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 Microbioljournal_title
Current microbiologyauthors
Le Hénaff M,Chollet A,Fontenelle Cdoi
10.1007/s002840010332keywords:
subject
Has Abstractpub_date
2001-12-01 00:00:00pages
424-8issue
6eissn
0343-8651issn
1432-0991journal_volume
43pub_type
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