FATE OF HIGHLY EXPRESSED PROTEINS DESTINED TO PEROXISOMES IN SACCHAROMYCES-CEREVISIAE

被引:25
作者
HARTIG, A
OGRIS, M
COHEN, G
BINDER, M
机构
[1] LUDWIG BOLTZMANN FORSCHUNGSSTELLE BIOCHEM,A-1090 VIENNA,AUSTRIA
[2] INST TUMORBIOL KREBSFORSCH,A-1090 VIENNA,AUSTRIA
[3] MT SINAI MED CTR,DEPT CELL BIOL & ANAT,NEW YORK,NY 10029
关键词
Overexpression; Peroxisomes; Protein translocation; Saccharomyces cerevisiae;
D O I
10.1007/BF00321111
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Import of proteins into organelles usually requires a cis-acting targeting signal. Analysis of various hybrid proteins, consisting of mouse DHFR and parts of catalase A from Saccharomyces cerevisiae, revealed that fusion proteins containing the N-terminal 126 amino acids, or less, of catalase A remain in the cytosol whereas fusion proteins containing 140, or more, N-terminal amino acids of catalase A form large aggregates inside the cell. These protein bodies, which lack a surrounding membrane, copurified with peroxisomes on cell fractionation. The peroxisomal targeting signal of catalase A does not reside at the C-terminus or at the N-terminus. © 1990 Springer-Verlag.
引用
收藏
页码:23 / 27
页数:5
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