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

Baoyu Chen, Tatyana A. Sysoeva, Saikat Chowdhury, B. Tracy Nixon

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Bacterial EBPs (enhancer-binding proteins) play crucial roles in regulating cellular responses to environmental changes, in part by providing efficient control over σ54-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 σ54-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 σ54 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 σ54-binding activity of an isolated EBP AAA+ domain in the ATP hydrolysis cycle.

Original languageEnglish (US)
Pages (from-to)89-93
Number of pages5
JournalBiochemical Society transactions
Volume36
Issue number1
DOIs
StatePublished - Feb 1 2008

Fingerprint

Signal transduction
Carrier Proteins
Signal Transduction
X ray scattering
Adenosine Triphosphatases
Hydrolysis
Adenosine Triphosphate
X-Rays
Holoenzymes
DNA-Directed RNA Polymerases
Transcription
Genes
Scattering
Protein Domains
DNA

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Chen, Baoyu ; Sysoeva, Tatyana A. ; Chowdhury, Saikat ; Nixon, B. Tracy. / Regulation and action of the bacterial enhancer-binding protein AAA+ domains. In: Biochemical Society transactions. 2008 ; Vol. 36, No. 1. pp. 89-93.
@article{8e5f6bbd5ff648f8888f258203ef9aed,
title = "Regulation and action of the bacterial enhancer-binding protein AAA+ domains",
abstract = "Bacterial EBPs (enhancer-binding proteins) play crucial roles in regulating cellular responses to environmental changes, in part by providing efficient control over σ54-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 σ54-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 σ54 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 σ54-binding activity of an isolated EBP AAA+ domain in the ATP hydrolysis cycle.",
author = "Baoyu Chen and Sysoeva, {Tatyana A.} and Saikat Chowdhury and Nixon, {B. Tracy}",
year = "2008",
month = "2",
day = "1",
doi = "10.1042/BST0360089",
language = "English (US)",
volume = "36",
pages = "89--93",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "1",

}

Regulation and action of the bacterial enhancer-binding protein AAA+ domains. / Chen, Baoyu; Sysoeva, Tatyana A.; Chowdhury, Saikat; Nixon, B. Tracy.

In: Biochemical Society transactions, Vol. 36, No. 1, 01.02.2008, p. 89-93.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Regulation and action of the bacterial enhancer-binding protein AAA+ domains

AU - Chen, Baoyu

AU - Sysoeva, Tatyana A.

AU - Chowdhury, Saikat

AU - Nixon, B. Tracy

PY - 2008/2/1

Y1 - 2008/2/1

N2 - Bacterial EBPs (enhancer-binding proteins) play crucial roles in regulating cellular responses to environmental changes, in part by providing efficient control over σ54-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 σ54-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 σ54 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 σ54-binding activity of an isolated EBP AAA+ domain in the ATP hydrolysis cycle.

AB - Bacterial EBPs (enhancer-binding proteins) play crucial roles in regulating cellular responses to environmental changes, in part by providing efficient control over σ54-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 σ54-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 σ54 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 σ54-binding activity of an isolated EBP AAA+ domain in the ATP hydrolysis cycle.

UR - http://www.scopus.com/inward/record.url?scp=39449114777&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=39449114777&partnerID=8YFLogxK

U2 - 10.1042/BST0360089

DO - 10.1042/BST0360089

M3 - Article

C2 - 18208392

AN - SCOPUS:39449114777

VL - 36

SP - 89

EP - 93

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 1

ER -