期刊
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL
卷 19, 期 -, 页码 3407-3415出版社
ELSEVIER
DOI: 10.1016/j.csbj.2021.05.0512001-0370/
关键词
Deinococcus radiodurans; Late embryogenesis abundant proteins; DR1172; DR1372; Oxidation; Desiccation
资金
- National Institutes of Health [R01 AI1138203, R01 AI109317-01A1, AI097532-01A1]
Deinococcus radiodurans is an extremophile with remarkable stress tolerance against DNA-damaging agents like gamma rays, ultraviolet radiation, oxidation, and desiccation. Global regulators of this bacterium play a crucial role in responding to oxidative and desiccation stresses. The Late Embryogenesis Abundant proteins (LEAs) in D. radiodurans are essential for stabilizing metabolic enzymes and maintaining metal ion homeostasis under oxidative and desiccation conditions, showing potential for biotechnological and therapeutic applications.
Deinococcus radiodurans, an important extremophile, possesses extraordinary stress tolerance ability against lethal and mutagenic effects of DNA-damaging agents, such as c-rays, ultraviolet, oxidation, and desiccation. How global regulators of this bacterium function in response to oxidation and desiccation has been an intense topic as elucidating such mechanisms may help to facilitate some beneficial applications in agriculture or medicine. Particularly, a variety of functional proteins have been characterized for D. radiodurans' behaviors under abiotic stresses. Interestingly, a group of Late Embryogenesis Abundant proteins (LEAs) in D. radiodurans have been characterized both biochemically and physiologically, which are shown indispensable for stabilizing crucial metabolic enzymes in a chaperone-like man-ner and thereby maintaining the metal ion homeostasis under oxidation and desiccation. The rapid progress in understanding deinococcal LEA proteins has substantially extended their functions in both plants and animals. Herein, we discuss the latest studies of radiodurans LEA proteins ranging from the classification to structures to functions. Importantly, the harnessing of these proteins may have unlimited potential for biotechnology, engineering and disease treatments. (C) 2021 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.
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