A GMC oxidoreductase homologue is required for acetylation of glycopeptidolipid in Mycobacterium smegmatis.
The Mycobacterium tuberculosis Rv3409c gene is required for modulation of the Toll-like receptor 2 (TLR-2) signaling response in infected macrophages. Although each is annotated as encoding a cholesterol oxidase, neither Rv3409c nor its ortholog MSMEG1604 is required for the metabolism of cholesterol in mycobacteria. Here we report that a unique lipid, L1334, accumulates in a MSMEG1604 transposon mutant in the Mycobacterium smegmatis cell envelope. L1334 is a polar glycopeptidolipid that is hyperrhamnosylated and in which the 6-deoxytalose moiety is not acetylated. The alteration of L1334 acetylation is consistent with a reduced level of interference with TLR-2 signaling in mutant infected macrophages.
Department of Chemistry, Stony Brook University , Stony Brook, New York 11794-3400, United States.
Jin
J
Gao
Nicole S
NS
Sampson
D000107:Acetylation; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D050545:Choline Dehydrogenase / Q000378:metabolism; D005948:Glucose Dehydrogenases / Q000378:metabolism; D006020:Glycopeptides / Q000378:metabolism*; D009154:Mutation; D020102:Mycobacterium smegmatis / Q000235:genetics / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006020:Glycopeptides; D000429:Alcohol Oxidoreductases; D005948:Glucose Dehydrogenases; D050545:Choline Dehydrogenase