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      Pleiotropic roles of late embryogenesis abundant proteins of Deinococcus radiodurans against oxidation and desiccation

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          Abstract

          Deinococcus radiodurans, an important extremophile, possesses extraordinary stress tolerance ability against lethal and mutagenic effects of DNA-damaging agents, such as γ-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 manner 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.

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          Most cited references85

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          THE MOLECULAR BASIS OF DEHYDRATION TOLERANCE IN PLANTS.

          Molecular studies of drought stress in plants use a variety of strategies and include different species subjected to a wide range of water deficits. Initial research has by necessity been largely descriptive, and relevant genes have been identified either by reference to physiological evidence or by differential screening. A large number of genes with a potential role in drought tolerance have been described, and major themes in the molecular response have been established. Particular areas of importance are sugar metabolism and late-embryogenesis-abundant (LEA) proteins. Studies have begun to examine mechanisms that control the gene expression, and putative regulatory pathways have been established. Recent attempts to understand gene function have utilized transgenic plants. These efforts are of clear agronomic importance.
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            Reconciling the chemistry and biology of reactive oxygen species.

            There is a vast literature on the generation and effects of reactive oxygen species in biological systems, both in relation to damage they cause and their involvement in cell regulatory and signaling pathways. The biological chemistry of different oxidants is becoming well understood, but it is often unclear how this translates into cellular mechanisms where redox changes have been demonstrated. This review addresses this gap. It examines how target selectivity and antioxidant effectiveness vary for different oxidants. Kinetic considerations of reactivity are used to assess likely targets in cells and how reactions might be influenced by restricted diffusion and compartmentalization. It also highlights areas where greater understanding is required on the fate of oxidants generated by cellular NADPH oxidases and on the identification of oxidant sensors in cell signaling.
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              The continuing conundrum of the LEA proteins.

              Research into late embryogenesis abundant (LEA) proteins has been ongoing for more than 20 years but, although there is a strong association of LEA proteins with abiotic stress tolerance particularly dehydration and cold stress, for most of that time, their function has been entirely obscure. After their initial discovery in plant seeds, three major groups (numbered 1, 2 and 3) of LEA proteins have been described in a range of different plants and plant tissues. Homologues of groups 1 and 3 proteins have also been found in bacteria and in certain invertebrates. In this review, we present some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlight several possible functions. These include roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as "space fillers" to prevent cellular collapse at low water activities. This multifunctional capacity of the LEA proteins is probably attributable in part to their structural plasticity, as they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. The challenge now facing researchers investigating these enigmatic proteins is to make sense of the various in vitro defined functions in the living cell: Are the LEA proteins truly multi-talented, or are they still just misunderstood?
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                Author and article information

                Contributors
                Journal
                Comput Struct Biotechnol J
                Comput Struct Biotechnol J
                Computational and Structural Biotechnology Journal
                Research Network of Computational and Structural Biotechnology
                2001-0370
                04 June 2021
                2021
                04 June 2021
                : 19
                : 3407-3415
                Affiliations
                [a ]Department of Biomedical Sciences, School of Medicine and Health Sciences, University of North Dakota, Grand Forks, ND 58203-9037, USA
                [b ]Laboratory of Microbiology, Wageningen University & Research, Wageningen 6708 WE, The Netherlands
                [c ]Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China
                Author notes
                [1]

                The authors contributed equally to this work.

                Article
                S2001-0370(21)00238-5
                10.1016/j.csbj.2021.05.051
                8213827
                34188783
                a6d77ae7-9b64-4229-8dd1-dd998bdc7295
                © 2021 The Authors

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                : 1 March 2021
                : 30 May 2021
                : 30 May 2021
                Categories
                Review Article

                deinococcus radiodurans,late embryogenesis abundant proteins,dr1172,dr1372,oxidation,desiccation

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