Lipid-protein interaction of the MscS mechanosensitive channel examined by scanning mutagenesis

Takeshi Nomura, Masahiro Sokabe, Kenjiro Yoshimura

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The mechanosensitive channel of small conductance (MscS) is a bacterial mechanosensitive channel that opens in response to rapid hypoosmotic stress. Since MscS can be opened solely by membrane stretch without help from any accessory protein, the lipid-protein interface must play a crucial role in sensing membrane tension. In this study, the hydrophobic residues in the lipid-protein interface were substituted one by one with a hydrophilic amino acid, asparagine, to modify the interaction between the protein and the lipid. Function of the mutant MscSs was examined by patch-clamp and hypoosmotic shock experiments. An increase in the gating threshold and a decrease in the viability on hypoosmotic shock were observed when the hydrophobic residues near either end of the first or the second transmembrane helix (TM1 or TM2) were replaced with asparagine. This observation indicates that the lipid-protein interaction at the ends of both helices (TM1 and TM2) is essential to MscS function.

Original languageEnglish
Pages (from-to)2874-2881
Number of pages8
JournalBiophysical Journal
Volume91
Issue number8
DOIs
Publication statusPublished - 2006 Oct
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

Cite this

Lipid-protein interaction of the MscS mechanosensitive channel examined by scanning mutagenesis. / Nomura, Takeshi; Sokabe, Masahiro; Yoshimura, Kenjiro.

In: Biophysical Journal, Vol. 91, No. 8, 10.2006, p. 2874-2881.

Research output: Contribution to journalArticle

@article{de1dfc47e41d427392124f7656c312d9,
title = "Lipid-protein interaction of the MscS mechanosensitive channel examined by scanning mutagenesis",
abstract = "The mechanosensitive channel of small conductance (MscS) is a bacterial mechanosensitive channel that opens in response to rapid hypoosmotic stress. Since MscS can be opened solely by membrane stretch without help from any accessory protein, the lipid-protein interface must play a crucial role in sensing membrane tension. In this study, the hydrophobic residues in the lipid-protein interface were substituted one by one with a hydrophilic amino acid, asparagine, to modify the interaction between the protein and the lipid. Function of the mutant MscSs was examined by patch-clamp and hypoosmotic shock experiments. An increase in the gating threshold and a decrease in the viability on hypoosmotic shock were observed when the hydrophobic residues near either end of the first or the second transmembrane helix (TM1 or TM2) were replaced with asparagine. This observation indicates that the lipid-protein interaction at the ends of both helices (TM1 and TM2) is essential to MscS function.",
author = "Takeshi Nomura and Masahiro Sokabe and Kenjiro Yoshimura",
year = "2006",
month = "10",
doi = "10.1529/biophysj.106.084541",
language = "English",
volume = "91",
pages = "2874--2881",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "8",

}

TY - JOUR

T1 - Lipid-protein interaction of the MscS mechanosensitive channel examined by scanning mutagenesis

AU - Nomura, Takeshi

AU - Sokabe, Masahiro

AU - Yoshimura, Kenjiro

PY - 2006/10

Y1 - 2006/10

N2 - The mechanosensitive channel of small conductance (MscS) is a bacterial mechanosensitive channel that opens in response to rapid hypoosmotic stress. Since MscS can be opened solely by membrane stretch without help from any accessory protein, the lipid-protein interface must play a crucial role in sensing membrane tension. In this study, the hydrophobic residues in the lipid-protein interface were substituted one by one with a hydrophilic amino acid, asparagine, to modify the interaction between the protein and the lipid. Function of the mutant MscSs was examined by patch-clamp and hypoosmotic shock experiments. An increase in the gating threshold and a decrease in the viability on hypoosmotic shock were observed when the hydrophobic residues near either end of the first or the second transmembrane helix (TM1 or TM2) were replaced with asparagine. This observation indicates that the lipid-protein interaction at the ends of both helices (TM1 and TM2) is essential to MscS function.

AB - The mechanosensitive channel of small conductance (MscS) is a bacterial mechanosensitive channel that opens in response to rapid hypoosmotic stress. Since MscS can be opened solely by membrane stretch without help from any accessory protein, the lipid-protein interface must play a crucial role in sensing membrane tension. In this study, the hydrophobic residues in the lipid-protein interface were substituted one by one with a hydrophilic amino acid, asparagine, to modify the interaction between the protein and the lipid. Function of the mutant MscSs was examined by patch-clamp and hypoosmotic shock experiments. An increase in the gating threshold and a decrease in the viability on hypoosmotic shock were observed when the hydrophobic residues near either end of the first or the second transmembrane helix (TM1 or TM2) were replaced with asparagine. This observation indicates that the lipid-protein interaction at the ends of both helices (TM1 and TM2) is essential to MscS function.

UR - http://www.scopus.com/inward/record.url?scp=33749527976&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749527976&partnerID=8YFLogxK

U2 - 10.1529/biophysj.106.084541

DO - 10.1529/biophysj.106.084541

M3 - Article

VL - 91

SP - 2874

EP - 2881

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 8

ER -