TARGETING SEQUENCES OF THE 2 MAJOR PEROXISOMAL PROTEINS IN THE METHYLOTROPHIC YEAST HANSENULA-POLYMORPHA

被引:48
|
作者
HANSEN, H
DIDION, T
THIEMANN, A
VEENHUIS, M
ROGGENKAMP, R
机构
[1] UNIV DUSSELDORF,INST MIKROBIOL,UNIV STR 1,W-4000 DUSSELDORF 1,GERMANY
[2] UNIV GRONINGEN,CTR BIOL,ELECTRON MICROSCOPY LAB,9751 NN HAREN,NETHERLANDS
来源
MOLECULAR & GENERAL GENETICS | 1992年 / 235卷 / 2-3期
关键词
PEROXISOMES; TARGETING SIGNALS; YEAST; HANSENULA-POLYMORPHA;
D O I
10.1007/BF00279370
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
Dihydroxyacetone synthase (DAS) and methanol oxidase (MOX) are the major enzyme constituents of the peroxisomal matrix in the methylotrophic yeast Hansenula polymorpha when grown on methanol as a sole carbon source. In order to characterize their topogenic signals the localization of truncated polypeptides and hybrid proteins was analysed in transformed yeast cells by subcellular fractionation and electron microscopy. The C-terminal part of DAS, when fused to the bacterial beta-lactamase or mouse dihydrofolate reductase, directed these hybrid polypeptides to the peroxisome compartment. The targeting signal was further delimited to the extreme C-terminus, comprising the sequence N-K-L-COOH, similar to the recently identified and widely distributed peroxisomal targeting signal (PTS) S-K-L-COOH in firefly luciferase. By an identical approach, the extreme C-terminus of MOX, comprising the tripeptide A-R-F-COOH, was shown to be the PTS of this protein. Furthermore, on fusion of a C-terminal sequence from firefly luciferase including the PTS, beta-lactamase was also imported into the peroxisomes of H. polymorpha. We conclude that, besides the conserved PTS (or described variants), other amino acid sequences with this function have evolved in nature.
引用
收藏
页码:269 / 278
页数:10
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