TOC1 clock protein phosphorylation controls complex formation with NF-YB/C to repress hypocotyl growth.

Autor: Yan J; Molecular Genetics, Ohio State University, Columbus, OH, USA., Li S; Molecular Genetics, Ohio State University, Columbus, OH, USA.; Memorial Sloan Kettering Cancer Center, Molecular Biology Program, New York, NY, USA., Kim YJ; Molecular Genetics, Ohio State University, Columbus, OH, USA., Zeng Q; Molecular Genetics, Ohio State University, Columbus, OH, USA., Radziejwoski A; POSTECH, Division of Integrative Biosciences and Biotechnology, Pohang, South Korea., Wang L; Molecular Genetics, Ohio State University, Columbus, OH, USA.; The Chinese Academy of Sciences, Institute of Botany, Beijing, China., Nomura Y; RIKEN Center for Sustainable Resource Science (CSRS), Plant Proteomics Research Unit, Yokohama, Japan., Nakagami H; RIKEN Center for Sustainable Resource Science (CSRS), Plant Proteomics Research Unit, Yokohama, Japan.; Max Planck Institute for Plant Breeding Research, Protein Mass Spectrometry, Cologne, Germany., Somers DE; Molecular Genetics, Ohio State University, Columbus, OH, USA.; POSTECH, Division of Integrative Biosciences and Biotechnology, Pohang, South Korea.
Jazyk: angličtina
Zdroj: The EMBO journal [EMBO J] 2021 Dec 15; Vol. 40 (24), pp. e108684. Date of Electronic Publication: 2021 Nov 02.
DOI: 10.15252/embj.2021108684
Abstrakt: Plant photoperiodic growth is coordinated by interactions between circadian clock and light signaling networks. How post-translational modifications of clock proteins affect these interactions to mediate rhythmic growth remains unclear. Here, we identify five phosphorylation sites in the Arabidopsis core clock protein TIMING OF CAB EXPRESSION 1 (TOC1) which when mutated to alanine eliminate detectable phosphorylation. The TOC1 phospho-mutant fails to fully rescue the clock, growth, and flowering phenotypes of the toc1 mutant. Further, the TOC1 phospho-mutant shows advanced phase, a faster degradation rate, reduced interactions with PHYTOCHROME-INTERACTING FACTOR 3 (PIF3) and HISTONE DEACETYLASE 15 (HDA15), and poor binding at pre-dawn hypocotyl growth-related genes (PHGs), leading to a net de-repression of hypocotyl growth. NUCLEAR FACTOR Y subunits B and C (NF-YB/C) stabilize TOC1 at target promoters, and this novel trimeric complex (NF-TOC1) acts as a transcriptional co-repressor with HDA15 to inhibit PIF-mediated hypocotyl elongation. Collectively, we identify a molecular mechanism suggesting how phosphorylation of TOC1 alters its phase, stability, and physical interactions with co-regulators to precisely phase PHG expression to control photoperiodic hypocotyl growth.
(© 2021 The Authors.)
Databáze: MEDLINE
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