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Updated: May 23, 2026

Translation Efficiency Test Using Polysome Profiles Under Heat Stress
Published on: October 11, 2024
Serine/threonine protein phosphatase 5 (PP5) interacts with substrate under heat stress conditions and forms protein
Jin Ho Park1, Woe Yeon Kim, Ho Byoung Chae
1Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju, Korea.
Abstract:
Protein phosphatase 5 plays a pivotal role in signal transduction in animal and plant cells, and it was previously shown that Arabidopsis protein phosphatase 5 (AtPP5) performs multiple enzymatic activities that are mediated by conformational changes induced by heat shock stress. In addition, transgenic overexpression of AtPP5 gene conferred enhanced heat shock resistance compared with wild-type plant. However, the molecular mechanism underlying this enhanced heat shock tolerance through functional and conformational changes upon heat stress is not clear. In this report, AtPP5 was shown to preferentially interact with its substrate, MDH, under heat stress conditions. In addition, in co-IP analysis, AtPP5 was observed to form a complex with AtHsp90 in Arabidopsis. These results suggest that AtPP5 may enhance thermotolerance via forming multi-chaperone complexes under heat shock conditions in Arabidopsis. Finally, we show that AtPP5 is primarily localized in the cytoplasm of Arabidopsis.
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