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 journalArticle

146 Citations (Scopus)

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

Fingerprint

Cloning
Yeast
Farnesyltranstransferase
Rats
Organism Cloning
Complementary DNA
Yeasts
Peptides
ras Proteins
Fungal Proteins
Human Activities
Transfection
Cysteine
Membrane Proteins
Proteins
Genes
Tissue
Kidney
Amino Acids
Messenger RNA

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

cDNA cloning and expression of the peptide-binding β subunit of rat p21rasfarnesyltransferase, the counterpart of yeast DPR1/RAM1. / Chen, Wen Ji; Andres, Douglas A.; Goldstein, Joseph L.; Russell, David W.; Brown, Michael S.

In: Cell, Vol. 66, No. 2, 26.07.1991, p. 327-334.

Research output: Contribution to journalArticle

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AU - Brown, Michael S.

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