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.
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Chakraborti and colleagues (pp. 1345–1362) report the identification of bacteriophage ƛ NinH as a structural and functional analog of the bacterial nucleoid-associated protein Fis. NinH may influence phage excision-integration reactions or bacterial gene expression by competing with Fis for binding sites. The cover image shows Fis bound to DNA with homology to NinH highlighted. NinH binds and bends DNA with a preference for a 15 bp palindromic motif that is closely related to that recognised by E. coli Fis.
A structure model explaining the binding between a ubiquitous unconventional G-protein (OsYchF1) and a plant-specific C2-domain protein (OsGAP1) from rice
Ming-Yan Cheung, Jacky Chi-Ki Ngo, Zhongzhou Chen, Qi Jia, Tianjie Li, Yitao Gou, Yi Wang, Hon-Ming Lam; A structure model explaining the binding between a ubiquitous unconventional G-protein (OsYchF1) and a plant-specific C2-domain protein (OsGAP1) from rice. Biochem J 30 October 2020; 477 (20): 3935–3949. doi: https://doi.org/10.1042/BCJ20200380
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