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多形汉逊酵母中过氧化物酶体过氧化氢酶的靶向信号

Targeting signal of the peroxisomal catalase in the methylotrophic yeast Hansenula polymorpha.

作者信息

Didion T, Roggenkamp R

机构信息

Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Germany.

出版信息

FEBS Lett. 1992 Jun 1;303(2-3):113-6. doi: 10.1016/0014-5793(92)80500-g.

Abstract

The methylotrophic yeast, Hansenula polymorpha, harbours a unique catalase (EC 1.11.1.6), which is essential for growth on methanol as a carbon source and is located in peroxisomes. Its corresponding gene has been cloned and the nucleotide sequence determined. The deduced amino acid sequence displayed the tripeptide serine-lysine-isoleucine at the extreme C-terminus, which is similar to sequences of other peroxisomal targeting signals. Exchange of the ultimate amino acid, isoleucine, of catalase for serine revealed a cytosolic enzyme activity and a concomitant loss of peroxisome function. We concluded that the tripeptide is essential for targeting of catalase in H. polymorpha.

摘要

多形汉逊酵母这种甲基营养型酵母含有一种独特的过氧化氢酶(EC 1.11.1.6),它对于以甲醇作为碳源生长至关重要,且定位于过氧化物酶体中。其相应基因已被克隆并测定了核苷酸序列。推导的氨基酸序列在极端C末端显示出丝氨酸 - 赖氨酸 - 异亮氨酸三肽,这与其他过氧化物酶体靶向信号的序列相似。将过氧化氢酶的末端氨基酸异亮氨酸替换为丝氨酸后,显示出胞质酶活性,并伴随过氧化物酶体功能丧失。我们得出结论,该三肽对于多形汉逊酵母中过氧化氢酶的靶向定位至关重要。

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