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Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis
Here, we review the diverse roles and functions of AAA+ protease complexes in protein homeostasis, control of stress response and cellular development pathways by regulatory and general proteolysis in the Gram-positive model organism Bacillus subtilis. We discuss in detail the intricate involvement...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5506225/ https://www.ncbi.nlm.nih.gov/pubmed/28748186 http://dx.doi.org/10.3389/fmolb.2017.00044 |
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author | Elsholz, Alexander K. W. Birk, Marlene S. Charpentier, Emmanuelle Turgay, Kürşad |
author_facet | Elsholz, Alexander K. W. Birk, Marlene S. Charpentier, Emmanuelle Turgay, Kürşad |
author_sort | Elsholz, Alexander K. W. |
collection | PubMed |
description | Here, we review the diverse roles and functions of AAA+ protease complexes in protein homeostasis, control of stress response and cellular development pathways by regulatory and general proteolysis in the Gram-positive model organism Bacillus subtilis. We discuss in detail the intricate involvement of AAA+ protein complexes in controlling sporulation, the heat shock response and the role of adaptor proteins in these processes. The investigation of these protein complexes and their adaptor proteins has revealed their relevance for Gram-positive pathogens and their potential as targets for new antibiotics. |
format | Online Article Text |
id | pubmed-5506225 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-55062252017-07-26 Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis Elsholz, Alexander K. W. Birk, Marlene S. Charpentier, Emmanuelle Turgay, Kürşad Front Mol Biosci Molecular Biosciences Here, we review the diverse roles and functions of AAA+ protease complexes in protein homeostasis, control of stress response and cellular development pathways by regulatory and general proteolysis in the Gram-positive model organism Bacillus subtilis. We discuss in detail the intricate involvement of AAA+ protein complexes in controlling sporulation, the heat shock response and the role of adaptor proteins in these processes. The investigation of these protein complexes and their adaptor proteins has revealed their relevance for Gram-positive pathogens and their potential as targets for new antibiotics. Frontiers Media S.A. 2017-07-12 /pmc/articles/PMC5506225/ /pubmed/28748186 http://dx.doi.org/10.3389/fmolb.2017.00044 Text en Copyright © 2017 Elsholz, Birk, Charpentier and Turgay. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Elsholz, Alexander K. W. Birk, Marlene S. Charpentier, Emmanuelle Turgay, Kürşad Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis |
title | Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis |
title_full | Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis |
title_fullStr | Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis |
title_full_unstemmed | Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis |
title_short | Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis |
title_sort | functional diversity of aaa+ protease complexes in bacillus subtilis |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5506225/ https://www.ncbi.nlm.nih.gov/pubmed/28748186 http://dx.doi.org/10.3389/fmolb.2017.00044 |
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