PROKARYOTIC TRANSLATION INITIATION-FACTOR IF3 IS AN ELONGATED PROTEIN CONSISTING OF 2 CRYSTALLIZABLE DOMAINS

被引：34

作者：

KYCIA, JH ^{[1
]}

BIOU, V ^{[1
]}

SHU, F ^{[1
]}

GERCHMAN, SE ^{[1
]}

GRAZIANO, V ^{[1
]}

RAMAKRISHNAN, V ^{[1
]}

机构：

[1] BROOKHAVEN NATL LAB,DEPT BIOL,UPTON,NY 11973

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 18期

关键词：

D O I：

10.1021/bi00018a022

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：

We show that translation initiation factor IF3 can be split into two fragments of nearly equal size by the Escherichia coli outer membrane protease omptin. Circular dichroism and small-angle neutron scattering show that the two fragments are structured as domains. Each domain is relatively compact, and they are separated by about 45 Angstrom in intact IF3. Thus IF3 is an elongated protein that consists of two well-separated domains. We suggest that these two domains are involved in ribosome binding across the cleft of the 30S ribosome. We also report the crystallization of each domain of IF3.

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页码：6183 / 6187

页数：5

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