A structure model explaining the binding between a ubiquitous unconventional G-protein (OsYchF1) and a plant-specific C2-domain protein (OsGAP1) from rice.

Autor:	Cheung MY; School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR., Ngo JC; School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR., Chen Z; State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China., Jia Q; School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.; Key Laboratory for Genetics Breeding and Multiple Utilization of Crops, Ministry of Education/College of Agriculture, Fujian Agriculture and Forestry University, Fuzhou 350002, China., Li T; Department of Physics, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR., Gou Y; Department of Physics, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR., Wang Y; Department of Physics, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR., Lam HM; School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.; Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR.
Jazyk:	angličtina
Zdroj:	The Biochemical journal [Biochem J] 2020 Oct 30; Vol. 477 (20), pp. 3935-3949.
DOI:	10.1042/BCJ20200380
Abstrakt:	The unconventional G-protein OsYchF1 plays regulatory roles in plant defense and abiotic stress responses. We have previously resolved the crystal structures of OsYchF1 and its plant-specific regulator, OsGAP1, and determined the residues on OsGAP1 that are essential for its binding to OsYchF1. In this study, we employed site-directed mutagenesis to identify four critical residues on the TGS domain of OsYchF1 that are critical for its binding to OsGAP1. We also generated a docking model of the OsYchF1 : OsGAP1 complex to dissect the molecular basis of their interactions. Our finding not only reveals the roles of the key interacting residues controlling the binding between OsYchF1 and OsGAP1, but also provides a working model on the potential regulatory mechanism mediated by a TGS domain, particularly in the class of GTPase of the OBG family. (© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.)
Databáze:	MEDLINE
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