Fatty acylation of polypeptides in the nematode Caenorhabditis elegans.
Covalent modification of eucaryotic proteins, involving addition of fatty acyl groups, is a widespread phenomenon. Here we describe the occurrence of this form of covalent modification in the free-living nematode, Caenorhabditis elegans. Following incubation in the presence of either [3H]-myristic acid or [3H]-palmitic acid, specific C. elegans polypeptides became labelled. Chemical analysis revealed that following incubation of C. elegans with [3H]-myristic acid, polypeptides became labelled with myristoyl, palmitoyl or stearoyl moieties; after incubation with [3H]-palmitic acid, palmitoyl or stearoyl moieties were incorporated into polypeptides. Fatty acyl groups were linked to target polypeptides, predominantly through alkali-labile thioester or ester linkages and acid-labile amide linkages. Where myristoylation involved an amide linkage, the modified amino acid was usually glycine. Preliminary immunological evidence indicated that heterotrimeric GTP-binding protein alpha subunit(s) are possible target(s) for acylation in C. elegans.
Aspbury
R A
RA
Department of Biochemistry, University of Liverpool, UK.
Fisher
M J
MJ
Rees
H H
HH
D000215:Acylation; D000818:Animals; D017173:Caenorhabditis elegans / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D015801:Helminth Proteins / Q000302:isolation & purification / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D019814:Myristic Acid / Q000378:metabolism*; D019308:Palmitic Acid / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013229:Stearic Acids / Q000378:metabolism; D014316:Tritium
D015801:Helminth Proteins; D010455:Peptides; D013229:Stearic Acids; D019814:Myristic Acid; D014316:Tritium; D019308:Palmitic Acid; C031183:stearic acid; D007930:Leucine