Abstract
We used site-directed mutagenesis to engineer two constitutively active forms of the α subunit of a rice heterotrimeric G protein. The recombinant proteins produced from these novel cDNAs had GTP-binding activity but no GTPase activity. A chimeric gene for a constitutively active form of the α subunit was introduced into the rice mutant d1, which is defective for the α-subunit gene. All the transformants essentially showed a wild-type phenotype compared with normal cultivars, although seed sizes were substantially increased and internode lengths also showed some increase. © 2005 JSPP.
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Oki, K., Fujisawa, Y., Kato, H., & Iwasaki, Y. (2005). Study of the constitutively active form of the α subunit of rice heterotrimeric G proteins. Plant and Cell Physiology, 46(2), 381–386. https://doi.org/10.1093/pcp/pci036
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