The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues.
The yeast SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) protein Ykt6 was shown to mediate palmitoylation of the fusion factor Vac8 in a reaction essential for the fusion of vacuoles. Here I present evidence that hYkt6 (human Ykt6) has self-palmitoylating activity. Incubation of recombinant hYkt6 with [3H]Pal-CoA ([3H]palmitoyl-CoA) leads to covalent attachment of palmitate to C-terminal cysteine residues. The N-terminal domain of human Ykt6 contains a Pal-CoA binding site and is required for the reaction.
Department of Immunology and Molecular Biology, Vet.-Med. Faculty, Free University Berlin, Philippstrasse 13, 10115 Berlin, Federal Republic of Germany. mveit@city.vetmed.fu-berlin.de
Michael
M
Veit
D000595:Amino Acid Sequence; D002460:Cell Line; D003545:Cysteine / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D019308:Palmitic Acid / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D050683:R-SNARE Proteins
D008565:Membrane Proteins; D010455:Peptides; D050683:R-SNARE Proteins; C491482:YKT6 protein, human; D019308:Palmitic Acid; D003545:Cysteine