Journal
FUNCTIONAL & INTEGRATIVE GENOMICS
Volume 9, Issue 4, Pages 433-446Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s10142-009-0132-0
Keywords
Arabidopsis thaliana; Heat shock protein; Hsp70; J-protein; ATPase activity
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Funding
- Indian Institute of Science, Bangalore
- Wellcome Trust [WT081643MA]
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Plants are sessile organisms that have evolved a variety of mechanisms to maintain their cellular homeostasis under stressful environmental conditions. Survival of plants under abiotic stress conditions requires specialized group of heat shock protein machinery, belonging to Hsp70:J-protein family. These heat shock proteins are most ubiquitous types of chaperone machineries involved in diverse cellular processes including protein folding, translocation across cell membranes, and protein degradation. They play a crucial role in maintaining the protein homeostasis by reestablishing functional native conformations under environmental stress conditions, thus providing protection to the cell. J-proteins are co-chaperones of Hsp70 machine, which play a critical role by stimulating Hsp70s ATPase activity, thereby stabilizing its interaction with client proteins. Using genome-wide analysis of Arabidopsis thaliana, here we have outlined identification and systematic classification of J-protein co-chaperones which are key regulators of Hsp70s function. In comparison with Saccharomyces cerevisiae model system, a comprehensive domain structural organization, cellular localization, and functional diversity of A. thaliana J-proteins have also been summarized.
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