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

Sacha De Carlo, Baoyu Chen, Timothy R. Hoover, Elena Kondrashkina, Eva Nogales, B. Tracy Nixon

Research output: Contribution to journalArticle

95 Scopus citations

Abstract

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 σ54 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 σ54 binding, as well as in the DNA-binding domains.

Original languageEnglish (US)
Pages (from-to)1485-1495
Number of pages11
JournalGenes and Development
Volume20
Issue number11
DOIs
StatePublished - Jun 1 2006

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology

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