Membrane protein insertase YidC in bacteria and archaea.

Abstract:

:The insertion of proteins into the prokaryotic plasma membrane is catalyzed by translocases and insertases. On one hand, the Sec translocase operates as a transmembrane channel that can open laterally to first bind and then release the hydrophobic segments of a substrate protein into the lipid bilayer. On the other hand, YidC insertases interact with their substrates in a groove-like structure at an amphiphilic protein-lipid interface thus allowing the transmembrane segments of the substrate to slide into the lipid bilayer. The recently published high-resolution structures of YidC provide new mechanistic insights of how transmembrane proteins achieve the transition from an aqueous environment in the cytoplasm to the hydrophobic lipid bilayer environment of the membrane.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Kuhn A,Kiefer D

doi

10.1111/mmi.13586

subject

Has Abstract

pub_date

2017-02-01 00:00:00

pages

590-594

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

103

pub_type

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