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
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
收藏
页码:310 / 314
页数:5
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