WATERMELON GLYOXYSOMAL MALATE-DEHYDROGENASE IS SORTED TO PEROXISOMES OF THE METHYLOTROPHIC YEAST, HANSENULA-POLYMORPHA

被引：15

作者：

VANDERKLEI, IJ

FABER, KN

KEIZERGUNNINK, I

GIETL, C

HARDER, W

VEENHUIS, M

机构：

[1] UNIV GRONINGEN, CTR BIOL, ELECTRON MICROSCOPY LAB, KERKLAAN 30, 9751 NN HAREN, NETHERLANDS

[2] TECH UNIV MUNICH, INST BOT & MICROBIOL, D-80333 MUNICH, GERMANY

来源：

FEBS LETTERS | 1993年 / 334卷 / 01期

关键词：

MALATE DEHYDROGENASE; GLYOXYSOME; PEROXISOME; HANSENULA-POLYMORPHA; CITRULLUS-VULGARIS; PROTEIN TARGETING;

D O I：

10.1016/0014-5793(93)81697-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：128 / 132

页数：5

共 24 条

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