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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Nomura T,Sokabe M,Yoshimura Kdoi
10.1529/biophysj.106.084541subject
Has Abstractpub_date
2006-10-15 00:00:00pages
2874-81issue
8eissn
0006-3495issn
1542-0086pii
S0006-3495(06)72001-Xjournal_volume
91pub_type
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