西瓜乙醛酸循环体苹果酸脱氢酶被分选到甲基营养型酵母多形汉逊酵母的过氧化物酶体中。

Watermelon glyoxysomal malate dehydrogenase is sorted to peroxisomes of the methylotrophic yeast, Hansenula polymorpha.

作者信息

van der Klei I J, Faber K N, Keizer-Gunnink I, Gietl C, Harder W, Veenhuis M

机构信息

Laboratory for Electron Microscopy, University of Groningen, Haren, The Netherlands.

出版信息

FEBS Lett. 1993 Nov 8;334(1):128-32. doi: 10.1016/0014-5793(93)81697-x.

DOI:10.1016/0014-5793(93)81697-x

PMID:8224215

Abstract

We have studied the fate of the watermelon (Citrullus vulgaris Schrad.) glyoxysomal enzyme, malate dehydrogenase (gMDH), after synthesis in the methylotrophic yeast, Hansenula polymorpha. The gene encoding the precursor form of gMDH (pre-gMDH) was cloned in an H. polymorpha expression vector downstream of the inducible H. polymorpha alcohol oxidase promoter. During methylotrophic growth, pre-gMDH was synthesized and imported into peroxisomes, where it was enzymatically active. The apparent molecular mass of the protein located in H. polymorpha peroxisomes was equal to that of pre-gMDH (41 kDa), indicating that N-terminal processing of the transit peptide had not occurred in the yeast.

摘要

我们研究了西瓜（Citrullus vulgaris Schrad.）乙醛酸循环体酶——苹果酸脱氢酶（gMDH）在甲基营养型酵母多形汉逊酵母（Hansenula polymorpha）中合成后的命运。编码gMDH前体形式（前体gMDH）的基因被克隆到一个多形汉逊酵母表达载体中，位于可诱导的多形汉逊酵母醇氧化酶启动子下游。在甲基营养生长过程中，前体gMDH被合成并导入过氧化物酶体，在那里它具有酶活性。位于多形汉逊酵母过氧化物酶体中的蛋白质的表观分子量与前体gMDH的分子量相等（41 kDa），这表明转运肽的N端加工在酵母中并未发生。