cDNA cloning and expression of the peptide-binding β subunit of rat p21rasfarnesyltransferase, the counterpart of yeast DPR1/RAM1

Wen Ji Chen, Douglas A. Andres, Joseph L. Goldstein, David W. Russell, Michael S. Brown

Research output: Contribution to journalArticlepeer-review

152 Scopus citations

Abstract

Protein farnesyltransferase is a heterodimeric enzyme that attaches a farnesyl group to cysteine in ras proteins and other membrane-associated proteins. The β subunit contains the recognition site for the peptide substrates, but is inactive in the absence of the α subunit. A cloned cDNA for the rat β subunit predicts a protein of 437 amino acids whose mRNA is present in many tissues. Transfection of the β subunit cDNA produced farnesyltransferase activity in human kidney cells, but only when it was transfected together with a cDNA encoding part of the α subunit. Each of the subunits appeared to be unstable in the transfected cells unless the other subunit was present. The rat β subunit shows 37% sequence identity with the protein encoded by the yeast DPR1/RAM1 gene, indicating that DPR1/RAM1 is the yeast counterpart of the peptide-binding subunit of the mammalian farnesyltransferase.

Original languageEnglish
Pages (from-to)327-334
Number of pages8
JournalCell
Volume66
Issue number2
DOIs
StatePublished - Jul 26 1991

Bibliographical note

Funding Information:
We thankourcolleaguesYuva1 Reissand MiguelSeabrafor invaluable discussions. Jeff Cormier, Gloria Brunschede, and Debbie Noble provided excellent technical assistance. This research was supported by grants from the National Institutes of Health (HL 20948) the Lucille p. Markey Charitable Trust, and the Perot Familv Foundation.

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (all)

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