The structural basis for regulated assembly and function of the transcriptional activator NtrC

被引：102

作者：

De Carlo, Sacha

Chen, Baoyu

Hoover, Timothy R.

Kondrashkina, Elena

Nogales, Eva

Nixon, B. Tracy ^{[1
]}

机构：

[1] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Lawrence Berkeley Natl Lab, Berkeley, CA 94720 USA

[3] Penn State Univ, Integrat Biosci Grad Degree Program Chem Biol, University Pk, PA 16802 USA

[4] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA

[5] Univ Georgia, Dept Microbiol, Athens, GA 30602 USA

[6] IIT, BioCAT, APS, Argonne Natl Lab, Argonne, IL 60439 USA

来源：

GENES & DEVELOPMENT | 2006年 / 20卷 / 11期

关键词：

NtrC; gene regulation; AAA plus ATPase assembly; transcription activation; enhancer-binding protein; two-component signal transduction;

D O I：

10.1101/gad.1418306

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

In two-component signal transduction, an input triggers phosphorylation of receiver domains that regulate the status of output modules. One such module is the AAA+ ATPase domain in bacterial enhancer-binding proteins that remodel the sigma(54) form of RNA polymerase. We report X-ray solution scattering and electron microscopy structures of the activated, full-length nitrogen-regulatory protein C (NtrC) showing a novel mechanism for regulation of AAA+ ATPase assembly via the juxtaposition of the receiver domains and ATPase ring. Accompanying the hydrolysis cycle that is required for transcriptional activation, we observed major order-disorder changes in the GAFTGA loops involved in sigma(54) binding, as well as in the DNA-binding domains.

引用

页码：1485 / 1495

页数：11

共 57 条

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