysins (Atl, LytM, and LytN) and regulators (ArlRS, Mgr/Rat, and CidA). Taken together, the above results indicate that the essential Gcp is involved in the modification of substrates of murein hydrolases as well as in the regulation of expression and/or activity of some murein hydrolases, which, in turn, may play important roles in bacterial viability.

    Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Publishing Authors By Initials

    l zhengL Zheng,c yuC Yu,k baylesK Bayles,i lasaI Lasa,y jiY Ji,

    For similar bacteria: gram-positive bacteria: gram-positive cocci: staphylococcaceae: staphylococcus: staphylococcus aureus research abstracts see: bacteria: gram-positive bacteria: gram-positive cocci: staphylococcaceae: staphylococcus: staphylococcus aureus research

    PUBMED ID PMID:

    MEDLINE DATE:

    Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Journal of bacteriology

    VOLUME: 189

    Page Numbers: 2734-42

    Journal Abbreviation: J. Bacteriol.

    ISSN: 0021-9193

    DAY: 19

    MONTH: 01

    YEAR: 2007

    Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985120

    Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Keywords Mesh Terms:

    KEYWORDS: Staphylococcus aureus

    MESH TERMS: growth & development

    Chemical & Substance for Abstract: Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus. Information

    Substance Name: N-Acetylmuramoyl-L-alanine Amidase

    Registry Number: EC 3.5.1.28

    Grant and Affiliation Information for Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus.

    AFFILIATION: Department of Veterinary and Biomedical Sciences, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Ave., St. Paul, MN 55108, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIAID

    GRANT: AI065740

    ACRONYM: AI

    MEDLINETA: J Bacteriol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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