European Biophysics Journal

, 38:1013

Conserved motifs in mechanosensitive channels MscL and MscS

Biophysics Letter

DOI: 10.1007/s00249-009-0460-y

Cite this article as:
Balleza, D. & Gómez-Lagunas, F. Eur Biophys J (2009) 38: 1013. doi:10.1007/s00249-009-0460-y

Abstract

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.

Keywords

Mechanosensitive channels Motifs Sequence logos 

Abbreviations

MS

Mechanosensitive ion channels

EcoMscL

Escherichiacoli MscL

TbMscL

Mycobacteriumtuberculosis MscL

EcoMscS

Escherichiacoli MscS

WT

Wild type

Supplementary material

249_2009_460_MOESM1_ESM.pdf (88 kb)
Table S1. MscL Family (PDF 88 kb)
249_2009_460_MOESM2_ESM.pdf (22 kb)
Table S2. MscS Family (PDF 22 kb)
249_2009_460_MOESM3_ESM.jpg (880 kb)
Figure S1. Multiple alignment of representative MscL and MscS proteins from prokaryotic and eukaryotic sources. The MscL sequences were from Escherichia coli (gi: 169890645), Rhizobium etli (gi: 86356220), Mycobacterium tuberculosis (gi: 148660766), Staphylococcus aureus (gi: 49483541), Methanoregula boonei (gi: 154151033), Methanosaeta thermophila (gi: 116754059), Aspergillus clavatus (gi: 121712146) and Magnaporthe grisea (gi: 145613616). The MscS sequences were from E. coli (gi: 16130825), R. etli (gi: 86357039), B. cereus (gi: 152977676), S. aureus (gi: 150392894), Methanocaldococcus jannaschii (gi: 2501530), Methanoregula boonei (gi: 154150843), Arabidopsis thaliana (gi: 27363434) (AtMSL3) and Chlamydomonas reinhardtii (gi: 159464821) (MSC1) (JPG 879 kb)
249_2009_460_MOESM4_ESM.jpg (558 kb)
Figure S2. Structure of TbMscL (M. tuberculosis) with the location of highly conserved residues defined by Weblogo in homologs for the three domains of life. We show the equivalent positions to numbering of E. coli: A20 [A18], I24 [V22], V33 [V31], S35 [K33], V37 [T35], I40 [I38] and P43 [P41] (TM1) and separately G76 [N70], F78 [L72] and F85 [F79] (TM2). The structure is based on the data set of 2OAR in the Protein Data Bank (JPG 557 kb)
249_2009_460_MOESM5_ESM.jpg (556 kb)
Figure S3. Structure of EcoMscS (E. coli) with the location of highly conserved residues defined by Weblogo in homologs for the three domains of life. We show the follow positions: G101, G104, G108, A110, N117 and G121 (TM3) in the context of the whole protein. The structure is based on the data set of 2OAU in the Protein Data Bank (JPG 555 kb)

Copyright information

© European Biophysical Societies' Association 2009

Authors and Affiliations

  1. 1.Laboratory of Molecular BiologyUniversity of WisconsinMadisonUSA
  2. 2.Departmento de Fisiología, Facultad de MedicinaUNAM. México. Cd. UniversitariaMéxico DFMexico

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