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. 2019 Jun 5;10:750. doi: 10.3389/fpls.2019.00750

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Copyright © 2019 Chi, Koo, Oh, Lee, Park, Phan, Wi, Bae, Paeng, Chae, Kang, Kim, Kim, Yun and Lee.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Identified functions of Arabidopsis USPs in response to temperature stresses. Arabidopsis USP, AtUSP, functions as a protein chaperone and an RNA chaperone under high- and low-temperature conditions, respectively. (Left panel) The protein chaperone function of AtUSP protects crucial intracellular substrates from heat shock-mediated aggregation working at the plant cytoplasm. During the process, protein structure of AtUSP changes from a small molecular species to oligomeric complexes in response to heat shock. The structural change enables the protein to get the protein chaperone function. (Right panel) AtUSP acts as an RNA chaperone under cold stress condition working at the plant nucleus. AtUSP can restore the cold-mediated unfolded or over-stabilized non-functional RNAs to their native forms of functional RNAs to serve them for protein translation.