4.6 Article

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

期刊

MOLECULES
卷 27, 期 9, 页码 -

出版社

MDPI
DOI: 10.3390/molecules27092934

关键词

dehydrin; Arctic mouse-ear chickweed; intermolecular disulfide bond; reactive oxygen species; dimerization; cysteine

资金

  1. National Research Foundation of Korea Grant from the Korean Government (MSIT
  2. the Ministry of Science and ICT) [NRF-2021M1A5A1075524, KOPRIPN22014]
  3. Ministry of Oceans and Fisheries, Korea [15250103, PM22030]
  4. National Research Foundation of Korea [2021M1A5A1075524] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

向作者/读者索取更多资源

The CaDHN gene from the Arctic mouse-ear chickweed contains an unusual single cysteine residue that can form intermolecular disulfide bonds, enhancing the plant's tolerance to abiotic stress by regulating protein dimerization.
The stress-responsive, SK5 subclass, dehydrin gene, CaDHN, has been identified from the Arctic mouse-ear chickweed Cerastium arcticum. 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 C. arcticum 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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