Characterization of the putative alpha subunit of a heterotrimeric G protein in rice.
作者： Yukimoto Iwasaki , Teruhisa Kato , Toshio Kaidoh , Atsushi Ishikawa , Tadashi Asahi
关键词: Mastoparan 、 Heterotrimeric G protein 、 Biochemistry 、 GTPase-activating protein 、 Protein G 、 Gs alpha subunit 、 Molecular biology 、 Gi alpha subunit 、 G alpha subunit 、 Biology 、 Cholera toxin
摘要: A recombinant protein with a cDNA that encodes the putative alpha subunit of rice heterotrimeric G was synthesized in Escherichia coli and purified. The (rGrice alpha) an apparent molecular mass 45 kDa bound guanosine 5'-(3-O-thio)triphosphate association constant (kapp) 0.36. also hydrolyzed GTP its kcat 0.44. rGrice ADP-ribosylated by activated cholera toxin. Monoclonal antibodies raised against reacted polypeptide localized plasma membrane seedlings. peptide map this after digestion V8 protease identical to alpha. membrane, as well alpha, GTPase activity stimulated 2.5-fold mastoparan 7 but not 17. These properties were similar those subunits proteins animals, suggesting is truly itself.
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