PlantGlutaTransV1, Main, Exploration, bibRecord, 000141

Glutathione S-transferase: a versatile protein family.

Identifieur interne : 000141 ( Main/Exploration ); précédent : 000140; suivant : 000142

Glutathione S-transferase: a versatile protein family.

Auteurs : Swati Vaish ; Divya Gupta ; Rajesh Mehrotra ; Sandhya Mehrotra ; Mahesh Kumar Basantani

Source :

3 Biotech [ 2190-572X ] ; 2020.

RBID : pubmed:32656054

Abstract

Glutathione-S transferase (GST) is a most ancient protein superfamily of multipurpose roles and evolved principally from gene duplication of an ancestral GSH binding protein. They have implemented in diverse plant functions such as detoxification of xenobiotic, secondary metabolism, growth and development, and majorly against biotic and abiotic stresses. The vital structural features of GSTs like highly divergent functional topographies, conserved integrated architecture with separate binding pockets for substrates and ligand, the stringent structural fidelity with high Tm values (50º-60º), and stress-responsive cis-regulatory elements in the promoter region offer this protein as most flexible plant protein for plant breeding approaches, biotechnological applications, etc. This review article summarizes the recent information of GST evolution, and their distribution and structural features with emphasis on the assorted roles of Ser and Cys GSTs with the signature motifs in their active sites, alongside their recent biotechnological application in the area of agriculture, environment, and nanotechnology have been highlighted.

DOI: 10.1007/s13205-020-02312-3
PubMed: 32656054
PubMed Central: PMC7320970

Affiliations:

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<front><div type="abstract" xml:lang="en">Glutathione-S transferase (GST) is a most ancient protein superfamily of multipurpose roles and evolved principally from gene duplication of an ancestral GSH binding protein. They have implemented in diverse plant functions such as detoxification of xenobiotic, secondary metabolism, growth and development, and majorly against biotic and abiotic stresses. The vital structural features of GSTs like highly divergent functional topographies, conserved integrated architecture with separate binding pockets for substrates and ligand, the stringent structural fidelity with high Tm values (50º-60º), and stress-responsive cis-regulatory elements in the promoter region offer this protein as most flexible plant protein for plant breeding approaches, biotechnological applications, etc. This review article summarizes the recent information of GST evolution, and their distribution and structural features with emphasis on the assorted roles of Ser and Cys GSTs with the signature motifs in their active sites, alongside their recent biotechnological application in the area of agriculture, environment, and nanotechnology have been highlighted.</div>
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<tree><noCountry><name sortKey="Basantani, Mahesh Kumar" sort="Basantani, Mahesh Kumar" uniqKey="Basantani M" first="Mahesh Kumar" last="Basantani">Mahesh Kumar Basantani</name>
<name sortKey="Gupta, Divya" sort="Gupta, Divya" uniqKey="Gupta D" first="Divya" last="Gupta">Divya Gupta</name>
<name sortKey="Mehrotra, Rajesh" sort="Mehrotra, Rajesh" uniqKey="Mehrotra R" first="Rajesh" last="Mehrotra">Rajesh Mehrotra</name>
<name sortKey="Mehrotra, Sandhya" sort="Mehrotra, Sandhya" uniqKey="Mehrotra S" first="Sandhya" last="Mehrotra">Sandhya Mehrotra</name>
<name sortKey="Vaish, Swati" sort="Vaish, Swati" uniqKey="Vaish S" first="Swati" last="Vaish">Swati Vaish</name>
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Glutathione S-transferase: a versatile protein family.

Glutathione S-transferase: a versatile protein family.

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