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Evolutionary analysis of globin domains from kinetoplastids
Akash Mitra1,2, Kusumita Acharya1, Arijit Bhattacharya3
1Department of Microbiology, Adamas University, Barasat-Barrackpore Rd, Kolkata, 700126, India.
Archives of Microbiology
|July 16, 2022
Summary
Globin domains in kinetoplastids evolved differently, with some fused to adenylate cyclase or oxidoreductase. Leishmania
Area of Science:
- Parasitology
- Evolutionary Biology
- Molecular Biology
Background:
- Globin (Gb) domains are crucial for sensing gaseous ligands like oxygen and nitric oxide.
- Gb domain-containing heme binding adenylate cyclases (GbAC) modulate Leishmania's response to stress.
- Kinetoplastids exhibit diverse lifestyles and varying Gb-domain distributions.
Purpose of the Study:
- To explore the evolution of Gb-domains across different kinetoplastid groups.
- To investigate the origin and functional divergence of Gb-domain containing proteins in Leishmania.
Main Methods:
- Comparative genomics and evolutionary analysis (codon adaptation, orthologue-paralogue, synteny analysis).
- Structural alignment and heme-binding residue prediction.
- Phylogenetic analysis of GbOxR and bacterial flavohemoglobins.
Main Results:
- GbOxR domains cluster with bacterial flavohemoglobins.
- Leishmania's sole Gb-domain protein (OsAC) likely acquired via horizontal gene transfer.
- Significant functional divergence exists between GbAC and GbOxR orthologues.
- Genomic reduction of GbOxR and GbAC loci observed in dixenous trypanosomatids.
Conclusions:
- Gb-domain evolution in kinetoplastids is marked by fusion events and potential horizontal gene transfer.
- Functional divergence and genomic reduction shaped the diversity of Gb-domain proteins in kinetoplastids.
- Understanding Gb-domain evolution provides insights into kinetoplastid adaptation to host environments.
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