ArticleScientific reports2017
DrwH, a novel WHy domain-containing hydrophobic LEA5C protein from Deinococcus radiodurans, protects enzymatic activity under oxidative stress.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 25 citations in OpenAlex.
- A Cold-Induced LEA3 Protein, DohD, Confers Cryoprotective Protection Against Low-Temperature Stress inInternational journal of molecular sciences · 2025Article
- Improved Salt Tolerance inInternational journal of molecular sciences · 2025Article
- Artificial Proteins Designed from G3LEA Contribute to Enhancement of Oxidation Tolerance inAntioxidants (Basel, Switzerland) · 2023Article
- A Novel Glycoside Hydrolase DogH Utilizing Soluble Starch to Maltose Improve Osmotic Tolerance inInternational journal of molecular sciences · 2023Article
- Article
- Pleiotropic roles of late embryogenesis abundant proteins ofComputational and structural biotechnology journal · 2021Review
- The Novel ncRNA OsiR Positively Regulates Expression ofInternational journal of molecular sciences · 2020Article
- Comparative Proteomics Analysis Reveals New Features of the Oxidative Stress Response in the Polyextremophilic BacteriumMicroorganisms · 2020Article
- Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms.Microbial biotechnology · 2019Article
- Dissecting the Genomic Diversification of Late Embryogenesis Abundant (LEA) Protein Gene Families in Plants.Genome biology and evolution · 2019Article
- Structural Plasticity of Intrinsically Disordered LEA Proteins fromFrontiers in plant science · 2019Article
- MiningInternational journal of molecular sciences · 2018Article
- Alleviation of adverse effects of drought stress on wheat seed germination using atmospheric dielectric barrier discharge plasma treatment.Scientific reports · 2017Article
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22 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Water stress and hypersensitive response (WHy) domain is typically found as a component of atypical late embryogenesis abundant (LEA) proteins closely associated with resistance to multiple stresses in numerous organisms. Several putative LEA proteins have been identified in Deinococcus bacteria; however their precise function remains unclear. This work reports the characterization of a Deinococcus-specific gene encoding a novel WHy domain-containing hydrophobic LEA5C protein (named DrwH) in D. radiodurans R1. The expression of the drwH gene was induced by oxidative and salinity stresses. Inactivation of this gene resulted in increased sensitivity to oxidative and salinity stresses as well as reduced activities of antioxidant enzymes. The WHy domain of the DrwH protein differs structurally from that of a previously studied bacterial LEA5C protein, dWHy1, identified as a gene product from an Antarctic desert soil metagenome library. Further analysis indicated that in E. coli, the function of DrwH is related to oxidative stress tolerance, whereas dWHy1 is associated with freezing-thawing stress tolerance. Under oxidative stress induced by H
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