Tan X, Waterham H R, Veenhuis M, Cregg J M
Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000.
J Cell Biol. 1995 Feb;128(3):307-19. doi: 10.1083/jcb.128.3.307.
We previously described the isolation of mutants of the methylotrophic yeast Hansenula polymorpha that are defective in peroxisome biogenesis. Here, we describe the characterization of one of these mutants, per8, and the cloning of the PER8 gene. In either methanol or methylamine medium, conditions that normally induce the organelles, per8 cells contain no peroxisome-like structures and peroxisomal enzymes are located in the cytosol. The sequence of PER8 predicts that its product (Per8p) is a novel polypeptide of 34 kD, and antibodies against Per8p recognize a protein of 31 kD. Analysis of the primary sequence of Per8p revealed a 39-amino-acid cysteine-rich segment with similarity to the C3HC4 family of zinc-finger motifs. Overexpression of PER8 results in a markedly enhanced increase in peroxisome numbers. We show that Per8p is an integral membrane protein of the peroxisome and that it is concentrated in the membranes of newly formed organelles. We propose that Per8p is a component of the molecular machinery that controls the proliferation of this organelle.
我们之前描述过甲醇营养型酵母多形汉逊酵母中过氧化物酶体生物发生存在缺陷的突变体的分离。在此，我们描述其中一个突变体per8的特征以及PER8基因的克隆。在甲醇或甲胺培养基中，即在通常诱导细胞器产生的条件下，per8细胞不含过氧化物酶体样结构，过氧化物酶体酶位于细胞质中。PER8的序列预测其产物（Per8p）是一种34kD的新型多肽，针对Per8p的抗体识别出一种31kD的蛋白质。对Per8p一级序列的分析揭示了一个与锌指基序C3HC4家族相似的富含39个氨基酸的半胱氨酸片段。PER8的过表达导致过氧化物酶体数量显著增加。我们表明Per8p是过氧化物酶体的一种整合膜蛋白，并且它集中在新形成细胞器的膜中。我们提出Per8p是控制该细胞器增殖的分子机制的一个组成部分。
