Rice dwarf mutant d1 , which is defective in the α subunit of the heterotrimeric G protein, affects gibberellin signal transduction

糊粉 异三聚体G蛋白 突变体 生物 赤霉素 信号转导 蛋白质亚单位 细胞生物学 野生型 G蛋白 生物化学 遗传学 基因
作者
Miyako Ueguchi‐Tanaka,Yukiko Fujisawa,Masatomo Kobayashi,Motoyuki Ashikari,Yukimoto Iwasaki,Hidemi Kitano,Makoto Matsuoka
出处
期刊:Proceedings of the National Academy of Sciences of the United States of America [Proceedings of the National Academy of Sciences]
卷期号:97 (21): 11638-11643 被引量:384
标识
DOI:10.1073/pnas.97.21.11638
摘要

Previously, we reported that the rice dwarf mutant, d1 , is defective in the α subunit of the heterotrimeric G protein (Gα). In the present study, gibberellin (GA) signaling in d1 and the role of the Gα protein in the GA-signaling pathway were investigated. Compared with the wild type, GA induction of α-amylase activity in aleurone cells of d1 was greatly reduced. Relative to the wild type, the GA 3 -treated aleurone layer of d1 had lower expression of Ramy1A , which encodes α-amylase, and OsGAMYB , which encodes a GA-inducible transcriptional factor, and no increase in expression of Ca 2 + -ATPase . However, in the presence of high GA concentrations, α-amylase induction occurred even in d1 . The GA sensitivity of second leaf sheath elongation in d1 was similar to that of the wild type in terms of dose responsiveness, but the response of internode elongation to GA was much lower in d1 . Furthermore, Os20ox expression was up-regulated, and the GA content was elevated in the stunted internodes of d1 . All these results suggest that d1 affects a part of the GA-signaling pathway, namely the induction of α-amylase in the aleurone layer and internode elongation. In addition, a double mutant between d1 and another GA-signaling mutant, slr , revealed that SLR is epistatic to the D1 , supporting that the Gα protein is involved in GA signaling. However, the data also provide evidence for the presence of an alternative GA-signaling pathway that does not involve the Gα protein. It is proposed that GA signaling via the Gα protein may be more sensitive than that of the alternative pathway, as indicated by the low GA responsiveness of this Gα-independent pathway.
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