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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Online Access: | http://dx.doi.org/10.1080/19420889.2016.1264546 |
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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 |
work_keys_str_mv |
AT adrienthurotte membranechaperoningbymembersofthepspaim30proteinfamily AT thomasbruser membranechaperoningbymembersofthepspaim30proteinfamily AT thorstenmascher membranechaperoningbymembersofthepspaim30proteinfamily AT dirkschneider membranechaperoningbymembersofthepspaim30proteinfamily |
_version_ |
1724237870504345600 |