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Homologue structure of the SLAC1 anion channel for closing stomata in leaves

Author

Listed:
  • Yu-hang Chen

    (Columbia University
    NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA)

  • Lei Hu

    (Columbia University)

  • Marco Punta

    (NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
    Technical University of Munich)

  • Renato Bruni

    (NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA)

  • Brandan Hillerich

    (NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA)

  • Brian Kloss

    (NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA)

  • Burkhard Rost

    (Columbia University
    NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
    Technical University of Munich)

  • James Love

    (NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA)

  • Steven A. Siegelbaum

    (Columbia University
    Columbia University
    Howard Hughes Medical Institute, Columbia University)

  • Wayne A. Hendrickson

    (Columbia University
    NYCOMPS, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027, USA
    Howard Hughes Medical Institute, Columbia University
    Columbia University)

Abstract

The plant SLAC1 anion channel controls turgor pressure in the aperture-defining guard cells of plant stomata, thereby regulating the exchange of water vapour and photosynthetic gases in response to environmental signals such as drought or high levels of carbon dioxide. Here we determine the crystal structure of a bacterial homologue (Haemophilus influenzae) of SLAC1 at 1.20 Å resolution, and use structure-inspired mutagenesis to analyse the conductance properties of SLAC1 channels. SLAC1 is a symmetrical trimer composed from quasi-symmetrical subunits, each having ten transmembrane helices arranged from helical hairpin pairs to form a central five-helix transmembrane pore that is gated by an extremely conserved phenylalanine residue. Conformational features indicate a mechanism for control of gating by kinase activation, and electrostatic features of the pore coupled with electrophysiological characteristics indicate that selectivity among different anions is largely a function of the energetic cost of ion dehydration.

Suggested Citation

  • Yu-hang Chen & Lei Hu & Marco Punta & Renato Bruni & Brandan Hillerich & Brian Kloss & Burkhard Rost & James Love & Steven A. Siegelbaum & Wayne A. Hendrickson, 2010. "Homologue structure of the SLAC1 anion channel for closing stomata in leaves," Nature, Nature, vol. 467(7319), pages 1074-1080, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7319:d:10.1038_nature09487
    DOI: 10.1038/nature09487
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    Cited by:

    1. Yawen Li & Yinan Ding & Lili Qu & Xinru Li & Qinxuan Lai & Pingxia Zhao & Yongxiang Gao & Chengbin Xiang & Chunlei Cang & Xin Liu & Linfeng Sun, 2022. "Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Yeongmok Lee & Hyeon Seong Jeong & Seoyeon Jung & Junmo Hwang & Chi Truc Han Le & Sung-Hoon Jun & Eun Jo Du & KyeongJin Kang & Beom-Gi Kim & Hyun-Ho Lim & Sangho Lee, 2023. "Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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