The small heat shock proteins, chaperonin 10, in plants: An evolutionary view and emerging functional diversity

•MSA analysis of Cpn10 domains demonstrated conserved sites despite of divergence.•Phylogenetic analysis revealed expansion and diversification of Cpn10 gene family.•Ka/Ks ratio of homologous pairs suggested evolutionary conservancy of Cpn10.•Cpn10 predominantly interact with chloroplastic and mitoc...

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Bibliographic Details
Published in:Environmental and experimental botany 2021-02, Vol.182, p.104323, Article 104323
Main Authors: Pareek, Akanksha, Mishra, Divya, Rathi, Divya, Verma, Jitendra Kumar, Chakraborty, Subhra, Chakraborty, Niranjan
Format: Article
Language:English
Subjects:
Chaperonin
Cpn10 domains
Evolutionary lineage
Genome-wide analysis
Hormonal cross-talk
Localization prediction
Phylogenetic relationship
Stress tolerance
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Summary:•MSA analysis of Cpn10 domains demonstrated conserved sites despite of divergence.•Phylogenetic analysis revealed expansion and diversification of Cpn10 gene family.•Ka/Ks ratio of homologous pairs suggested evolutionary conservancy of Cpn10.•Cpn10 predominantly interact with chloroplastic and mitochondrial proteins.•Transcriptional regulation of theCaCpn10 genes suggested stress-adaptive responses. Small heat shock proteins (sHSPs) constitute a class of molecular chaperones, which are evolutionarily conserved yet diverse group of molecules, rapidly produced in response to stress. In this study, we sought to identify plant sHSPs, especially chaperonin 10 (Cpn10) family members in major evolutionary lineages, and determine their biological significance. Multiple sequence alignment of Cpn10 domains revealed divergent amino acids as well as conserved sites. Phylogenetic tree depicted the diversification and expansion of Cpn10 gene family. During the process of evolution, the Ka/Ks ratio of orthologous and paralogous pairs was
ISSN:0098-8472
1873-7307
DOI:10.1016/j.envexpbot.2020.104323