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

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 H

SUBMITTER: Guihur A 

PROVIDER: S-EPMC8359368 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature