Pex19p，一种对过氧化物酶体生物发生至关重要的法尼基化蛋白。
Pex19p, a farnesylated protein essential for peroxisome biogenesis.
作者信息
Götte K, Girzalsky W, Linkert M, Baumgart E, Kammerer S, Kunau W H, Erdmann R
机构信息
Institut für Physiologische Chemie, Ruhr-Universität Bochum, Germany.
出版信息
Mol Cell Biol. 1998 Jan;18(1):616-28. doi: 10.1128/MCB.18.1.616.
Abstract
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.
摘要
我们报告了Pex19p的鉴定和分子特征，它是一种39.7 kDa的油酸诱导型、法尼基化蛋白，对酿酒酵母中的过氧化物酶体生物发生至关重要。缺乏Pex19p的细胞的特征是没有形态上可检测到的过氧化物酶体，并且过氧化物酶体基质蛋白错误定位于细胞质中。人类HK33基因产物被鉴定为Pex19p的推定人类同源物。有证据表明，Pex19p的法尼基化发生在C末端CKQQ氨基酸序列的半胱氨酸处。Pex19p的法尼基化被证明对该蛋白在过氧化物酶体生物发生中的正常功能至关重要。Pex19p在体内被证明与Pex3p相互作用，并且这种相互作用需要Pex19p的法尼基化。
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