Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins.
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.
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City.
H C
HC
Rilling
E
E
Bruenger
W W
WW
Epstein
A A
AA
Kandutsch
D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003545:Cysteine; D004987:Ethers; D008798:Mevalonic Acid / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins; D013729:Terpenes / Q000378:metabolism*
D004987:Ethers; D011506:Proteins; D013729:Terpenes; D003545:Cysteine; D008798:Mevalonic Acid