Identification of conserved motifs selected for functional analysis of MSL2.

<p>(A) Topology of MscS and predicted topology of MSL2. Dark grey box, chloroplast transit peptide. Light grey boxes, transmembrane helices. (B) The MscS domain according to an alignment of the conserved region of <i>E. coli</i> MscS and five representative MscS-Like (MSL) proteins from <i>A. thaliana</i>. Double dots and asterisks indicate similar and conserved residues, respectively. Sequences corresponding to TM3a, TM3b, and the ß-domain of MscS are indicated by lines <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040336#pone.0040336-Bass1" target="_blank">[21]</a>. (C–F) Ribbon diagram of a single subunit of MscS from the revised Rees crystal structure (PDB 20AU <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040336#pone.0040336-Steinbacker1" target="_blank">[13]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040336#pone.0040336-Bass1" target="_blank">[21]</a>). The three conserved motifs functionally characterized in this report are highlighted in blue, (MscS L109, MSL2 V273/L277); yellow (MscS P129, MSL2 P297); and green (MscS P166/N167/N177; MSL2 P339/N340/N350) in (B) and shown in red in (D–F).