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来自拟南芥的两个编码SNF-1相关蛋白激酶的新基因:AtSR1和AtSR2转录本对细胞分裂素和糖类的差异积累,以及AtSR2对蔗糖合酶的磷酸化作用。

Two novel genes encoding SNF-1 related protein kinases from Arabidopsis thaliana: differential accumulation of AtSR1 and AtSR2 transcripts in response to cytokinins and sugars, and phosphorylation of sucrose synthase by AtSR2.

作者信息

Chikano H, Ogawa M, Ikeda Y, Koizumi N, Kusano T, Sano H

机构信息

Laboratory of Plant Molecular Breeding, Research and Education Center for Genetic Information, Nara Institute of Science and Technology, Ikoma, Japan.

出版信息

Mol Gen Genet. 2001 Jan;264(5):674-81. doi: 10.1007/s004380000354.

Abstract

We searched for genes encoding members of the group-3 SNF1-related protein kinase (SnRK3) family in the Arabidopsis thaliana database, and seven independent sequences were identified. Transcripts of two of them were found to accumulate differentially upon treatment with light, cytokinins and sugars. Full-length cDNAs were isolated and designated as AtSR1 and AtSR2; they encode polypeptides of 442 and 429 amino acids with relative molecular masses of 50.3 kDa and 48.2 kDa, respectively. In etiolated seedlings, no transcripts of either gene were observed. However, upon exposure to light or cytokinins, transcripts of AtSR1 but not AtSR2 began to accumulate. The induction with light was greatly reduced in the presence of a cytokinin antagonist, suggesting that cytokinins are involved in light-signaling pathways. In contrast, transcription of AtSR2, but not of AtSR1, was greatly increased by sucrose, as well as glucose and fructose. AtSR2 expressed in E. coli efficiently phosphorylated sucrose synthase in the presence of manganese ions. These results suggest that, although SnRK3 proteins may generally be involved in sugar metabolism, expression of AtSR1 and AtSR2 is differentially and distinctly regulated by various external signals, and AtSR2 may function in the regulation of sucrose synthase by specific phosphorylation.

摘要

我们在拟南芥数据库中搜索了编码3组SNF1相关蛋白激酶(SnRK3)家族成员的基因,共鉴定出7个独立序列。其中两个序列的转录本在光照、细胞分裂素和糖类处理后出现差异积累。分离出了全长cDNA,并将其命名为AtSR1和AtSR2;它们分别编码442和429个氨基酸的多肽,相对分子质量分别为50.3 kDa和48.2 kDa。在黄化幼苗中,未观察到这两个基因的转录本。然而,在光照或细胞分裂素处理后,AtSR1的转录本开始积累,而AtSR2的转录本未积累。在细胞分裂素拮抗剂存在的情况下,光照诱导作用大大降低,这表明细胞分裂素参与了光信号通路。相反,蔗糖以及葡萄糖和果糖可使AtSR2的转录大幅增加,而AtSR1的转录则无明显变化。在大肠杆菌中表达的AtSR2在锰离子存在的情况下能够有效磷酸化蔗糖合酶。这些结果表明,尽管SnRK3蛋白可能普遍参与糖代谢,但AtSR1和AtSR2的表达受到各种外部信号的差异且独特的调控,并且AtSR2可能通过特异性磷酸化作用于蔗糖合酶的调控。

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