Source:http://linkedlifedata.com/resource/pubmed/id/20637039
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-8-11
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pubmed:abstractText |
The disaccharide d-N-acetylglucosamine-l-rhamnose plays an important role in the mycobacterial cell wall as a linker connecting arabinogalactan and peptidoglycan via a phosphodiester linkage. The first step of the disaccharide linker is the formation of decaprenyl phosphate-GlcNAc, which is catalyzed by GlcNAc-1-phosphate transferase. In Gram-negative bacteria, the wecA gene specifies the UDP-GlcNAc: undecaprenyl phosphate GlcNAc-1-phosphate transferase (WecA), which catalyzes the first step in the biosynthesis of lipopolysaccharide O-antigen. Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 show homology to Escherichia coli WecA protein. We cloned Rv1302 and MSMEG_4947 and introduced plasmids pYJ-1 (carrying Rv1302) and pYJ-2 (carrying MSMEG_4947) into a wecA-defective strain of E. coli MV501, respectively. Lipopolysaccharide analysis demonstrated that lipopolysaccharide synthesis in MV501 (pYJ-1) and MV501 (pYJ-2) was restored upon complementation with Rv1302 and MSMEG_4947, respectively. This provides the first evidence that Rv1302 and MSMEG_4947 have the same function as E. coli WecA. We also generated an M. smegmatis MSMEG_4947 knockout mutant using a homologous recombination strategy. The disruption of MSMEG_4947 in the M. smegmatis genome resulted in the loss of viability at a nonpermissive temperature. Scanning electron microscopy and transmission electron microscopy results showed that the lack of the MSMEG_4947 protein causes drastic morphological changes in M. smegmatis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases (Other Substituted...,
http://linkedlifedata.com/resource/pubmed/chemical/rfe protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1574-6968
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
310
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
54-61
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pubmed:meshHeading |
pubmed-meshheading:20637039-Bacterial Proteins,
pubmed-meshheading:20637039-Escherichia coli,
pubmed-meshheading:20637039-Escherichia coli Proteins,
pubmed-meshheading:20637039-Gene Deletion,
pubmed-meshheading:20637039-Genes, Essential,
pubmed-meshheading:20637039-Genetic Complementation Test,
pubmed-meshheading:20637039-Microbial Viability,
pubmed-meshheading:20637039-Microscopy, Electron, Scanning,
pubmed-meshheading:20637039-Microscopy, Electron, Transmission,
pubmed-meshheading:20637039-Mycobacterium smegmatis,
pubmed-meshheading:20637039-Mycobacterium tuberculosis,
pubmed-meshheading:20637039-Plasmids,
pubmed-meshheading:20637039-Sequence Homology, Amino Acid,
pubmed-meshheading:20637039-Transferases (Other Substituted Phosphate Groups)
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pubmed:year |
2010
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pubmed:articleTitle |
Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Dalian Medical University, 9 W. Lushun South Road, Dalian, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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