CO2 response screen in grass Brachypodium reveals the key role of a MAP kinase in CO2-triggered stomatal closure.

Autor:	Lopez BNK; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Ceciliato PHO; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Takahashi Y; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA.; Institute of Transformative Bio-Molecules (ITbM), Nagoya University, Nagoya, Aichi 464-0813, Japan., Rangel FJ; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Salem EA; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Kernig K; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Chow K; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Zhang L; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Sidhom MA; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Seitz CG; Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093, USA., Zheng T; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA., Sibout R; Biopolymères Interactions Assemblages, Equipe Paroi Végétale et Polymères Pariétaux (PVPP), Impasse Y. Cauchois/Site de la Géraudière BP71627, Nantes 44316 cedex 03, France., Laudencia-Chingcuanco DL; Crop Improvement and Genetics Research, USDA, ARS, PWA, WRRC-CIG, Albany, CA 94710, USA., Woods DP; Department of Plant Sciences, University of California, Davis, CA 95616, USA., McCammon JA; Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093, USA., Vogel JP; U.S. Department of Energy Joint Genome Institute, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Schroeder JI; School of Biological Sciences, Cell and Developmental Biology Department, University of California San Diego, La Jolla, CA 92093-0116, USA.
Jazyk:	angličtina
Zdroj:	Plant physiology [Plant Physiol] 2024 Sep 02; Vol. 196 (1), pp. 495-510.
DOI:	10.1093/plphys/kiae262
Abstrakt:	Plants respond to increased CO2 concentrations through stomatal closure, which can contribute to increased water use efficiency. Grasses display faster stomatal responses than eudicots due to dumbbell-shaped guard cells flanked by subsidiary cells working in opposition. However, forward genetic screening for stomatal CO2 signal transduction mutants in grasses has yet to be reported. The grass model Brachypodium distachyon is closely related to agronomically important cereal crops, sharing largely collinear genomes. To gain insights into CO2 control mechanisms of stomatal movements in grasses, we developed an unbiased forward genetic screen with an EMS-mutagenized B. distachyon M5 generation population using infrared imaging to identify plants with altered leaf temperatures at elevated CO2. Among isolated mutants, a "chill1" mutant exhibited cooler leaf temperatures than wild-type Bd21-3 parent control plants after exposure to increased CO2. chill1 plants showed strongly impaired high CO2-induced stomatal closure despite retaining a robust abscisic acid-induced stomatal closing response. Through bulked segregant whole-genome sequencing analyses followed by analyses of further backcrossed F4 generation plants and generation and characterization of sodium azide and CRISPR-cas9 mutants, chill1 was mapped to a protein kinase, Mitogen-Activated Protein Kinase 5 (BdMPK5). The chill1 mutation impaired BdMPK5 protein-mediated CO2/HCO3- sensing together with the High Temperature 1 (HT1) Raf-like kinase in vitro. Furthermore, AlphaFold2-directed structural modeling predicted that the identified BdMPK5-D90N chill1 mutant residue is located at the interface of BdMPK5 with the BdHT1 Raf-like kinase. BdMPK5 is a key signaling component that mediates CO2-induced stomatal movements and is proposed to function as a component of the primary CO2 sensor in grasses. Competing Interests: Conflict of interest statement. None declared. (© The Author(s) 2024. Published by Oxford University Press on behalf of American Society of Plant Biologists. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.)
Databáze:	MEDLINE
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