Regulation and action of the bacterial enhancer-binding protein AAA+ domains.


Journal Article

Bacterial EBPs (enhancer-binding proteins) play crucial roles in regulating cellular responses to environmental changes, in part by providing efficient control over sigma(54)-dependent gene transcription. The AAA+ (ATPase associated with various cellular activites) domain of the EBPs, when assembled into a ring, uses energy from ATP binding, hydrolysis and product release to remodel the sigma(54)-RNAP (RNA polymerase) holoenzyme so that it can transition from closed to open form at promoter DNA. The assembly, and hence activity, of these ATPases are regulated by many different signal transduction mechanisms. Recent advances in solution scattering techniques, when combined with high-resolution structures and biochemical data, have enabled us to obtain mechanistic insights into the regulation and action of a subset of these sigma(54) activators: those whose assembly into ring form is controlled by two-component signal transduction. We review (i) experimental considerations of applying the SAXS (small-angle X-ray scattering)/WAXS (wide-angle X-ray scattering) technique, (ii) distinct regulation mechanisms of the AAA+ domains of three EBPs by similar two-component signal transduction receiver domains, and (iii) major conformational changes and correlated sigma(54)-binding activity of an isolated EBP AAA+ domain in the ATP hydrolysis cycle.

Full Text

Cited Authors

  • Chen, B; Sysoeva, TA; Chowdhury, S; Nixon, BT

Published Date

  • February 2008

Published In

Volume / Issue

  • 36 / Pt 1

Start / End Page

  • 89 - 93

PubMed ID

  • 18208392

Pubmed Central ID

  • 18208392

Electronic International Standard Serial Number (EISSN)

  • 1470-8752

International Standard Serial Number (ISSN)

  • 0300-5127

Digital Object Identifier (DOI)

  • 10.1042/BST0360089


  • eng