Investigating the Functional Role of the Cysteine Residue in Dehydrin from the Arctic Mouse-Ear Chickweed

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2022 May 14

PMID 35566285

Authors

Il-Sup Kim

Woong Choi

Ae Kyung Park

Hyun Kim

Jonghyeon Son

Jun Hyuck Lee

Seung Chul Shin

T Doohun Kim

Han-Woo Kim

Affiliations

Soon will be listed here.

Abstract

The stress-responsive, SK subclass, dehydrin gene, , has been identified from the Arctic mouse-ear chickweed . CaDHN contains an unusual single cysteine residue (Cys143), which can form intermolecular disulfide bonds. Mutational analysis and a redox experiment confirmed that the dimerization of CaDHN was the result of an intermolecular disulfide bond between the cysteine residues. The biochemical and physiological functions of the mutant C143A were also investigated by in vitro and in vivo assays using yeast cells, where it enhanced the scavenging of reactive oxygen species (ROS) by neutralizing hydrogen peroxide. Our results show that the cysteine residue in CaDHN helps to enhance tolerance to abiotic stress by regulating the dimerization of the intrinsically disordered CaDHN protein, which acts as a defense mechanism against extreme polar environments.

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