title: The HAB1 PP2C is inhibited by ABA-dependent PYL10 interaction.
abstract: PYL10 is a monomeric abscisic acid (ABA) receptor that inhibits protein phosphatase 2C (PP2C) activity in Arabidopsis thaliana. Previous studies reported that the PP2C phosphatase inhibition by PYL10 was ABA-independent. Here, systematic PYL10 biochemical studies demonstrated that PYL10 activity was ABA-dependent, and the previously reported studies was interfered by the presence of BSA in the commercial kit. To investigate dynamic mechanism of how ABA binding to PYL10 induces PP2C phosphatase inhibiting activity, solution NMR relaxation analysis of apo-PYL10 and PYL10/ABA were conducted following backbone resonance assignments. Reduced spectrum density mapping of the backbone relaxation data revealed that PYL10 was more flexible in ABA bound form than apo-PYL10, indicating an increased conformational entropy upon ligand binding. Moreover, to illustrate conformation exchanges of PYL10 upon ABA binding, NMR line shape analysis was performed with increasing concentrations of ABA, and the results indicated that PYL10 backbone conformational changes occur at different time scales.
authors.affiliation: Hefei 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.
authors.forename: Juan
authors.initials: J
authors.lastname: Li
authors.affiliation: Hefei 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.
authors.forename: Chaowei
authors.initials: C
authors.lastname: Shi
authors.affiliation: Hefei 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.
authors.forename: Demeng
authors.initials: D
authors.lastname: Sun
authors.affiliation: Hefei 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.
authors.forename: Yao
authors.initials: Y
authors.lastname: He
authors.affiliation: Hefei 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.
authors.forename: Chaohua
authors.initials: C
authors.lastname: Lai
authors.affiliation: Hefei 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.
authors.forename: Pei
authors.initials: P
authors.lastname: Lv
authors.affiliation: Hefei 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.
authors.forename: Ying
authors.initials: Y
authors.lastname: Xiong
authors.affiliation: Hefei 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.
authors.forename: Longhua
authors.initials: L
authors.lastname: Zhang
authors.affiliation: High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, P.R. China.
authors.forename: Fangming
authors.initials: F
authors.lastname: Wu
authors.affiliation: 1] Hefei 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 [2] High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui 230031, P.R. China.
authors.forename: Changlin
authors.initials: C
authors.lastname: Tian
mesh_terms: D000040:Abscisic Acid / Q000737:chemistry / Q000494:pharmacology*; D017360:Arabidopsis / Q000187:drug effects / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D000071636:Protein Phosphatase 2C; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; C560427:PYL10 protein, Arabidopsis; D011956:Receptors, Cell Surface; D000040:Abscisic Acid; D010749:Phosphoprotein Phosphatases; D000071636:Protein Phosphatase 2C