Functional diversity of AAA+ protease complexes in Bacillus subtilis

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dc.identifier.uri http://dx.doi.org/10.15488/3340
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/3370
dc.contributor.author Elsholz, Alexander K.W.
dc.contributor.author Birk, Marlene S.
dc.contributor.author Charpentier, Emmanuelle
dc.contributor.author Turgay, Kürsad
dc.date.accessioned 2018-05-18T12:03:55Z
dc.date.available 2018-05-18T12:03:55Z
dc.date.issued 2017
dc.identifier.citation Elsholz, A.K.W.; Birk, M.S.; Charpentier, E.; Turgay, K.: Functional diversity of AAA+ protease complexes in Bacillus subtilis. In: Frontiers in Molecular Biosciences 4 (2017), 44. DOI: https://doi.org/10.3389/fmolb.2017.00044
dc.description.abstract 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. © 2017 Elsholz, Birk, Charpentier and Turgay. eng
dc.language.iso eng
dc.publisher Lausanne : Frontiers Media S.A.
dc.relation.ispartofseries Frontiers in Molecular Biosciences 4 (2017)
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject AAA+ protease complexes eng
dc.subject Adaptor proteins eng
dc.subject Bacillus subtilis eng
dc.subject Chaperones eng
dc.subject Hsp100/Clp proteins eng
dc.subject McsB eng
dc.subject Protein quality control eng
dc.subject Regulatory proteolysis eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Functional diversity of AAA+ protease complexes in Bacillus subtilis
dc.type Article
dc.type Text
dc.relation.issn 2296-889X
dc.relation.doi https://doi.org/10.3389/fmolb.2017.00044
dc.bibliographicCitation.issue JUL
dc.bibliographicCitation.volume 4
dc.bibliographicCitation.firstPage 44
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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