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Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein
RpoS, an RNA polymerase σ factor, controls the response of Escherichia coli and related bacteria to multiple stress responses. During nonstress conditions, RpoS is rapidly degraded by ClpXP, mediated by the adaptor protein RssB, a member of the response regulator family. In response to stress, RpoS...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3877760/ https://www.ncbi.nlm.nih.gov/pubmed/24352426 http://dx.doi.org/10.1101/gad.229617.113 |
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author | Battesti, Aurelia Hoskins, Joel R. Tong, Song Milanesio, Paola Mann, Jessica M. Kravats, Andrea Tsegaye, Yodit M. Bougdour, Alexandre Wickner, Sue Gottesman, Susan |
author_facet | Battesti, Aurelia Hoskins, Joel R. Tong, Song Milanesio, Paola Mann, Jessica M. Kravats, Andrea Tsegaye, Yodit M. Bougdour, Alexandre Wickner, Sue Gottesman, Susan |
author_sort | Battesti, Aurelia |
collection | PubMed |
description | RpoS, an RNA polymerase σ factor, controls the response of Escherichia coli and related bacteria to multiple stress responses. During nonstress conditions, RpoS is rapidly degraded by ClpXP, mediated by the adaptor protein RssB, a member of the response regulator family. In response to stress, RpoS degradation ceases. Small anti-adaptor proteins—IraP, IraM, and IraD, each made under a different stress condition—block RpoS degradation. RssB mutants resistant to either IraP or IraM were isolated and analyzed in vivo and in vitro. Each of the anti-adaptors is unique in its interaction with RssB and sensitivity to RssB mutants. One class of mutants defined an RssB N-terminal region close to the phosphorylation site and critical for interaction with IraP but unnecessary for IraM and IraD function. A second class, in the RssB C-terminal PP2C-like domain, led to activation of RssB function. These mutants allowed the response regulator to act in the absence of phosphorylation but did not abolish interaction with anti-adaptors. This class of mutants is broadly resistant to the anti-adaptors and bears similarity to constitutively activated mutants found in a very different PP2C protein. The mutants provide insight into how the anti-adaptors perturb RssB response regulator function and activation. |
format | Online Article Text |
id | pubmed-3877760 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38777602014-06-15 Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein Battesti, Aurelia Hoskins, Joel R. Tong, Song Milanesio, Paola Mann, Jessica M. Kravats, Andrea Tsegaye, Yodit M. Bougdour, Alexandre Wickner, Sue Gottesman, Susan Genes Dev Research Paper RpoS, an RNA polymerase σ factor, controls the response of Escherichia coli and related bacteria to multiple stress responses. During nonstress conditions, RpoS is rapidly degraded by ClpXP, mediated by the adaptor protein RssB, a member of the response regulator family. In response to stress, RpoS degradation ceases. Small anti-adaptor proteins—IraP, IraM, and IraD, each made under a different stress condition—block RpoS degradation. RssB mutants resistant to either IraP or IraM were isolated and analyzed in vivo and in vitro. Each of the anti-adaptors is unique in its interaction with RssB and sensitivity to RssB mutants. One class of mutants defined an RssB N-terminal region close to the phosphorylation site and critical for interaction with IraP but unnecessary for IraM and IraD function. A second class, in the RssB C-terminal PP2C-like domain, led to activation of RssB function. These mutants allowed the response regulator to act in the absence of phosphorylation but did not abolish interaction with anti-adaptors. This class of mutants is broadly resistant to the anti-adaptors and bears similarity to constitutively activated mutants found in a very different PP2C protein. The mutants provide insight into how the anti-adaptors perturb RssB response regulator function and activation. Cold Spring Harbor Laboratory Press 2013-12-15 /pmc/articles/PMC3877760/ /pubmed/24352426 http://dx.doi.org/10.1101/gad.229617.113 Text en Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/. |
spellingShingle | Research Paper Battesti, Aurelia Hoskins, Joel R. Tong, Song Milanesio, Paola Mann, Jessica M. Kravats, Andrea Tsegaye, Yodit M. Bougdour, Alexandre Wickner, Sue Gottesman, Susan Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein |
title | Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein |
title_full | Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein |
title_fullStr | Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein |
title_full_unstemmed | Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein |
title_short | Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein |
title_sort | anti-adaptors provide multiple modes for regulation of the rssb adaptor protein |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3877760/ https://www.ncbi.nlm.nih.gov/pubmed/24352426 http://dx.doi.org/10.1101/gad.229617.113 |
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