scholarly journals Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli.

1996 ◽  
Vol 15 (18) ◽  
pp. 4798-4805 ◽  
Author(s):  
P. Blount ◽  
S. I. Sukharev ◽  
P. C. Moe ◽  
M. J. Schroeder ◽  
H. R. Guy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Topology ◽  
Mechanosensitive Channel ◽  
Channel Protein

scholarly journals Identification of mutations that alter the gating of the Escherichia coli mechanosensitive channel protein, MscK

2007 ◽  
Vol 66 (2) ◽  
pp. 552-552
Author(s):  
Chan Li ◽  
Michelle D. Edwards ◽  
Hotcherl Jeong ◽  
John Roth ◽  
Ian R. Booth
Keyword(s):  
Escherichia Coli ◽  
Mechanosensitive Channel ◽  
Channel Protein

scholarly journals Identification of mutations that alter the gating of the Escherichia coli mechanosensitive channel protein, MscK

2007 ◽  
Vol 64 (2) ◽  
pp. 560-574 ◽  
Author(s):  
Chan Li ◽  
Michelle D. Edwards ◽  
Hochterl Jeong ◽  
John Roth ◽  
Ian R. Booth
Keyword(s):  
Escherichia Coli ◽  
Mechanosensitive Channel ◽  
Channel Protein

scholarly journals Membrane topology of the Escherichia coli ExbD protein.

1992 ◽  
Vol 174 (16) ◽  
pp. 5485-5487 ◽  
Author(s):  
K Kampfenkel ◽  
V Braun
Keyword(s):  
Escherichia Coli ◽  
Membrane Topology

Temperature-sensitive mutants of MscL mechanosensitive channel

2019 ◽  
Vol 166 (3) ◽  
pp. 281-288 ◽  
Author(s):  
Naoto Owada ◽  
Megumi Yoshida ◽  
Kohei Morita ◽  
Kenjiro Yoshimura
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Structural Change ◽  
Cell Growth ◽  
Thermodynamic Stability ◽  
Transmembrane Helix ◽  
Mechanosensitive Channel ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Membrane Stretching

Abstract MscL is a mechanosensitive channel that undergoes a global conformational change upon application of membrane stretching. To elucidate how the structural stability and flexibility occur, we isolated temperature-sensitive (Ts) mutants of Escherichia coli MscL that allowed cell growth at 32°C but not at 42°C. Two Ts mutants, L86P and D127V, were identified. The L86P mutation occurred in the second transmembrane helix, TM2. Substitution of residues neighbouring L86 with proline also led to a Ts mutation, but the substitution of L86 with other amino acids did not result in a Ts phenotype, indicating that the Ts phenotype was due to a structural change of TM2 helix by the introduction of a proline residue. The D127V mutation was localized in the electrostatic belt of the bundle of cytoplasmic helices, indicating that stability of the pentameric bundle of the cytoplasmic helix affects MscL structure. Together, this study described a novel class of MscL mutations that were correlated with the thermodynamic stability of the MscL structure.

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