Figure 1.

Alignment of bacterial-type and tRNase ZS-like candidates in green plants. Bacterial-type tRNase ZSs are from P. patens (PpaTRZ3), O. lucimarinus (OluTRZ2), M. pusilla (MpuTRZ2), Synechocystis sp. PCC 6803 (slr0050), E. coli (EcoTrz1) [72], B. subtilis (BsuTrz1) [60] and humans (HsaTrz1) [14]. Plant tRNase ZS-like (TLP) candidates are from S. moellendorffii (SmoTLP1 and SmoTLP2), V. carteri (VcaTLP1), C. reinhardtii (CreTLP1 and CreTLP2). TM-type tRNase ZSs from T. maritima (TmaTrz1) [30] and A. thaliana (AthTRZ1) [20] are included for comparison. The alignment was constructed using Clustal W [68]. Identical residues are on a black ground and conserved residues shared in gray. Also indicated above the alignment are the conserved motifs of tRNase Zs, which are labeled according to references [33,40,41]. The numbers in brackets indicate the length of the region in the protein, which are species-specific and could not be correctly aligned. Hyphens represent gaps introduced into sequences for maximum alignment. Amino acid residues predicted to be critical for activity are indicated by a star.

Fan et al. BMC Evolutionary Biology 2011 11:219   doi:10.1186/1471-2148-11-219
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