FUNCTION OF N-TERMINAL IMPORT SIGNALS IN TRYPANOSOME MICROBODIES

被引：51

作者：

BLATTNER, J ^{[1
]}

DORSAM, H ^{[1
]}

CLAYTON, CE ^{[1
]}

机构：

[1] UNIV HEIDELBERG, ZENTRUM MOLEK BIOL, D-69120 HEIDELBERG, GERMANY

来源：

FEBS LETTERS | 1995年 / 360卷 / 03期

关键词：

GLYCOSOME; PROTEIN IMPORT; N-TERMINAL SIGNAL SEQUENCE; TRYPANOSOMA BRUCEI;

D O I：

10.1016/0014-5793(95)00128-V

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：

The glycosomes of trypanosomes are related to eukaryotic peroxisomes. For many glycosomal and peroxisomal proteins, a C-terminal SKL-like tripeptide known as PTS-1 serves as the targeting signal. For peroxisomes, a second N-terminal signal (PTS-2) was demonstrated on rat 3-ketoacyl-CoA thiolase. Several glycosomal proteins do not bear a PTS-1. One such protein, fructose bisphosphate aldolase, has a PTS-2 homology at its N-terminus. To find out whether the PTS-2 pathway exists in trypanosomes, we expressed chloramphenicol acetyltransferase fusion proteins bearing N-terminal segments of either rat thiolase or trypanosome aldolase. The mammalian PTS-2 clearly mediated glycosomal import. The aldolase N-terminus mediated import with variable efficiency depending on the length of the appended sequence. These results provide evidence for the existence of the PTS-2 pathway in trypanosomes.

引用

页码：310 / 314

页数：5

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