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Pex19p, a Farnesylated Protein Essential for Peroxisome Biogenesis
Author(s) -
Klaudia Götte,
Wolfgang Girzalsky,
Michael Linkert,
Evelyn Baumgart,
Stefan Kammerer,
WolfHubert Kunau,
Ralf Erdmann
Publication year - 1998
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.18.1.616
Subject(s) - prenylation , peroxisome , biology , biogenesis , biochemistry , peroxisomal targeting signal , cytosol , peptide sequence , microbiology and biotechnology , protein targeting , saccharomyces cerevisiae , immunoprecipitation , membrane protein , gene , enzyme , membrane
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.

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