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      Proteomic analysis of gametophytic sex expression in the fern Ceratopteris thalictroides

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          Abstract

          Ceratopteris thalictroides, a model fern, has two kinds of gametophytes with different sex expression: male and hermaphrodite. Hermaphroditic gametophytes have one or several archegonia beneath the growing point and a few antheridia at the base or margin. Male gametophytes show a spoon-like shape with much longer than the width and produce many antheridia at the margin and surface. The results of chlorophyll fluorescence detection showed that the photochemical efficiency of hermaphrodites was higher than that of males. By using two-dimensional electrophoresis and mass spectrometry, the differentially abundant proteins in hermaphroditic and male gametophytes were identified. A total of 1136 ± 55 protein spots were detected in Coomassie-stained gels of proteins from hermaphroditic gametophytes, and 1130 ± 65 spots were detected in gels of proteins from male gametophytes. After annotation, 33 spots representing differentially abundant proteins were identified. Among these, proteins involved in photosynthesis and chaperone proteins were over-represented in hermaphrodites, whereas several proteins involved in metabolism were increased in male gametophytes in order to maintain their development under relatively nutritionally deficient conditions. Furthermore, the differentially abundant cytoskeletal proteins detected in this study, such as centrin and actin, may be involved in the formation of sexual organs and are directly related to sex expression. These differentially abundant proteins are important for maintaining the development of gametophytes of different sexes in C. thalictroides.

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

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            Transcriptional profiling of Arabidopsis heat shock proteins and transcription factors reveals extensive overlap between heat and non-heat stress response pathways

            Background The heat shock response of Arabidopsis thaliana is dependent upon a complex regulatory network involving twenty-one known transcription factors and four heat shock protein families. It is known that heat shock proteins (Hsps) and transcription factors (Hsfs) are involved in cellular response to various forms of stress besides heat. However, the role of Hsps and Hsfs under cold and non-thermal stress conditions is not well understood, and it is unclear which types of stress interact least and most strongly with Hsp and Hsf response pathways. To address this issue, we have analyzed transcriptional response profiles of Arabidopsis Hsfs and Hsps to a range of abiotic and biotic stress treatments (heat, cold, osmotic stress, salt, drought, genotoxic stress, ultraviolet light, oxidative stress, wounding, and pathogen infection) in both above and below-ground plant tissues. Results All stress treatments interact with Hsf and Hsp response pathways to varying extents, suggesting considerable cross-talk between heat and non-heat stress regulatory networks. In general, Hsf and Hsp expression was strongly induced by heat, cold, salt, and osmotic stress, while other types of stress exhibited family or tissue-specific response patterns. With respect to the Hsp20 protein family, for instance, large expression responses occurred under all types of stress, with striking similarity among expression response profiles. Several genes belonging to the Hsp20, Hsp70 and Hsp100 families were specifically upregulated twelve hours after wounding in root tissue, and exhibited a parallel expression response pattern during recovery from heat stress. Among all Hsf and Hsp families, large expression responses occurred under ultraviolet-B light stress in aerial tissue (shoots) but not subterranean tissue (roots). Conclusion Our findings show that Hsf and Hsp family member genes represent an interaction point between multiple stress response pathways, and therefore warrant functional analysis under conditions apart from heat shock treatment. In addition, our analysis revealed several family and tissue-specific heat shock gene expression patterns that have not been previously described. These results have implications regarding the molecular basis of cross-tolerance in plant species, and raise new questions to be pursued in future experimental studies of the Arabidopsis heat shock response network.
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              Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity

              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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                Author and article information

                Contributors
                Role: Data curationRole: Formal analysisRole: InvestigationRole: Writing – original draft
                Role: Formal analysisRole: InvestigationRole: Writing – original draft
                Role: Data curationRole: InvestigationRole: Methodology
                Role: Investigation
                Role: Resources
                Role: ConceptualizationRole: Writing – review & editing
                Role: ConceptualizationRole: Funding acquisitionRole: MethodologyRole: Project administrationRole: ResourcesRole: Writing – review & editing
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, CA USA )
                1932-6203
                19 August 2019
                2019
                : 14
                : 8
                : e0221470
                Affiliations
                [1 ] College of Life Science, East China Normal University, Shanghai, China
                [2 ] College of Life Science, Shanghai Normal University, Shanghai, China
                Northeast Forestry University, CHINA
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Author information
                http://orcid.org/0000-0001-5732-1903
                Article
                PONE-D-19-19650
                10.1371/journal.pone.0221470
                6699692
                31425560
                b1cb4a46-16d1-4d69-b728-847c8b2246ab
                © 2019 Chen et al

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                : 12 July 2019
                : 8 August 2019
                Page count
                Figures: 4, Tables: 1, Pages: 14
                Funding
                Funded by: funder-id http://dx.doi.org/10.13039/100007219, Natural Science Foundation of Shanghai;
                Award ID: 13ZR1429700
                Award Recipient :
                Funded by: Science and Engineering Research Project of Shanghai Normal University
                Award ID: DYL201702
                Award Recipient :
                This research was supported by the Natural Science Foundation of Shanghai (13ZR1429700,J.C), and the Science and Engineering Research Project of Shanghai Normal University (DYL201702, J.C). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Research Article
                Biology and Life Sciences
                Biochemistry
                Plant Biochemistry
                Photosynthesis
                Biology and Life Sciences
                Plant Science
                Plant Biochemistry
                Photosynthesis
                Biology and Life Sciences
                Biochemistry
                Plant Biochemistry
                Photosynthesis
                Ribulose-1,5-Bisphosphate Carboxylase Oxygenase
                Biology and Life Sciences
                Plant Science
                Plant Biochemistry
                Photosynthesis
                Ribulose-1,5-Bisphosphate Carboxylase Oxygenase
                Biology and Life Sciences
                Biochemistry
                Proteins
                Cytoskeletal Proteins
                Physical Sciences
                Chemistry
                Physical Chemistry
                Photochemistry
                Biology and Life Sciences
                Biochemistry
                Proteins
                Contractile Proteins
                Actins
                Biology and Life Sciences
                Biochemistry
                Proteins
                Cytoskeletal Proteins
                Actins
                Biology and Life Sciences
                Organisms
                Eukaryota
                Plants
                Ferns
                Biology and Life Sciences
                Cell Biology
                Cellular Structures and Organelles
                Chloroplasts
                Chlorophyll
                Biology and Life Sciences
                Cell Biology
                Plant Cell Biology
                Chloroplasts
                Chlorophyll
                Biology and Life Sciences
                Plant Science
                Plant Cell Biology
                Chloroplasts
                Chlorophyll
                Biology and Life Sciences
                Cell Biology
                Cellular Types
                Plant Cells
                Chloroplasts
                Chlorophyll
                Biology and Life Sciences
                Cell Biology
                Plant Cell Biology
                Plant Cells
                Chloroplasts
                Chlorophyll
                Biology and Life Sciences
                Plant Science
                Plant Cell Biology
                Plant Cells
                Chloroplasts
                Chlorophyll
                Physical Sciences
                Materials Science
                Materials
                Pigments
                Organic Pigments
                Chlorophyll
                Biology and Life Sciences
                Developmental Biology
                Morphogenesis
                Sexual Differentiation
                Custom metadata
                All relevant data are within the manuscript and its Supporting Information files.

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