STRUCTURAL AND FUNCTIONAL DOMAINS OF ESCHERICHIA-COLI INITIATION FACTOR-IF2

被引：30

作者：

LAALAMI, S

SACERDOT, C

VACHON, G

MORTENSEN, K

SPERLINGPETERSEN, HU

CENATIEMPO, Y

GRUNBERGMANAGO, M

机构：

[1] INST BIOL PHYS CHIM,13 RUE PIERRE & MARIE CURIE,F-75005 PARIS,FRANCE

[2] AARHUS UNIV,DEPT CHEM,BIODESIGN LAB,DK-8000 AARHUS,DENMARK

[3] UNIV POITIERS,BIOL MOLEC LAB,CNRS,URA 1172,F-86022 POITIERS,FRANCE

来源：

BIOCHIMIE | 1991年 / 73卷 / 12期

关键词：

TRANSLATION INITIATION FACTOR-II; IF2-ALPHA AND IF2-BETA; G-BINDING PROTEIN; G-DOMAIN;

D O I：

10.1016/0300-9084(91)90191-3

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：

Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNA(f)(Met) to the 30S ribosomal subunit. After formation of 70S translation initiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.

引用

页码：1557 / 1566

页数：10

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