Cloning and expression of a cDNA encoding the α subunit of rat p21ras protein farnesyltransferase

W. J. Chen, D. A. Andres, J. L. Goldstein, M. S. Brown

Research output: Contribution to journalArticlepeer-review

98 Scopus citations

Abstract

The complete amino acid sequence of the a subunit of heterodimeric p21ras protein farnesyltransferase from rat has been deduced from the sequence of a cloned cDNA. The cDNA encodes a 377-amino acid protein that migrates on NaDodSO4/polyacrylamide gels identically to the α subunit purified from rat brain. When introduced into mammalian cells by transfection, the cDNA for the α subunit produced no immunodetectable protein or farnesyltransferase activity unless the cells were simultaneously transfected with a cDNA encoding β subunit. In light of previous evidence that α subunit forms a heterodimer with at least two different β subunits, current data suggest a mechanism for coordinating amounts of α and β subunits. If an α subunit were stable only as a complex with a β subunit, the number of α subunits would be automatically maintained at a level just sufficient to balance all β subunits, thereby avoiding the potentially toxic overaccumulation of free α subunits.

Original languageEnglish
Pages (from-to)11368-11372
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number24
StatePublished - 1991

Keywords

  • Covalent modification
  • Heterodimeric enzymes
  • Protein isoprenylation

ASJC Scopus subject areas

  • General

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