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We used site-directed mutagenesis to engineer two constitutively active forms of the alpha 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 alpha subunit was introduced into the rice mutant d1, which is defective for the alpha-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.

Study of the Constitutively Active Form of the α Subunit of Rice Heterotrimeric G Proteins