Study of the constitutively active form of the alpha subunit of rice heterotrimeric G proteins.
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.
Oki
Katsuyuki
K
Fukui Prefectural University, Faculty of Bioscience, Kenjyojima, Matsuoka-cho, Yoshida-gun, Fukui, 910-1195 Japan.
Fujisawa
Yukiko
Y
Kato
Hisaharu
H
Iwasaki
Yukimoto
Y
D000595:Amino Acid Sequence; D044385:GTP-Binding Protein alpha Subunits / Q000235:genetics* / Q000378:metabolism*; D018506:Gene Expression Regulation, Plant; D008969:Molecular Sequence Data; D012275:Oryza / Q000235:genetics* / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
D044385:GTP-Binding Protein alpha Subunits; D011993:Recombinant Fusion Proteins