期刊
G3-GENES GENOMES GENETICS
卷 7, 期 6, 页码 1941-1954出版社
GENETICS SOCIETY AMERICA
DOI: 10.1534/g3.117.042291
关键词
Arabidopsis thaliana; Hsp40; Hsp70; J protein; yeast; evolution
资金
- Indian Ministry of Human Resource Development
- Department of Biotechnology (DBT), Indian Ministry of Science and Technology
- DBT [DBT/PR6885/GBD/27/488/2012]
- Department of Science and Technology [EMR/2015/001213]
- IISER Bhopal
- Lafayette College Chemistry Department
- EXCEL research scholarship program
- National Institute of General Medical Sciences of the National Institutes of Health [R15GM110606]
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.
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