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The HAB1 PP2C is inhibited by ABA-dependent PYL10 interaction
Juan Li1, Chaowei Shi1, Demeng Sun1
1Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, P.R. China.
Scientific Reports
|June 6, 2015
Summary
PYL10
Area of Science:
- Plant molecular biology
- Biochemistry
- Structural biology
Background:
- PYL10 is a monomeric abscisic acid (ABA) receptor in Arabidopsis thaliana.
- Previous research suggested ABA-independent PP2C phosphatase inhibition by PYL10.
- This ABA-independent activity was potentially due to experimental interference.
Purpose of the Study:
- To clarify the ABA dependency of PYL10's PP2C phosphatase inhibitory activity.
- To investigate the dynamic mechanism of ABA binding to PYL10 and its effect on PP2C inhibition.
- To elucidate the conformational changes in PYL10 upon ABA binding.
Main Methods:
- Systematic biochemical assays to determine PYL10 activity.
- Solution Nuclear Magnetic Resonance (NMR) relaxation analysis of apo-PYL10 and PYL10/ABA complex.
- Backbone resonance assignments and reduced spectral density mapping.
- NMR line shape analysis at varying ABA concentrations.
Main Results:
- PYL10's PP2C phosphatase inhibitory activity is ABA-dependent, correcting previous findings.
- BSA contamination in commercial kits interfered with prior ABA-independent observations.
- PYL10 exhibits increased flexibility and conformational entropy upon ABA binding.
- Conformational changes in PYL10 occur across different timescales upon ABA interaction.
Conclusions:
- PYL10 functions as an ABA-dependent receptor.
- ABA binding induces dynamic conformational changes in PYL10, impacting its PP2C inhibitory function.
- Understanding these dynamics provides insight into plant hormone signaling pathways.
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