Identification of SLAC1 anion channel residues required for CO 2 /bicarbonate sensing and regulation of stomatal movements
| Autor: | J. Andrew McCammon, Jingbo Zhang, Julian I. Schroeder, Felix Hauser, Nuo Wang, Yinglong Miao, Wouter-Jan Rappel |
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| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
0301 basic medicine Multidisciplinary biology Bicarbonate Xenopus Anion channel activity biology.organism_classification 01 natural sciences 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Guard cell Biophysics Patch clamp Abscisic acid Intracellular Ion channel 010606 plant biology & botany |
| Zdroj: | Proceedings of the National Academy of Sciences. 115:11129-11137 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1807624115 |
| Popis: | Increases in CO2 concentration in plant leaves due to respiration in the dark and the continuing atmospheric [CO2] rise cause closing of stomatal pores, thus affecting plant–water relations globally. However, the underlying CO2/bicarbonate (CO2/HCO3−) sensing mechanisms remain unknown. [CO2] elevation in leaves triggers stomatal closure by anion efflux mediated via the SLAC1 anion channel localized in the plasma membrane of guard cells. Previous reconstitution analysis has suggested that intracellular bicarbonate ions might directly up-regulate SLAC1 channel activity. However, whether such a CO2/HCO3− regulation of SLAC1 is relevant for CO2 control of stomatal movements in planta remains unknown. Here, we computationally probe for candidate bicarbonate-interacting sites within the SLAC1 anion channel via long-timescale Gaussian accelerated molecular dynamics (GaMD) simulations. Mutations of two putative bicarbonate-interacting residues, R256 and R321, impaired the enhancement of the SLAC1 anion channel activity by CO2/HCO3− in Xenopus oocytes. Mutations of the neighboring charged amino acid K255 and residue R432 and the predicted gate residue F450 did not affect HCO3− regulation of SLAC1. Notably, gas-exchange experiments with slac1-transformed plants expressing mutated SLAC1 proteins revealed that the SLAC1 residue R256 is required for CO2 regulation of stomatal movements in planta, but not for abscisic acid (ABA)-induced stomatal closing. Patch clamp analyses of guard cells show that activation of S-type anion channels by CO2/HCO3−, but not by ABA, was impaired, indicating the relevance of R256 for CO2 signal transduction. Together, these analyses suggest that the SLAC1 anion channel is one of the physiologically relevant CO2/HCO3− sensors in guard cells. |
| Databáze: | OpenAIRE |
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