| Autor: |
Amit K. Verma, Danish Diwan, Sandeep Raut, Neha Dobriyal, Rebecca E. Brown, Vinita Gowda, Justin K. Hines, Chandan Sahi |
| Jazyk: |
angličtina |
| Rok vydání: |
2017 |
| Předmět: |
|
| Zdroj: |
G3: Genes, Genomes, Genetics, Vol 7, Iss 6, Pp 1941-1954 (2017) |
| Druh dokumentu: |
article |
| 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: |
Directory of Open Access Journals |
| Externí odkaz: |
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