Regulation of translation termination: Conserved structural motifs in bacterial and eukaryotic polypeptide release factors

被引:26
作者
Nakamura, Y
Ito, K
Matsumura, K
Kawazu, Y
Ebihara, K
机构
[1] Department of Tumor Biology, Institute of Medical Science, University of Tokyo
来源
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE | 1995年 / 73卷 / 11-12期
关键词
translation termination; stop codon recognition; peptide chain release factors; seven-domain model;
D O I
10.1139/o95-120
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
Translation termination requires codon-dependent polypeptide release factors. The mechanism of stop codon recognition by release factors is unknown and holds considerable interest since it entails protein-RNA recognition rather than the well-understood mRNA-tRNA interaction in codon-anticodon pairing. Bacteria have two codon-specific release factors and our picture of prokaryotic translation is changing because a third factor, which stimulates the other two, has now been found. Moreover, a highly conserved eukaryotic protein family possessing properties of polypeptide release factor has now been sought. This review summarizes our current understanding of the structural and functional organization of release factors as well as our recent findings of highly conserved structural motifs in bacterial and eukaryotic polypeptide release factors.
引用
收藏
页码:1113 / 1122
页数:10
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