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Late Embryogenesis Abundant Protein–Client Protein Interactions

Department of Horticulture, University of Kentucky Seed Biology Program, Plant Science Building, 1405 Veterans Drive, University of Kentucky, Lexington, KY 40546-0312, USA
Agriculture College, Al-Muthanna University, Samawah, Al-Muthanna 66001, Iraq
Department of Horticulture, Faculty of Crop Production Sciences, The University of Agriculture, Peshawar, Khyber Pakhtunkhwa 25120, Pakistan
Agroceres, Inc., Patos de Minas, Minas Gerais CEP: 38703-240, Brazil
Departamento de Agricultura—Setor de Sementes, Federal University of Lavras, Lavras, Minas Gerais CEP: 37200-000, Brazil
Germisul Ltd., Campo Grande, Mato Grosso do Sul CEP: 79108-011, Brazil
Department of Vegetable Production, (UNESP) National University of São Paulo, Jaboticabal, São Paulo CEP: 14884-900, Brazil
Department of Biology, Faculty of Philosophy, Science and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo CEP: 14040-901, Brazil
Author to whom correspondence should be addressed.
Plants 2020, 9(7), 814;
Received: 28 May 2020 / Revised: 22 June 2020 / Accepted: 24 June 2020 / Published: 29 June 2020
The intrinsically disordered proteins belonging to the LATE EMBRYOGENESIS ABUNDANT protein (LEAP) family have been ascribed a protective function over an array of intracellular components. We focus on how LEAPs may protect a stress-susceptible proteome. These examples include instances of LEAPs providing a shield molecule function, possibly by instigating liquid-liquid phase separations. Some LEAPs bind directly to their client proteins, exerting a holdase-type chaperonin function. Finally, instances of LEAP–client protein interactions have been documented, where the LEAP modulates (interferes with) the function of the client protein, acting as a surreptitious rheostat of cellular homeostasis. From the examples identified to date, it is apparent that client protein modulation also serves to mitigate stress. While some LEAPs can physically bind and protect client proteins, some apparently bind to assist the degradation of the client proteins with which they associate. Documented instances of LEAP–client protein binding, even in the absence of stress, brings to the fore the necessity of identifying how the LEAPs are degraded post-stress to render them innocuous, a first step in understanding how the cell regulates their abundance. View Full-Text
Keywords: late embryogenesis abundant; protein interaction; desiccation; seed; natural protection and repair mechanism; stress late embryogenesis abundant; protein interaction; desiccation; seed; natural protection and repair mechanism; stress
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MDPI and ACS Style

Dirk, L.M.A.; Abdel, C.G.; Ahmad, I.; Neta, I.C.S.; Pereira, C.C.; Pereira, F.E.C.B.; Unêda-Trevisoli, S.H.; Pinheiro, D.G.; Downie, A.B. Late Embryogenesis Abundant Protein–Client Protein Interactions. Plants 2020, 9, 814.

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