Repressed function of the C terminal domain of GS3 in grain size regulation
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摘要
Grain yield in many cereal crops is largely determined by grain size. Our group previously established that GS3-4 allele showing stronger effect on reducing grain size due to its deficiency of the C terminal cysteine-rich domain,compared with the GS3-1 allele. Here show that the cysteine-rich domain cloud not interact with the N terminal(OSR) domain,excluding the possibility of head–to-tail interaction to block the function of OSR. We detected the protein level of the GS3-1 and GS3-4 transgenic plant which under ubiquitin promoter and fused with Flag tag in the C terminal. As expect,the enhanced phenotype mediated by overexpressing GS3-4 was correlated with the increased protein level but not m RNA level. Accumulation of GS3-1 protein but not GS3-4 protein was detected compared with the untreated control when treated with the proteasome inhibitor MG-132,suggesting that GS3-1 might degrade via C terminal domain through the proteasome-mediated pathway. These findings added to the understanding of the molecular mechanism with respect to GS3 in grain size regulation.
Grain yield in many cereal crops is largely determined by grain size. Our group previously established that GS3-4 allele showing stronger effect on reducing grain size due to its deficiency of the C terminal cysteine-rich domain,compared with the GS3-1 allele. Here show that the cysteine-rich domain cloud not interact with the N terminal(OSR) domain,excluding the possibility of head–to-tail interaction to block the function of OSR. We detected the protein level of the GS3-1 and GS3-4 transgenic plant which under ubiquitin promoter and fused with Flag tag in the C terminal. As expect,the enhanced phenotype mediated by overexpressing GS3-4 was correlated with the increased protein level but not m RNA level. Accumulation of GS3-1 protein but not GS3-4 protein was detected compared with the untreated control when treated with the proteasome inhibitor MG-132,suggesting that GS3-1 might degrade via C terminal domain through the proteasome-mediated pathway. These findings added to the understanding of the molecular mechanism with respect to GS3 in grain size regulation.
引文

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