Conserved motifs in mechanosensitive channels MscL and MscS
被引:51
作者:
Balleza, Daniel
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机构:
Univ Wisconsin, Mol Biol Lab, Madison, WI 53706 USA
Univ Nacl Autonoma Mexico, Fac Med, Dept Fisiol, Mexico City 04510, DF, MexicoUniv Wisconsin, Mol Biol Lab, Madison, WI 53706 USA
Balleza, Daniel
[1
,2
]
Gomez-Lagunas, Froylan
论文数: 0引用数: 0
h-index: 0
机构:
Univ Nacl Autonoma Mexico, Fac Med, Dept Fisiol, Mexico City 04510, DF, MexicoUniv Wisconsin, Mol Biol Lab, Madison, WI 53706 USA
Gomez-Lagunas, Froylan
[2
]
机构:
[1] Univ Wisconsin, Mol Biol Lab, Madison, WI 53706 USA
[2] Univ Nacl Autonoma Mexico, Fac Med, Dept Fisiol, Mexico City 04510, DF, Mexico
来源:
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
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2009年
/
38卷
/
07期
Mechanosensitive (MS) channels play a major role in protecting bacterial cells against hypo-osmotic shock. To understand their function, it is important to identify the conserved motifs using sequence analysis methods. In this study, the sequence conservation was investigated by an in silico analysis to generate sequence logos. We have identified new conserved motifs in the domains TM1, TM2 and the cytoplasmic helix from 231 homologs of MS channel of large conductance (MscL). In addition, we have identified new motifs for the TM3 and the cytoplasmic carboxy-terminal domain from 309 homologs of MS channel of small conductance (MscS). We found that the conservation in MscL homologs is high for TM1 and TM2 in the three domains of life. The conservation in MscS homologs is high only for TM3 in Bacteria and Archaea.