Importance of hydrophobic matching for spontaneous insertion of a single-spanning membrane protein.

Abstract:

:In this study, we have investigated the effect of hydrophobic mismatch between the thickness of the membrane and a transmembrane segment of a protein that directly inserts into the membrane bilayer. For this purpose we used mutants of the single-spanning Pf3 coat protein that can spontaneously insert into Escherichia coli membrane vesicles and large unilamellar vesicles (LUVs). The thickness of the liposomal bilayer could be altered by using lipids with different acyl chain lengths or by incorporation of cholesterol. The insertion efficiency of the protein clearly depended on the bilayer thickness, with most efficient insertion under hydrophobic matching conditions. To discriminate between effects of length and hydrophobicity, mutants with different synthetic transmembrane segments were constructed. These mutants inserted into LUVs in a mismatch-dependent manner. However, in particular for longer and less hydrophobic mutants, most efficient insertion was generally observed in thinner bilayers than expected on the basis of hydrophobic matching.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Ridder AN,van de Hoef W,Stam J,Kuhn A,de Kruijff B,Killian JA

doi

10.1021/bi0158674

subject

Has Abstract

pub_date

2002-04-16 00:00:00

pages

4946-52

issue

15

eissn

0006-2960

issn

1520-4995

pii

bi0158674

journal_volume

41

pub_type

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