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HISTONE DEACETYLASE 9 stimulates auxin-dependent thermomorphogenesis in Arabidopsis thaliana by mediating H2A.Z depletion

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    0520740 - ÚEB 2020 RIV US eng J - Journal Article
    van der Woude, A. - Perrella, C. - Snoek, L. B. - Van Hoogdalem, M. - Novák, Ondřej - Van Verk, M. C. - Van Kooten, H. N. - Zorn, L. E. - Tonckens, R. - Dongus, J. A. - Praat, M. - Stouten, E. A. - Proveniers, M. C.G. - Vellutini, E. - Patitaki, E. - Shapulatov, U. - Kohlen, W. - Balasubramanian, S. - Ljung, K. - van der Krol, A. R. - Smeekens, S. - Kaiserli, E. - van Zanten, M.
    HISTONE DEACETYLASE 9 stimulates auxin-dependent thermomorphogenesis in Arabidopsis thaliana by mediating H2A.Z depletion.
    Proceedings of the National Academy of Sciences of the United States of America. Roč. 116, č. 50 (2019), s. 25343-25354. ISSN 0027-8424. E-ISSN 1091-6490
    R&D Projects: GA MŠMT(CZ) EF16_019/0000827
    Institutional support: RVO:61389030
    Keywords : Arabidopsis * h2a.z * hda9 * Shade avoidance * Thermomorphogenesis
    OECD category: Biochemistry and molecular biology
    Impact factor: 9.412, year: 2019
    Method of publishing: Open access
    http://dx.doi.org/10.1073/pnas.1911694116

    Many plant species respond to unfavorable high ambient temperatures by adjusting their vegetative body plan to facilitate cooling. This process is known as thermomorphogenesis and is induced by the phytohormone auxin. Here, we demonstrate that the chromatinmodifying enzyme HISTONE DEACETYLASE 9 (HDA9) mediates thermomorphogenesis but does not interfere with hypocotyl elongation during shade avoidance. HDA9 is stabilized in response to high temperature and mediates histone deacetylation at the YUCCA8 locus, a rate-limiting enzyme in auxin biosynthesis, at warm temperatures. We show that HDA9 permits net eviction of the H2A.Z histone variant from nucleosomes associated with YUCCA8, allowing binding and transcriptional activation by PHYTOCHROME INTERACTING FACTOR 4, followed by auxin accumulation and thermomorphogenesis.
    Permanent Link: http://hdl.handle.net/11104/0305410

     
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