Membrane chaperoning by members of the PspA/IM30 protein family

PspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning ac...

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Main Authors: Adrien Thurotte, Thomas Brüser, Thorsten Mascher, Dirk Schneider
Format: Article
Language:English
Published: Taylor & Francis Group 2017-01-01
Series:Communicative & Integrative Biology
Subjects:
Online Access:http://dx.doi.org/10.1080/19420889.2016.1264546
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spelling doaj-893d7c2ce8de45298849e3ba970b75a62021-03-02T10:03:25ZengTaylor & Francis GroupCommunicative & Integrative Biology1942-08892017-01-0110110.1080/19420889.2016.12645461264546Membrane chaperoning by members of the PspA/IM30 protein familyAdrien Thurotte0Thomas Brüser1Thorsten Mascher2Dirk Schneider3Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität MainzInstitut für Mikrobiologie, Leibniz Universität HannoverInstitut für Mikrobiologie, Technische Universität DresdenInstitut für Pharmazie und Biochemie, Johannes Gutenberg-Universität MainzPspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.http://dx.doi.org/10.1080/19420889.2016.1264546IM30LiaHmembrane chaperonemembrane stressoligomerPspAPspA/IM30 familyVipp1YjfJ
collection DOAJ
language English
format Article
sources DOAJ
author Adrien Thurotte
Thomas Brüser
Thorsten Mascher
Dirk Schneider
spellingShingle Adrien Thurotte
Thomas Brüser
Thorsten Mascher
Dirk Schneider
Membrane chaperoning by members of the PspA/IM30 protein family
Communicative & Integrative Biology
IM30
LiaH
membrane chaperone
membrane stress
oligomer
PspA
PspA/IM30 family
Vipp1
YjfJ
author_facet Adrien Thurotte
Thomas Brüser
Thorsten Mascher
Dirk Schneider
author_sort Adrien Thurotte
title Membrane chaperoning by members of the PspA/IM30 protein family
title_short Membrane chaperoning by members of the PspA/IM30 protein family
title_full Membrane chaperoning by members of the PspA/IM30 protein family
title_fullStr Membrane chaperoning by members of the PspA/IM30 protein family
title_full_unstemmed Membrane chaperoning by members of the PspA/IM30 protein family
title_sort membrane chaperoning by members of the pspa/im30 protein family
publisher Taylor & Francis Group
series Communicative & Integrative Biology
issn 1942-0889
publishDate 2017-01-01
description PspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.
topic IM30
LiaH
membrane chaperone
membrane stress
oligomer
PspA
PspA/IM30 family
Vipp1
YjfJ
url http://dx.doi.org/10.1080/19420889.2016.1264546
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AT thorstenmascher membranechaperoningbymembersofthepspaim30proteinfamily
AT dirkschneider membranechaperoningbymembersofthepspaim30proteinfamily
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