Chemical analysis of lipid-modified membrane proteins in Acholeplasma laidlawii.
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.
Le Hénaff
M
M
UMR CNRS 6026, Groupe Membranes et Osmorégulation, Université de Rennes 1, Campus de Beaulieu, F-35042 Rennes Cedex, France. m-lehenaff@enitab.fr
Chollet
A
A
Fontenelle
C
C
D000128:Acholeplasma laidlawii / Q000737:chemistry / Q000378:metabolism*; D005227:Fatty Acids / Q000032:analysis*; D008563:Membrane Lipids / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry*; D019308:Palmitic Acid / Q000378:metabolism
D005227:Fatty Acids; D008563:Membrane Lipids; D008565:Membrane Proteins; D019308:Palmitic Acid