Membrane chaperoning by members of the PspA/IM30 protein family

6533b824fe1ef96bd1280c21

RESEARCH PRODUCT

Membrane chaperoning by members of the PspA/IM30 protein family

Thorsten Mascher Dirk Schneider Thomas Brüser Adrien Thurotte

subject

0301 basic medicine Dewey Decimal Classification::500 | Naturwissenschaften::570 | Biowissenschaften Biologie Protein family PspA 030106 microbiology Protein family Biology Biochemistry Oligomer Vipp1 03 medical and health sciences chemistry.chemical_compound ddc:570 membrane stress LiaH lcsh:QH301-705.5 Biology YjfJ Membrane stress Membrane Membrane structure membrane chaperone Monomer Membrane structure Monomer Membrane lcsh:Biology (General)chemistry Biochemistry Oligomer Membrane binding General Agricultural and Biological Sciences IM30 PspA/IM30 family

description

ABSTRACTPspA, 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.

year	journal	country	edition	language
2017-01-02	Communicative & Integrative Biology

https://doi.org/10.1080/19420889.2016.1264546

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