Gravitropism and Phototropism of Maize Coleoptiles : Evaluation of the Cholodny-Went Theory Through Effects of Auxin Application and Decapitation : GROWTH AND DEVELOPMENT

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We report the isolation of a cDNA for the a subunit of a G protein from rice (Oryza sativa L. cv. Nipponbare). The cDNA contained an open reading frame that encoded a protein of 380 amino acid residues with a mol wt of 44,204. We designated this polypeptide RGAI (rice G pro-tein a subunit 1). The amino acid sequence of RGAI was 77% and 86% identical to the sequences of a subunits from Arabidopsis thaliana and tomato (products of GPA I and TGA1), respective-ly, and 42% to 69% identical to sequences of mammalian a subunits. The regions essential for binding to GTP were preserved throughout all a subunits from higher plants and mammals. How-ever, the C-terminal amino acid sequence, which has been proposed to be a receptor-binding region, of RGAI was different not only from the analogous sequences of mammalian a subunits but also from those of the products of GPA1 and TGA1. The mRNA for RGA1, of 1.7 kb in length, was found in the roots and in the etiolated and greening leaves of rice, suggesting that RGAI might be a protein that is expressed constitutively.
日本植物生理学会の論文