Modification of glycopeptidolipids by an O-methyltransferase of Mycobacterium smegmatis
Glycopeptidolipids (GPLs) are a major component of the outer layers of the cell walls of several non-tuberculous mycobacteria. The Mycobacterium smegmatis GPLs consist of a diglycosylated lipopeptide core which is variably modified by acetylation and methylation. Analysis of a region of the M. smegm...
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| Vydané v: | Microbiology (Society for General Microbiology) Ročník 148; číslo Pt 10; s. 3079 |
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| Hlavní autori: | , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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England
01.10.2002
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| ISSN: | 1350-0872 |
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| Abstract | Glycopeptidolipids (GPLs) are a major component of the outer layers of the cell walls of several non-tuberculous mycobacteria. The Mycobacterium smegmatis GPLs consist of a diglycosylated lipopeptide core which is variably modified by acetylation and methylation. Analysis of a region of the M. smegmatis chromosome, upstream of the peptide synthetase gene, mps, revealed a GPL biosynthetic locus containing genes potentially involved in glycosylation, methylation, acetylation and transport of GPLs. Methyltransferases are required to modify rhamnose and the fatty acid of GPLs. Of the four methyltransferases encoded within the locus, one methyltransferase, Mtf2, was unlike sugar methyltransferases from other species. An mtf2 mutant was created and was shown to be unable to methylate the GPL fatty acids. Direct evidence is presented that Mtf2 is a methyltransferase that modifies the GPL fatty acid. |
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| AbstractList | Glycopeptidolipids (GPLs) are a major component of the outer layers of the cell walls of several non-tuberculous mycobacteria. The Mycobacterium smegmatis GPLs consist of a diglycosylated lipopeptide core which is variably modified by acetylation and methylation. Analysis of a region of the M. smegmatis chromosome, upstream of the peptide synthetase gene, mps, revealed a GPL biosynthetic locus containing genes potentially involved in glycosylation, methylation, acetylation and transport of GPLs. Methyltransferases are required to modify rhamnose and the fatty acid of GPLs. Of the four methyltransferases encoded within the locus, one methyltransferase, Mtf2, was unlike sugar methyltransferases from other species. An mtf2 mutant was created and was shown to be unable to methylate the GPL fatty acids. Direct evidence is presented that Mtf2 is a methyltransferase that modifies the GPL fatty acid.Glycopeptidolipids (GPLs) are a major component of the outer layers of the cell walls of several non-tuberculous mycobacteria. The Mycobacterium smegmatis GPLs consist of a diglycosylated lipopeptide core which is variably modified by acetylation and methylation. Analysis of a region of the M. smegmatis chromosome, upstream of the peptide synthetase gene, mps, revealed a GPL biosynthetic locus containing genes potentially involved in glycosylation, methylation, acetylation and transport of GPLs. Methyltransferases are required to modify rhamnose and the fatty acid of GPLs. Of the four methyltransferases encoded within the locus, one methyltransferase, Mtf2, was unlike sugar methyltransferases from other species. An mtf2 mutant was created and was shown to be unable to methylate the GPL fatty acids. Direct evidence is presented that Mtf2 is a methyltransferase that modifies the GPL fatty acid. Glycopeptidolipids (GPLs) are a major component of the outer layers of the cell walls of several non-tuberculous mycobacteria. The Mycobacterium smegmatis GPLs consist of a diglycosylated lipopeptide core which is variably modified by acetylation and methylation. Analysis of a region of the M. smegmatis chromosome, upstream of the peptide synthetase gene, mps, revealed a GPL biosynthetic locus containing genes potentially involved in glycosylation, methylation, acetylation and transport of GPLs. Methyltransferases are required to modify rhamnose and the fatty acid of GPLs. Of the four methyltransferases encoded within the locus, one methyltransferase, Mtf2, was unlike sugar methyltransferases from other species. An mtf2 mutant was created and was shown to be unable to methylate the GPL fatty acids. Direct evidence is presented that Mtf2 is a methyltransferase that modifies the GPL fatty acid. |
| Author | Jeevarajah, Dharshini Billman-Jacobe, Helen Patterson, John H McConville, Malcolm J |
| Author_xml | – sequence: 1 givenname: Dharshini surname: Jeevarajah fullname: Jeevarajah, Dharshini organization: Departments of Microbiology and Immunology1, and Biochemistry and Molecular Biology2, University of Melbourne, Victoria 3010, Australia – sequence: 2 givenname: John H surname: Patterson fullname: Patterson, John H organization: Departments of Microbiology and Immunology1, and Biochemistry and Molecular Biology2, University of Melbourne, Victoria 3010, Australia – sequence: 3 givenname: Malcolm J surname: McConville fullname: McConville, Malcolm J organization: Departments of Microbiology and Immunology1, and Biochemistry and Molecular Biology2, University of Melbourne, Victoria 3010, Australia – sequence: 4 givenname: Helen surname: Billman-Jacobe fullname: Billman-Jacobe, Helen organization: Departments of Microbiology and Immunology1, and Biochemistry and Molecular Biology2, University of Melbourne, Victoria 3010, Australia |
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| Snippet | Glycopeptidolipids (GPLs) are a major component of the outer layers of the cell walls of several non-tuberculous mycobacteria. The Mycobacterium smegmatis GPLs... |
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| SubjectTerms | Amino Acid Motifs Amino Acid Sequence Bacterial Proteins - genetics Bacterial Proteins - metabolism Gas Chromatography-Mass Spectrometry Gene Deletion Genetic Complementation Test Glycolipids - chemistry Glycolipids - metabolism Glycopeptides - chemistry Glycopeptides - metabolism Methylation Methyltransferases - genetics Methyltransferases - metabolism Molecular Sequence Data Multigene Family Mycobacterium smegmatis - enzymology Mycobacterium smegmatis - genetics Sequence Analysis, DNA Spectrometry, Mass, Electrospray Ionization |
| Title | Modification of glycopeptidolipids by an O-methyltransferase of Mycobacterium smegmatis |
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