The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells--the PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family.
The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells--the PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family.
复制标题
Pichia pastoris的PAS8突变体表现出Zellweger综合征细胞的过氧化物酶体进口缺乏 - PAS8蛋白与COOH-末端三肽过氧化物酶体靶向信号结合，并且是TPR蛋白家族的成员。
DOI：
10.1083/jcb.121.4.761
复制
发表时间：
1993-05
影响因子：
7.8
通讯作者：
Subramani, S
中科院分区：
文献类型：
--
作者：
McCollum, D;Monosov, E;Subramani, S
我们先前描述了分离出缺乏过氧化酶体组装的毕赤酵母突变株(PAS突变体)。我们描述了其中一个突变体PAS8的特征，以及PAS8基因的克隆。Pas8突变体不能生长，但不能分裂或分离过氧化物体，也不能诱导过氧化物体蛋白。两种不同的过氧化体靶向信号PTS1和PTS2已被鉴定，它们足以将蛋白质定向到过氧体基质中。我们发现，pas8突变体在导入具有PTS1靶向信号的蛋白质方面存在缺陷，但不存在PTS2靶向信号。这与在致命性人类过氧素体疾病Zellweger综合征患者的细胞中发现的进口缺陷相同。PAS8基因的克隆和序列分析表明，它是四肽重复基因家族中的一个新成员。针对细菌表达的PAS8产生的抗体被用来证明PAS8是一种过氧体，膜相关蛋白。此外，我们还发现，在体外翻译的PAS8蛋白能够特异性地结合PTS1靶向信号，从而增加了PAS8是PTS1受体的可能性。
We previously described the isolation of mutants of the yeast Pichia pastoris that are deficient in peroxisome assembly (pas mutants). We describe the characterization of one of these mutants, pas8, and the cloning of the PAS8 gene. The pas8 mutant is deficient for growth, but not for division or segregation of peroxisomes, or for induction of peroxisomal proteins. Two distinct peroxisomal targeting signals, PTS1 and PTS2, have been identified that are sufficient to direct proteins to the peroxisomal matrix. We show that the pas8 mutant is deficient in the import of proteins with the PTS1, but not the PTS2, targeting signal. This is the same import deficiency as that found in cells from patients with the lethal human peroxisomal disorder Zellweger syndrome. Cloning and sequencing of the PAS8 gene reveals that it is a novel member of the tetratricopeptide repeat gene family. Antibodies raised against bacterially expressed PAS8 are used to show that PAS8 is a peroxisomal, membrane-associated protein. Also, we have found that in vitro translated PAS8 protein is capable of binding the PTS1 targeting signal specifically, raising the possibility that PAS8 is a PTS1 receptor.