Pex19p, a farnesylated protein essential for peroxisome biogenesis

Mol Cell Biol. 1998 Jan;18(1):616-28. doi: 10.1128/MCB.18.1.616.


We report the identification and molecular characterization of Pex19p, an oleic acid-inducible, farnesylated protein of 39.7 kDa that is essential for peroxisome biogenesis in Saccharomyces cerevisiae. Cells lacking Pex19p are characterized by the absence of morphologically detectable peroxisomes and mislocalization of peroxisomal matrix proteins to the cytosol. The human HK33 gene product was identified as the putative human ortholog of Pex19p. Evidence is provided that farnesylation of Pex19p takes place at the cysteine of the C-terminal CKQQ amino acid sequence. Farnesylation of Pex19p was shown to be essential for the proper function of the protein in peroxisome biogenesis. Pex19p was shown to interact with Pex3p in vivo, and this interaction required farnesylation of Pex19p.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Fungal Proteins / physiology*
  • Gene Expression Regulation, Fungal
  • Humans
  • Membrane Proteins / genetics*
  • Microbodies / physiology*
  • Molecular Sequence Data
  • PHEX Phosphate Regulating Neutral Endopeptidase
  • Proteins / genetics
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment


  • Fungal Proteins
  • Membrane Proteins
  • PEX19 protein, S cerevisiae
  • Proteins
  • Saccharomyces cerevisiae Proteins
  • PHEX Phosphate Regulating Neutral Endopeptidase
  • PHEX protein, human