RIBOTOXIN RECOGNITION OF RIBOSOMAL-RNA AND A PROPOSAL FOR THE MECHANISM OF TRANSLOCATION

被引：196

作者：

WOOL, IG ^{[1
]}

GLUCK, A ^{[1
]}

ENDO, Y ^{[1
]}

机构：

[1] EHIME UNIV, FAC ENGN, DEPT APPL CHEM, MATSUYAMA, EHIME 790, JAPAN

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1992年 / 17卷 / 07期

关键词：

D O I：

10.1016/0968-0004(92)90407-Z

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：

The ribotoxins alpha-sarcin and ricin catalyse covalent modifications in adjacent nucleotides in 28S rRNA, yet the elements of nucleic acid structure that they recognize are not only different but incompatible. This suggests that this ribosomal domain (which in two dimensions is a seven-base-pair helical stem and a 17-member single-stranded loop) has alternate conformers. Since the domain is involved in binding of aminoacyl-tRNA and GTP hydrolysis, we propose that the switch between the two configurations, perhaps initiated by the binding of elongation factors, plays a role in translocation.

引用

页码：266 / 269

页数：4

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