Cryo-EM Structure of OSCA1.2 from Oryza sativa: Mechanical basis of hyperosmolality-gating in Plants

Maity, K.; Heumann, J.; McGrath, A. P.; Kopcho, N. J.; Hsu, P.-K.; Lee, C.-W.; Mapes, J. H.; Garza, D.; Krishnan, S.; Morgan, G. P.; Medrano-Soto, A.; Hendargo, K. J.; Klose, T.; Rees, S. D.; Saier, M. H.; Pineros, M.; Komives, E. A.; Schroeder, J. I.; Chang, G.; Stowell, M. H. B.

doi:10.1101/505453

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bioRxiv · 10.1101/505453

Cryo-EM Structure of OSCA1.2 from Oryza sativa: Mechanical basis of hyperosmolality-gating in Plants

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Abstract

Sensing and responding to environmental water deficiency and osmotic stresses is essential for the growth, development and survival of plants. Recently, an osmolality-sensing ion channel called OSCA1 was discovered that functions in sensing hyperosmolality in Arabidopsis. Here, we report the cryo-EM structure and function of an ion channel from rice (Oryza sativa; OsOSCA1.2), showing how it mediates hyperosmolality sensing and ion permeability. The structure reveals a dimer; the molecular architecture of each subunit consists of eleven transmembrane helices and a cytosolic soluble domain that has homology to RNA recognition proteins. The transmembrane domain is structurally related to the TMEM16 family of calcium dependent ion channels and scramblases. The cytosolic soluble domain possesses a distinct structural feature in the form of extended intracellular helical arms that is parallel to the plasma membrane. These helical arms are well positioned to sense lateral tension on the inner leaflet of the lipid bilayer caused by changes in turgor pressure. Computational dynamic analysis suggests how this domain couples to the transmembrane portion of the molecule to open the channel. Hydrogen-deuterium exchange mass spectrometry (HDXMS) experimentally confirms the conformational dynamics of these coupled domains. The structure provides a framework to understand the structural basis of hyperosmolality sensing in an important crop plant, extends our knowledge of the anoctamin superfamily important for plants and fungi, and provides a structural mechanism for translating membrane stress to ion transport regulation.

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Maity, K., Heumann, J., McGrath, A. P., Kopcho, N. J., Hsu, P.-K., Lee, C.-W., Mapes, J. H., Garza, D., Krishnan, S., Morgan, G. P., Medrano-Soto, A., Hendargo, K. J., Klose, T., Rees, S. D., Saier, M. H., Pineros, M., Komives, E. A., Schroeder, J. I., Chang, G., Stowell, M. H. B.. 2018-12-30. Cryo-EM Structure of OSCA1.2 from Oryza sativa: Mechanical basis of hyperosmolality-gating in Plants. https://doi.org/10.1101/505453

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