- Information
- Symbol: OsYchF1
- MSU: LOC_Os08g09940
- RAPdb: Os08g0199300
- Publication
- An ancient P-loop GTPase in rice is regulated by a higher plant-specific regulatory protein, 2010, J Biol Chem.
- ATP binding by the P-loop NTPase OsYchF1 an unconventional G protein contributes to biotic but not abiotic stress responses., 2016, Proc Natl Acad Sci U S A.
- Genbank accession number
- Key message
- The finding that OsYchF1 and OsGAP1 are involved in plant defense response might shed light on the functional roles of YchF homologues in plants
- Mutation of the noncanonical G4 motif of the OsYchF1 to the canonical sequence for GTP specificity precludes the binding/hydrolysis of ATP and prevents OsYchF1 from functioning as a negative regulator of plant-defense responses, while retaining its ability to bind/hydrolyze GTP and its function as a negative regulator of abiotic stress responses, demonstrating the specific role of ATP-binding/hydrolysis in disease resistance
- ATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein) contributes to biotic but not abiotic stress responses.
- Connection
- OsGAP1, OsYchF1, An ancient P-loop GTPase in rice is regulated by a higher plant-specific regulatory protein, Using the OsYchF1-OsGAP1 pair from rice as the prototype, we provide evidence for the regulation of GTPase/ATPase activities and RNA binding capacity of a plant YchF (OsYchF1) by its regulatory protein (OsGAP1)
- OsGAP1, OsYchF1, An ancient P-loop GTPase in rice is regulated by a higher plant-specific regulatory protein, The effects of OsGAP1 on the subcellular localization/cycling and physiological functions of OsYchF1 are also discussed
- OsGAP1, OsYchF1, An ancient P-loop GTPase in rice is regulated by a higher plant-specific regulatory protein, The finding that OsYchF1 and OsGAP1 are involved in plant defense response might shed light on the functional roles of YchF homologues in plants
- OsGAP1, OsYchF1, Site-Directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 on the Physiological Functions of the Rice GTPase-Activating Protein 1 OsGAP1., Site-Directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 on the Physiological Functions of the Rice GTPase-Activating Protein 1 (OsGAP1).
- OsGAP1, OsYchF1, Site-Directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 on the Physiological Functions of the Rice GTPase-Activating Protein 1 OsGAP1., We have previously reported that a member of this group, OsGAP1, is able to alleviate salt stress and stimulate defense responses, and bind to both phospholipids and an unconventional G-protein, OsYchF1
- OsGAP1, OsYchF1, Site-Directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 on the Physiological Functions of the Rice GTPase-Activating Protein 1 OsGAP1., On the other hand, the ability to alleviate salt stress by OsGAP1 is dependent only on its ability to bind OsYchF1 and is independent of its phospholipid-binding activity
- OsFKBP12, OsYchF1, A Rice Immunophilin Homolog, OsFKBP12, Is a Negative Regulator of Both Biotic and Abiotic Stress Responses, Using yeast two-hybrid tests, an ancient unconventional G-protein, OsYchF1, was identified as an interacting partner of OsFKBP12
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