Methylation of GPLs in Mycobacterium smegmatis and Mycobacterium avium

Several species of mycobacteria express abundant glycopeptidolipids (GPLs) on the surfaces of their cells. The GPLs are glycolipids that contain modified sugars including acetylated 6-deoxy-talose and methylated rhamnose. Four methyltransferases have been implicated in the synthesis of the GPLs of M...

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Vydané v:Journal of bacteriology Ročník 186; číslo 20; s. 6792
Hlavní autori: Jeevarajah, Dharshini, Patterson, John H, Taig, Ellen, Sargeant, Tobias, McConville, Malcolm J, Billman-Jacobe, Helen
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 01.10.2004
Predmet:
Amino Acid Sequence
Genetic Complementation Test
Glycolipids - metabolism
Glycopeptides - metabolism
Methylation
Methyltransferases - chemistry
Methyltransferases - genetics
Methyltransferases - metabolism
Molecular Sequence Data
Mutation
Mycobacterium avium - enzymology
Mycobacterium avium - genetics
Mycobacterium avium - metabolism
Mycobacterium smegmatis - enzymology
Mycobacterium smegmatis - genetics
Mycobacterium smegmatis - metabolism
Rhamnose - metabolism
Sequence Analysis, DNA
ISSN:0021-9193
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Shrnutí:Several species of mycobacteria express abundant glycopeptidolipids (GPLs) on the surfaces of their cells. The GPLs are glycolipids that contain modified sugars including acetylated 6-deoxy-talose and methylated rhamnose. Four methyltransferases have been implicated in the synthesis of the GPLs of Mycobacterium smegmatis and Mycobacterium avium. A rhamnosyl 3-O-methytransferase and a fatty acid methyltransferase of M. smegmatis have been previously characterized. In this paper, we characterize the methyltransferases that are responsible for modifying the hydroxyl groups at positions 2 and 4 of rhamnose and propose the biosynthetic sequence of GPL trimethylrhamnose formation. The analysis of M. avium genes through the creation of specific mutants is technically difficult; therefore, an alternative approach to determine the function of putative methyltransferases of M. avium was undertaken. Complementation of M. smegmatis methyltransferase mutants with M. avium genes revealed that MtfC and MtfB of the latter species have 4-O-methyltransferase activity and that MtfD is a 3-O-methyltransferase which can modify rhamnose of GPLs in M. smegmatis.
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ISSN:0021-9193
DOI:10.1128/JB.186.20.6792-6799.2004