A HIGHLY CONSERVED EUKARYOTIC PROTEIN FAMILY POSSESSING PROPERTIES OF POLYPEPTIDE-CHAIN RELEASE FACTOR

被引：357
作者：
FROLOVA, L
LEGOFF, X
RASMUSSEN, HH
CHEPEREGIN, S
DRUGEON, G
KRESS, M
ARMAN, I
HAENNI, AL
CELIS, JE
PHILIPPE, M
JUSTESEN, J
KISSELEV, L
机构：
[1] RUSSIAN ACAD SCI,VA ENGELHARDT MOLEC BIOL INST,MOSCOW 117984,RUSSIA
[2] AARHUS UNIV,DEPT BIOL MOLEC,DK-800 AARHUS C,DENMARK
[3] INST JACQUES MONOD,F-75251 PARIS 05,FRANCE
[4] UNIV RENNES 1,CNRS,URA 256,DEPT BIOL & GENET DEV,F-35042 RENNES,FRANCE
[5] AARHUS UNIV,INST MED BIOCHEM,DK-8000 AARHUS C,DENMARK
[6] AARHUS UNIV,DANISH CTR HUMAN GENOME RES,DK-8000 AARHUS C,DENMARK
[7] RUSSIAN ACAD SCI,INST MOLEC GENET,MOSCOW 123182,RUSSIA
[8] CNRS,ERS0048,MOLEC ONCOL LAB,F-94802 VILLEJUIF,FRANCE
来源：
NATURE | 1994年 / 372卷 / 6507期
关键词：
D O I：
10.1038/372701a0
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
THE termination of protein synthesis in ribosomes is governed by termination (stop) codons in messenger RNAs and by polypeptide chain release factors (RFs). Although the primary structure of prokaryotic RFs and yeast mitochrondrial RF is established(1-4), that of the only known eukaryotic RF (eRF)(5) remains obscure. Here we report the assignment of a family of tightly related proteins (designated eRF1) from lower and higher eukaryotes which are structurally and functionally similar to rabbit eRF. Two of these proteins, one from human(6) and the other from Xenopus laevis(7), have been expressed in yeast and Escherichia coli, respectively, purified and shown to be active in the in vitro RF assay. The other protein of this family, sup45 (sup1) of Saccharomyces cerevisiae, is involved in omnipotent suppression during translations(8-12). The amino-acid sequence of the eRF1 family is highly conserved. We conclude that the eRF1 proteins are directly implicated in the termination of translation in eukaryotes.
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页码：701 / 703
页数：3
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