Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana
| Autor: | Danish Diwan, Justin K. Hines, Rebecca E. Brown, Chandan Sahi, Sandeep Raut, Amit Kumar Verma, Vinita Gowda, Neha Dobriyal |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0106 biological sciences
0301 basic medicine Arabidopsis thaliana Computational biology yeast QH426-470 Biology 01 natural sciences Hsp70 Conserved sequence 03 medical and health sciences Heat shock protein evolution Botany Genetics Molecular Biology Genetics (clinical) Cellular compartment Hsp40 Phylogenetic tree J protein 030104 developmental biology Proteostasis Chaperone (protein) biology.protein Neofunctionalization 010606 plant biology & botany |
| Zdroj: | G3: Genes, Genomes, Genetics, Vol 7, Iss 6, Pp 1941-1954 (2017) |
| ISSN: | 2160-1836 |
| DOI: | 10.1534/g3.117.042291 |
| Popis: | Heat shock proteins of 70 kDa (Hsp70s) partner with structurally diverse Hsp40s (J proteins), generating distinct chaperone networks in various cellular compartments that perform myriad housekeeping and stress-associated functions in all organisms. Plants, being sessile, need to constantly maintain their cellular proteostasis in response to external environmental cues. In these situations, the Hsp70:J protein machines may play an important role in fine-tuning cellular protein quality control. Although ubiquitous, the functional specificity and complexity of the plant Hsp70:J protein network has not been studied. Here, we analyzed the J protein network in the cytosol of Arabidopsis thaliana and, using yeast genetics, show that the functional specificities of most plant J proteins in fundamental chaperone functions are conserved across long evolutionary timescales. Detailed phylogenetic and functional analysis revealed that increased number, regulatory differences, and neofunctionalization in J proteins together contribute to the emerging functional diversity and complexity in the Hsp70:J protein network in higher plants. Based on the data presented, we propose that higher plants have orchestrated their “chaperome,” especially their J protein complement, according to their specialized cellular and physiological stipulations. |
| Databáze: | OpenAIRE |
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