A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components

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FIGURE 2.
FIGURE 2.

Protein sequence alignments of gRNA-binding proteins. (A) The L. tarentolae Ltp26 amino acid sequence aligned with gBP25 from T. brucei and gBP27 from C. fasciculata (Blom et al. 2001). (B) The L. tarentolae Ltp28 amino acid sequence aligned with gBP29 from C. fasciculata (Blom et al. 2001) and gBP21 from T. brucei (Koller et al. 1997). (C) Motifs conserved between the p26 and p28 homologs from all three species. The alignments above were obtained using AlignX in the Vector NTI Suite (Informax). The extent of nucleotide similarity is color-coded: blue on cyan denotes a consensus residue from a block of similar residues at a given location; black denotes nonhomologous residues; black on green denotes a consensus residue from a single conservative residue at a given location; red on yellow denotes a consensus residue from completely conservative residues at a given position. The predicted mitochondrial signal sequence cleavage sites in A and B are indicated by arrows, and the internal peptides obtained by microsequencing are indicated with lines.

This Article

  1. RNA 9: 62-76