| Characterization of Listeria monocytogenes protein Lmo0327 with murein hydrolase activity. | |
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MedLine Citation:
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PMID: 16763838 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Listeria monocytogenes is an ubiquitous gram-positive, opportunistic food-borne human and animal pathogen. To date, five L. monocytogenes autolysins have been characterized: p60, p45, Ami, MurA and Auto and the preliminary results of our studies show that FlaA, a flagellar protein of L. monocytogenes, also has murein-degrading activity. In this study, a gene coding a 144 kDa protein (Lmo0327) with murein hydrolase activity was identified from a lambda Zap expression library of L. monocytogenes EGD genomic DNA, using a direct screening protocol involving the plating of infected Escherichia coli XL1-blue MRF' cells onto medium containing Bacillus subtilis murein, a substrate for autolytic proteins. Protein Lmo0327 has a signal sequence, a N-terminal LRR domain and a C-terminal wall-anchoring LPXTG motif. In order to examine the roles of this enzyme and the putative transcription regulator coded by gene lmo0326 located upstream of lmo0327, both structural genes were insertionally inactivated by site-specific integration of a temperature-sensitive plasmid. We show that Lmo0327 is a surface protein covalently linked to murein and that the putative transcription regulator Lmo0326 can be assumed to positively regulate the expression of gene lmo0327. The enzyme, which we have shown to have murein-hydrolysing activity, plays a role in cell separation and murein turnover. |
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Authors:
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Magdalena Popowska; Zdzislaw Markiewicz |
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Publication Detail:
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Type: Journal Article Date: 2006-06-09 |
Journal Detail:
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Title: Archives of microbiology Volume: 186 ISSN: 0302-8933 ISO Abbreviation: Arch. Microbiol. Publication Date: 2006 Jul |
Date Detail:
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Created Date: 2006-07-10 Completed Date: 2007-06-19 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0410427 Medline TA: Arch Microbiol Country: Germany |
Other Details:
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Languages: eng Pagination: 69-86 Citation Subset: IM |
Affiliation:
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Department of General Microbiology, Institute of Microbiology, Warsaw University, Miecznikowa 1, 02-096 Warsaw, Poland. magdapop@biol.uw.edu.pl |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Base Sequence Cell Wall / enzymology Cloning, Molecular DNA, Bacterial / genetics Listeria monocytogenes / enzymology*, genetics Models, Molecular Molecular Sequence Data N-Acetylmuramoyl-L-alanine Amidase / genetics, metabolism* Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins / biosynthesis, genetics Regulatory Elements, Transcriptional Transcription, Genetic |
| Chemical | |
Reg. No./Substance:
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0/DNA, Bacterial; 0/Recombinant Proteins; EC 3.5.1.28/N-Acetylmuramoyl-L-alanine Amidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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