cDNA cloning and expression of the α and β subunits of rat rab geranylgeranyl transferase

Scott A. Armstrong, Miguel C. Seabra, Thomas C. Südhof, Joseph L. Goldstein, Michael S. Brown

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Abstract

Rab geranylgeranyl transferasse (Rab GG transferase) attaches 20-carbon geranylgeranyl groups to cysteine residues in Rab proteins that contain the COOH-terminal sequence Cys-X-Cys or Cys-Cys. Rab GG transferase consists of two components that are separable in high salt solutions. Component A is a 95-kDa protein, and Component B is a heterodimer consisting of a 60-kDa α subunit and a 38-kDa β subunit. In the current paper, we have cloned cDNAs for the α and β subunits of Component B. The cDNAs for the rat α and β subunits predict proteins of 567 and 331 amino acids, respectively. The mRNAs for both subunits are expressed in many tissues. When transfected together in embryonic kidney 293 cells, the α and β subunit cDNAs produced Rab GG transferase activity that was stimulated in vitro by the addition of purified Component A. Comparisons of the amino acid sequences suggest that the proteins encoded by the Saccharomyces cerevisiae genes MAD2 and BET2 are the yeast counterparts of the mammalian Rab GG transferase α and β subunits, respectively.

Original languageEnglish (US)
Pages (from-to)12221-12229
Number of pages9
JournalJournal of Biological Chemistry
Volume268
Issue number16
Publication statusPublished - Jun 5 1993

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ASJC Scopus subject areas

  • Biochemistry

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