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Cell Mol Life Sci. 2010 Apr;67(7):1077-88. doi: 10.1007/s00018-009-0234-9. Epub 2009 Dec 29.

Helix insertion into bilayers and the evolution of membrane proteins.

Author information

1
Department of Biology, University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX, 78249, USA. Robert.Renthal@UTSA.edu

Abstract

Polytopic alpha-helical membrane proteins cannot spontaneously insert into lipid bilayers without assistance from polytopic alpha-helical membrane proteins that already reside in the membrane. This raises the question of how these proteins evolved. Our current knowledge of the insertion of alpha-helices into natural and model membranes is reviewed with the goal of gaining insight into the evolution of membrane proteins. Topics include: translocon-dependent membrane protein insertion, antibiotic peptides and proteins, in vitro insertion of membrane proteins, chaperone-mediated insertion of transmembrane helices, and C-terminal tail-anchored (TA) proteins. Analysis of the E. coli genome reveals several predicted C-terminal TA proteins that may be descendents of proteins involved in pre-cellular membrane protein insertion. Mechanisms of pre-translocon polytopic alpha-helical membrane protein insertion are discussed.

KEYWORDS:

Bacteriocins; Chaperones; Tail-anchored proteins; Translocons; α-Helical membrane proteins

PMID:
20039094
PMCID:
PMC2862650
DOI:
10.1007/s00018-009-0234-9
[Indexed for MEDLINE]
Free PMC Article
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