A CONSERVED SECONDARY STRUCTURAL MOTIF IN 23S RIBOSOMAL-RNA DEFINES THE SITE OF INTERACTION OF AMICETIN, A UNIVERSAL INHIBITOR OF PEPTIDE-BOND FORMATION

被引：50
|
作者：
LEVIEV, IG
RODRIGUEZFONSECA, C
PHAN, H
GARRETT, RA
HEILEK, G
NOLLER, HF
MANKIN, AS
机构：
[1] UNIV COPENHAGEN,INST MOLEC BIOL,DK-1307 COPENHAGEN K,DENMARK
[2] UNIV CALIF SANTA CRUZ,SINSHEIMER LABS,SANTA CRUZ,CA 95064
来源：
EMBO JOURNAL | 1994年 / 13卷 / 07期
关键词：
AMICETIN; PEPTIDYL TRANSFERASE;
D O I：
10.1002/j.1460-2075.1994.tb06432.x
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 binding site and probable site of action have been determined for the universal antibiotic amicetin which inhibits peptide bond formation. Evidence from in vivo mutants, site-directed mutations and chemical footprinting all implicate a highly conserved moth in the secondary structure of the 23S-like rRNA close to the central circle of domain V. We infer that this motif lies at, or close to, the catalytic site in the peptidyl transfer centre. The binding site of amicetin is the first of a group of functionally related hexose-cytosine inhibitors to be localized on the ribosome.
引用
收藏
页码：1682 / 1686
页数：5
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