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. 1989 Aug 30;163(1):143-8.
doi: 10.1016/0006-291x(89)92111-6.

Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins

H C Rilling  1 , E Bruenger, W W Epstein, A A Kandutsch
Affiliations

Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins

H C Rilling et al. Biochem Biophys Res Commun. .

Abstract

Prenylated amino acid fragments have been isolated from prenylated proteins of Chinese hamster ovary cells. Gel-exclusion chromatography indicates that these proteins are modified by two different prenyl groups. The prenyl-amino acid fragments are labeled by 35S from cysteine, and this bond is cleaved by Raney-Ni, proving that the prenyl residue is linked to protein via a thioether to cysteine. Hydrazinolysis has been used to demonstrate that the cysteine is carboxy terminal.

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