Chemical analysis of lipid-modified membrane proteins in Acholeplasma laidlawii.

Abstract:

:The lipid modification of membrane proteins was investigated in Acholeplasma laidlawii by metabolic labeling and by chemical analysis. A S-glycerylcysteine residue was identified from membrane proteins and we reported the strong preference for saturated acyl chains into the lipid modification. Differential release of fatty acids revealed a ratio [(O-ester- + amide-bound acyl chains)/O-ester-linked chains] close to 1.1 which suggests the involvement of only two O-ester linked fatty acids in the acylation process. Present data indicate that acyl proteins in A. laidlawii are true lipoproteins (mainly diacylated) probably processed by a mechanism analogous to that described for eubacteria and other mycoplasmas.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Le Hénaff M,Chollet A,Fontenelle C

doi

10.1007/s002840010332

keywords:

subject

Has Abstract

pub_date

2001-12-01 00:00:00

pages

424-8

issue

6

eissn

0343-8651

issn

1432-0991

journal_volume

43

pub_type

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