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Small Heat-Shock Proteins (sHSPs) and other proteins bearing alpha-crystallin domains (ACD) participate in defense against heat and oxidative stress and play important roles in cell cycle, cytoskeleton dynamics, and immunological and pathological mechanisms in eukaryotes. However, little is known about these proteins in early-diverging lineages of protists such as the kinetoplastids. Here, ACD-like proteins (ACDp) were investigated in genomes of 61 species of 12 kinetoplastid genera, including  Trypanosoma  spp. (23 species of mammals, reptiles and frogs),  Leishmania  spp. (mammals and lizards), trypanosomatids of insects,  Phytomonas  spp. of plants, and bodonids. Comparison of ACDps based on domain architecture, predicted tertiary structure, phylogeny and genome organization reveals a kinetoplastid evolutionarily conserved repertoire, which diversified prior to trypanosomatid adaptation to parasitic life. We identified 9 ACDp orthologs classified in 8 families of  Try ACD: four previously recognized (HSP20,  Try p23A,  Try p23B and ATOM69), and four characterized for the first time in kinetoplastids ( Try ACDP,  Try SGT1,  Try DYX1C1 and  Try NudC). A single copy of each ortholog was identified in each genome alongside  Try NudC1/ Try pNudC2 homologs and, overall, ACDPs were under strong selection pressures at main phylogenetic lineages. Transcripts of all ACDPs were identified across the life stages of  T. cruzi ,  T. brucei  and  Leishmania  spp., but proteomic profiles suggested that most ACDPs may be species- and stage-regulated. Our findings establish the basis for functional studies, and provided evolutionary and structural support for an underestimated repertoire of ACDps in the kinetoplastids.

plos one

Genome-wide identification of evolutionarily conserved Small Heat-Shock and eight other proteins bearing α-crystallin domain-like in kinetoplastid protists