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      Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity

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          Abstract

          As sessile organisms, plants are exposed to persistently changing stresses and have to be able to interpret and respond to them. The stresses, drought, salinity, chemicals, cold and hot temperatures, and various pathogen attacks have interconnected effects on plants, resulting in the disruption of protein homeostasis. Maintenance of proteins in their functional native conformations and preventing aggregation of non-native proteins are important for cell survival under stress. Heat shock proteins (HSPs) functioning as molecular chaperones are the key components responsible for protein folding, assembly, translocation, and degradation under stress conditions and in many normal cellular processes. Plants respond to pathogen invasion using two different innate immune responses mediated by pattern recognition receptors (PRRs) or resistance (R) proteins. HSPs play an indispensable role as molecular chaperones in the quality control of plasma membrane-resident PRRs and intracellular R proteins against potential invaders. Here, we specifically discuss the functional involvement of cytosolic and endoplasmic reticulum (ER) HSPs/chaperones in plant immunity to obtain an integrated understanding of the immune responses in plant cells.

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          Most cited references 94

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          Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response.

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            The heat-shock response.

             S Lindquist (1985)
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              Hsp90 as a capacitor of phenotypic variation.

              Heat-shock protein 90 (Hsp90) chaperones the maturation of many regulatory proteins and, in the fruitfly Drosophila melanogaster, buffers genetic variation in morphogenetic pathways. Levels and patterns of genetic variation differ greatly between obligatorily outbreeding species such as fruitflies and self-fertilizing species such as the plant Arabidopsis thaliana. Also, plant development is more plastic, being coupled to environmental cues. Here we report that, in Arabidopsis accessions and recombinant inbred lines, reducing Hsp90 function produces an array of morphological phenotypes, which are dependent on underlying genetic variation. The strength and breadth of Hsp90's effects on the buffering and release of genetic variation suggests it may have an impact on evolutionary processes. We also show that Hsp90 influences morphogenetic responses to environmental cues and buffers normal development from destabilizing effects of stochastic processes. Manipulating Hsp90's buffering capacity offers a tool for harnessing cryptic genetic variation and for elucidating the interplay between genotypes, environments and stochastic events in the determination of phenotype.
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                Author and article information

                Journal
                Plant Pathol J
                Plant Pathol. J
                The Plant Pathology Journal
                Korean Society of Plant Pathology
                1598-2254
                2093-9280
                December 2015
                30 December 2015
                : 31
                : 4
                : 323-333
                Affiliations
                [1 ]Department of Plant Biotechnology and PERI, Sejong University, Seoul 143-747, Korea
                [2 ]Department of Microbiology, Pusan National University, Busan 609-735, Korea
                Author notes
                [* ]Corresponding author. C.-J. Park, Phone) +82-2-3408-4378, FAX) +82-2-3408-4318, E-mail) cjpark@ 123456sejong.ac.kr . Y.-S. Seo, Phone) +82-51-510-2267, FAX) +82-51-514-1778, E-mail:) yseo2011@ 123456pusan.ac.kr , ORCID, Young-Su Seo, http://orcid.org/0000-0001-9191-1405, Chang-Jin Park, http://orcid.org/0000-0002-2586-8856
                Article
                ppj-31-323
                10.5423/PPJ.RW.08.2015.0150
                4677741
                94e68d6a-51ba-4250-831c-85300ac5b0ba
                © The Korean Society of Plant Pathology
                Categories
                Mini-Review

                chaperones, heat shock proteins, plant immunity

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