Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance.

Details

Serval ID
serval:BIB_4641E70C783E
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance.
Journal
Plant, cell & environment
Author(s)
Guihur A., Fauvet B., Finka A., Quadroni M., Goloubinoff P.
ISSN
1365-3040 (Electronic)
ISSN-L
0140-7791
Publication state
In Press
Peer-reviewed
Oui
Language
english
Notes
Publication types: Journal Article
Publication Status: aheadofprint
Abstract
At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat-labile membranes and proteins functional. A gradual morning pre-exposure to increasing sub-damaging temperatures induces heat-shock proteins (HSPs) that are central to the onset of plant acquired thermotolerance (AT). To gain knowledge on the mechanisms of AT in the model land plant Physcomitrium patens, we used label-free LC-MS/MS proteomics to quantify the accumulated and depleted proteins before and following a mild heat-priming treatment. High protein crowding is thought to promote protein aggregation, whereas molecular chaperones prevent and actively revert aggregation. Yet, we found that heat priming (HP) did not accumulate HSP chaperones in chloroplasts, although protein crowding was six times higher than in the cytosol. In contrast, several HSP20s strongly accumulated in the cytosol, yet contributing merely 4% of the net mass increase of heat-accumulated proteins. This is in poor concordance with their presumed role at preventing the aggregation of heat-labile proteins. The data suggests that under mild HP unlikely to affect protein stability. Accumulating HSP20s leading to AT, regulate the activity of rare and specific signalling proteins, thereby preventing cell death under noxious heat stress.
Keywords
Plant Science, Physiology, HSP20s-heat-shock proteins, Physcomitrium patens, RNA-Seq, heat-priming, heat-shock proteins, heat-shock response, molecular crowding, proteomics, thermotolerance
Pubmed
Web of science
Open Access
Yes
Funding(s)
University of Lausanne
Create date
22/12/2020 10:29
Last modification date
14/01/2021 7:22
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