Evidence for self‐association of the alternative sigma factor σ54. (11th February 2013)
- Record Type:
- Journal Article
- Title:
- Evidence for self‐association of the alternative sigma factor σ54. (11th February 2013)
- Main Title:
- Evidence for self‐association of the alternative sigma factor σ54
- Authors:
- Sabbatini, Massimo
Vezzoli, Alessandro
Milani, Mario
Bertoni, Giovanni - Abstract:
- <abstract abstract-type="main" id="febs12129-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="febs12129-sec-0001" sec-type="section"> <p>Sigma factor σ<sup>54</sup> has a distinct <italic>modus operandi</italic> for mediating the activation of bacterial RNA polymerase (RNAP) at promoter recognition motifs 12 and 24 bp upstream from transcription start sites. σ<sup>54</sup> was thought to act as monomer in all transcription steps. However, we provide evidence that σ<sup>54</sup> of <italic>Pseudomonas putida</italic> interacts stably with itself. The interface between monomers involves contacts in σ<sup>54</sup> regions I and III, sequences that play key roles in the transcription activation of σ<sup>54</sup>–RNAP holoenzyme. These roles include interactions with activator proteins and the −12 and −24 motifs. In particular, we detected inter‐monomer contacts between region I, and between region I and the C–terminal portion of region III. Our results suggest a new auto‐antagonistic regulatory state of σ<sup>54</sup>.</p> </sec> <sec id="febs12129-sec-0002" sec-type="section"> <title>Structured digital abstract</title> <p> <list id="febs12129-list-0001" list-type="bullet"> <list-item> <p>σ54 and σ54 bind by molecular sieving (View Interaction: 1, 2)</p> </list-item> <list-item> <p>σ54 and σ54 bind by blue native page (View interaction)</p> </list-item> <list-item> <p>P. aeruginosa σ54 physically interacts with P. aeruginosa σ54 by two hybrid (View<abstract abstract-type="main" id="febs12129-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="febs12129-sec-0001" sec-type="section"> <p>Sigma factor σ<sup>54</sup> has a distinct <italic>modus operandi</italic> for mediating the activation of bacterial RNA polymerase (RNAP) at promoter recognition motifs 12 and 24 bp upstream from transcription start sites. σ<sup>54</sup> was thought to act as monomer in all transcription steps. However, we provide evidence that σ<sup>54</sup> of <italic>Pseudomonas putida</italic> interacts stably with itself. The interface between monomers involves contacts in σ<sup>54</sup> regions I and III, sequences that play key roles in the transcription activation of σ<sup>54</sup>–RNAP holoenzyme. These roles include interactions with activator proteins and the −12 and −24 motifs. In particular, we detected inter‐monomer contacts between region I, and between region I and the C–terminal portion of region III. Our results suggest a new auto‐antagonistic regulatory state of σ<sup>54</sup>.</p> </sec> <sec id="febs12129-sec-0002" sec-type="section"> <title>Structured digital abstract</title> <p> <list id="febs12129-list-0001" list-type="bullet"> <list-item> <p>σ54 and σ54 bind by molecular sieving (View Interaction: 1, 2)</p> </list-item> <list-item> <p>σ54 and σ54 bind by blue native page (View interaction)</p> </list-item> <list-item> <p>P. aeruginosa σ54 physically interacts with P. aeruginosa σ54 by two hybrid (View interaction)</p> </list-item> <list-item> <p>σ54 physically interacts with σ54 by two hybrid (View Interaction: 1, 2, 3)</p> </list-item> <list-item> <p>p53 physically interacts with SV40T by two hybrid (View interaction)</p> </list-item> </list> </p> </sec> </abstract> … (more)
- Is Part Of:
- FEBS journal. Volume 280:Number 5(2013)
- Journal:
- FEBS journal
- Issue:
- Volume 280:Number 5(2013)
- Issue Display:
- Volume 280, Issue 5 (2013)
- Year:
- 2013
- Volume:
- 280
- Issue:
- 5
- Issue Sort Value:
- 2013-0280-0005-0000
- Page Start:
- 1371
- Page End:
- 1378
- Publication Date:
- 2013-02-11
- Subjects:
- Biochemistry -- Periodicals
Molecular biology -- Periodicals
Pathology, Molecular -- Periodicals
572 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://gateway.ovid.com/ovidweb.cgi?T=JS&MODE=ovid&NEWS=n&PAGE=toc&D=ovft&AN=01038983-000000000-00000 ↗
http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=ejb ↗
http://onlinelibrary.wiley.com/ ↗
http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=ejb ↗ - DOI:
- 10.1111/febs.12129 ↗
- Languages:
- English
- ISSNs:
- 1742-464X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3901.578500
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4353.xml