A common evolutionary origin reveals fundamental principles of protein insertases

F-Nora Vögtle; Hans-Georg Koch; Chris Meisinger

doi:10.1371/journal.pbio.3001558

A common evolutionary origin reveals fundamental principles of protein insertases

PLoS Biol. 2022 Mar 2;20(3):e3001558. doi: 10.1371/journal.pbio.3001558. eCollection 2022 Mar.

Authors

F-Nora Vögtle^{1

2

3}, Hans-Georg Koch⁴, Chris Meisinger^{3

4

5}

Affiliations

¹ Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany.
² Network Aging Research, Heidelberg University, Heidelberg, Germany.
³ CIBSS-Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
⁴ Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
⁵ BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany.

Abstract

Membrane proteins require protein machineries to insert their hydrophobic transmembrane domains (TMDs) into the lipid bilayer. A functional analysis of protein insertases in this issue of PLOS Biology reveals that the fundamental mechanism of membrane protein insertion is universally conserved.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Hydrophobic and Hydrophilic Interactions
Lipid Bilayers* / chemistry
Membrane Proteins* / genetics
Membrane Proteins* / metabolism

Substances

Lipid Bilayers
Membrane Proteins

Grants and funding

Work of the authors laboratories is supported by the Deutsche Forschungsgemeinschaft (DFG), under Germany's Excellence Strategy (CIBSS - EXC-2189 - Project ID 390939984 to C.M. and F.N.V.), the RTG 2202 (to H.G.K. and C.M.), KO2184/8 and KO2184/9 (to H.G.K.) and the SFB1381 (Project-ID 403222702; to F.N.V., H.G.K. and C.M.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.