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Biochim Biophys Acta. 1998 Oct 2;1394(1):90-8.

Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation.

Author information

1
Institut für Immunologie und Molekularbiologie, Fachbereich Veterinärmedizin der Freien Universität Berlin, Luisenstrasse 56, D-10117 Berlin, Germany.

Erratum in

  • Biochim Biophys Acta 1999 Jan 4;1436(3):630.

Abstract

Protein palmitoylation in vitro was studied using bovine rhodopsin as the substrate and a partially purified acylating enzymatic activity (PAT) from placental membranes. PAT incorporates fatty acid into rhodopsin with higher efficiency (10 times higher initial rate), as compared to autoacylation. The activity is sensitive to heat and trypsin, indicating a protein-mediated enzymatic process and requires the native conformation of rhodopsin. The presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT. The sites for non-enzymatic and enzymatic palmitoylation could not be distinguished by peptide mapping. The reversible palmitoylation described here will provide a tool for the study of the role of palmitoylation in photoreceptor function.

PMID:
9767130
DOI:
10.1016/s0005-2760(98)00097-6
[Indexed for MEDLINE]

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