Inhibition of the B-subtilis regulatory protein TRAP by the TRAP-inhibitory protein, AT

被引：59

作者：

Valbuzzi, A ^{[1
]}

Yanofsky, C ^{[1
]}

机构：

[1] Stanford Univ, Dept Biol Sci, Stanford, CA 94305 USA

来源：

SCIENCE | 2001年 / 293卷 / 5537期

关键词：

D O I：

10.1126/science.1062187

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An anti-TRAP (AT) protein, a factor of previously unknown function, conveys the metabolic signal that the cellular transfer RNA for tryptophan (tRNA(Trp)) is predominantly uncharged. Expression of the operon encoding AT is induced by uncharged tRNA(Trp). AT associates with TRAP, the trp operon attenuation protein, and inhibits its binding to its target RNA sequences. This relieves TRAP-mediated transcription termination and translation inhibition, increasing the rate of tryptophan biosynthesis. AT binds to TRAP primarily when it is in the tryptophan-activated state. The 53-residue AT polypeptide is homologous to the zinc-binding domain of DnaJ. The mechanisms regulating tryptophan biosynthesis in Bacillus subtilis differ from those used by Escherichia coli.

引用

页码：2057 / 2059

页数：3