A Cold-Induced LEA3 Protein, DohD, Confers Cryoprotective Protection Against Low-Temperature Stress in Deinococcus radiodurans DOI Open Access

Wenxiu Wang,

Zhi Qi,

Chunxia Yan

et al.

International Journal of Molecular Sciences, Journal Year: 2025, Volume and Issue: 26(8), P. 3511 - 3511

Published: April 9, 2025

Deinococcus radiodurans is a remarkably unique microorganism, exhibiting extraordinary tolerance to extreme conditions such as ionizing radiation, ultraviolet light, and desiccation. However, the response mechanisms of D. under low-temperature stress remain largely unexplored have yet be fully elucidated. The DohD protein hydrophilic member late embryogenesis abundant 3 (LEA3) family radiodurans, playing pivotal role in abiotic adaptation. Bioinformatics analysis revealed that contains tandem repeats disordered domains, with high α-helix content (91.41%). Furthermore, exhibits extremely low homology other proteins, highlighting its uniqueness radiodurans. Under (15 °C), expression dohD was significantly upregulated (5-fold), regulated by dual mechanism involving positive control DrRRA negative regulation Csp. Circular dichroism spectroscopy unveiled temperature-dependent structural plasticity: temperature increased from 0 °C 50° C, decreased 23.5% 18.7%, while antiparallel β-sheet 31.3% 50.8%. This suggests an interconversion strategy for thermal Additionally, deletion impaired cold, desiccation, oxidative, high-salt stresses, accompanied reduced activities antioxidant enzymes (SOD, CAT, POD) downregulation related gene expression. study elucidates multifunctional resistance through dynamics, transcriptional regulation, redox homeostasis, providing valuable insights into adaptation extremophiles.

Language: Английский

A Cold-Induced LEA3 Protein, DohD, Confers Cryoprotective Protection Against Low-Temperature Stress in Deinococcus radiodurans DOI Open Access

Wenxiu Wang,

Zhi Qi,

Chunxia Yan

et al.

International Journal of Molecular Sciences, Journal Year: 2025, Volume and Issue: 26(8), P. 3511 - 3511

Published: April 9, 2025

Deinococcus radiodurans is a remarkably unique microorganism, exhibiting extraordinary tolerance to extreme conditions such as ionizing radiation, ultraviolet light, and desiccation. However, the response mechanisms of D. under low-temperature stress remain largely unexplored have yet be fully elucidated. The DohD protein hydrophilic member late embryogenesis abundant 3 (LEA3) family radiodurans, playing pivotal role in abiotic adaptation. Bioinformatics analysis revealed that contains tandem repeats disordered domains, with high α-helix content (91.41%). Furthermore, exhibits extremely low homology other proteins, highlighting its uniqueness radiodurans. Under (15 °C), expression dohD was significantly upregulated (5-fold), regulated by dual mechanism involving positive control DrRRA negative regulation Csp. Circular dichroism spectroscopy unveiled temperature-dependent structural plasticity: temperature increased from 0 °C 50° C, decreased 23.5% 18.7%, while antiparallel β-sheet 31.3% 50.8%. This suggests an interconversion strategy for thermal Additionally, deletion impaired cold, desiccation, oxidative, high-salt stresses, accompanied reduced activities antioxidant enzymes (SOD, CAT, POD) downregulation related gene expression. study elucidates multifunctional resistance through dynamics, transcriptional regulation, redox homeostasis, providing valuable insights into adaptation extremophiles.

Language: Английский

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