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Genome-wide identification of evolutionarily conserved Small Heat-Shock and eight other proteins bearing α-crystallin domain-like in kinetoplastid protists.
- Source :
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PloS one [PLoS One] 2018 Oct 22; Vol. 13 (10), pp. e0206012. Date of Electronic Publication: 2018 Oct 22 (Print Publication: 2018). - Publication Year :
- 2018
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Abstract
- 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 TryACD: four previously recognized (HSP20, Tryp23A, Tryp23B and ATOM69), and four characterized for the first time in kinetoplastids (TryACDP, TrySGT1, TryDYX1C1 and TryNudC). A single copy of each ortholog was identified in each genome alongside TryNudC1/TrypNudC2 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.<br />Competing Interests: The authors have declared that no competing interests exist.
- Subjects :
- Amino Acid Sequence
Cilia metabolism
Cytoskeleton metabolism
Mitochondria metabolism
Mitochondrial Proteins metabolism
Phylogeny
Prokaryotic Cells metabolism
Protein Domains
Synteny genetics
Conserved Sequence
Evolution, Molecular
Genome
Heat-Shock Proteins, Small chemistry
Heat-Shock Proteins, Small genetics
Trypanosomatina genetics
alpha-Crystallins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 13
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 30346990
- Full Text :
- https://doi.org/10.1371/journal.pone.0206012