Membrane Chaperoning by Members of the PspA/IM30 Protein Family

Research output: Contribution to journalArticleResearchpeer review

Authors

Research Organisations

External Research Organisations

  • Johannes Gutenberg University Mainz
  • Technische Universität Dresden
View graph of relations

Details

Original languageEnglish
Article numbere1264546
JournalCommunicative & Integrative Biology
Publication statusPublished - 19 Feb 2017

Abstract

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.

Cite this

Membrane Chaperoning by Members of the PspA/IM30 Protein Family. / Thurotte, Adrien; Brüser, Thomas; Mascher, Thorsten et al.
In: Communicative & Integrative Biology, 19.02.2017.

Research output: Contribution to journalArticleResearchpeer review

Thurotte, A, Brüser, T, Mascher, T & Schneider, D 2017, 'Membrane Chaperoning by Members of the PspA/IM30 Protein Family', Communicative & Integrative Biology. https://doi.org/10.1080/19420889.2016.1264546
Thurotte, A., Brüser, T., Mascher, T., & Schneider, D. (2017). Membrane Chaperoning by Members of the PspA/IM30 Protein Family. Communicative & Integrative Biology, Article e1264546. https://doi.org/10.1080/19420889.2016.1264546
Thurotte A, Brüser T, Mascher T, Schneider D. Membrane Chaperoning by Members of the PspA/IM30 Protein Family. Communicative & Integrative Biology. 2017 Feb 19;e1264546. doi: 10.1080/19420889.2016.1264546
Thurotte, Adrien ; Brüser, Thomas ; Mascher, Thorsten et al. / Membrane Chaperoning by Members of the PspA/IM30 Protein Family. In: Communicative & Integrative Biology. 2017.
Download
@article{7716028bce95461e8b24cf22a51e058f,
title = "Membrane Chaperoning by Members of the PspA/IM30 Protein Family",
abstract = "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.",
author = "Adrien Thurotte and Thomas Br{\"u}ser and Thorsten Mascher and Dirk Schneider",
year = "2017",
month = feb,
day = "19",
doi = "10.1080/19420889.2016.1264546",
language = "English",

}

Download

TY - JOUR

T1 - Membrane Chaperoning by Members of the PspA/IM30 Protein Family

AU - Thurotte, Adrien

AU - Brüser, Thomas

AU - Mascher, Thorsten

AU - Schneider, Dirk

PY - 2017/2/19

Y1 - 2017/2/19

N2 - 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.

AB - 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.

U2 - 10.1080/19420889.2016.1264546

DO - 10.1080/19420889.2016.1264546

M3 - Article

JO - Communicative & Integrative Biology

JF - Communicative & Integrative Biology

SN - 1942-0889

M1 - e1264546

ER -

By the same author(s)