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Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases.

Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Research Abstract Details 

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  • Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Abstract Text:

    emina a stojkovi?Emina A Stojkovi?,lucia b rothman-denesLucia B Rothman-Denes,

    Escherichia coli phage N4 infection leads to delayed host cell lysis, 3000 particles per infected bacterium and a small plaque phenotype. We show that bacteriophage N4 encodes a murein hydrolase (gp61) that is essential for N4 plaque-forming ability. gp61 has a high level of sequence similarity to hypothetical proteobacterial proteins, and Vibrio harveyi phage VHML ORF 19. Nano-electrospray ionization (nESI) quadrupole ion trap (QIT) mass spectrometry (MS) analysis of muropeptides from purified gp61 digestion of E. coli peptidoglycan indicates that gp61 is an N-acetylmuramidase. The EGGY motif present near the N terminus of gp61 and its homologs contains the glutamic acid residue essential for enzymatic activity. These results provide evidence that N4 gp61 and its homologs define a new family of N-acetylmuramidases (pfam05838.4, DUF847, COG3926). In contrast to its homologs, gp61 contains an N-terminal signal sequence. When expressed at levels present during phage infection, gp61 localizes primarily to the cell inner membrane; in contrast, over-expression of recombinant N4 gp61 is sufficient for rapid cell lysis. Overproduction of the recombinant Salmonella typhimurium (STM0016) homolog is sufficient for cell lysis only when fused to the gp61 N-terminal signal sequence. The results of subcellular localization and of mutagenesis of the gp61 N-terminal signal sequence indicate that gp61 must be released from the inner membrane to be catalytically active.

    Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Publishing Authors By Initials

    ea stojkovi?EA Stojkovi?,lb rothman-denesLB Rothman-Denes,

    For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Journal Published:

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

    Journal: Journal of molecular biology

    VOLUME: 366

    Page Numbers: 406-19

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 0022-2836

    DAY: 11

    MONTH: 11

    YEAR: 2006

    Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985088

    Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Keywords Mesh Terms:

    KEYWORDS: Viral Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. Information

    Substance Name: N-Acetylmuramoyl-L-alanine Amidase

    Registry Number: EC 3.5.1.28

    Grant and Affiliation Information for Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases.

    AFFILIATION: Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NIAID

    GRANT: R01 AI12575

    ACRONYM: AI

    MEDLINETA: J Mol Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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