BINDING OF A PEA NUCLEAR-PROTEIN TO PROMOTERS OF CERTAIN PHOTOREGULATED GENES IS MODULATED BY PHOSPHORYLATION
BINDING OF A PEA NUCLEAR-PROTEIN TO PROMOTERS OF CERTAIN PHOTOREGULATED GENES IS MODULATED BY PHOSPHORYLATION
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DOI：
10.1105/tpc.1.11.1069
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发表时间：
1989-11-01
期刊：
影响因子：
11.6
通讯作者：
CASHMORE, AR
中科院分区：
文献类型：
--
作者：
DATTA, N;CASHMORE, AR
最近有许多报道记载了DNA结合蛋白的磷酸化[Montminy和Bilezikjian（1987）; Sorger，刘易斯和Pelham（1987）; Hoeffler，Kovelman和Roeder（1988）; Jones等（1988）; Prywes等（1988）; Sorger和Pelham（1988）; Yamamoto等人（1988）]，并且这些蛋白质中的至少一种的转录调节活性似乎受到这种修饰的调节[Montminy和Biliezikjian（1987）; Yamamoto等人（1988）]。我们在这里报告一种植物核蛋白，其DNA结合活性受到磷酸化的强烈影响。该蛋白AT-1与某些核基因启动子内的特定AT富集元件（AT-1盒）结合，所述核基因编码核酮糖-1，5-二磷酸羧化酶的小亚基和捕光叶绿素a/B蛋白复合物的多肽组分。AATATTTTTATT是AT-1盒的共有序列。我们发现，豌豆核提取物中AT-1的DNA结合能力可以通过磷酸化可逆地调节。AT-1在非磷酸化形式下是有活性的，并且由于磷酸化而失去所有DNA结合能力。磷酸化AT-1的激酶使用Mg-ATP和Mg-GTP作为底物，并被肝素和精胺抑制，这表明是NII型酪蛋白激酶。
There have been numerous recent reports documenting phosphorylation of DNA-binding proteins [Montminy and Bilezikjian (1987); Sorger, Lewis, and Pelham (1987); Hoeffler, Kovelman, and Roeder (1988); Jones et al. (1988); Prywes et al. (1988); Sorger and Pelham (1988); Yamamoto et al. (1988)], and the transcriptional regulatory activity of at least one of these proteins appears to be modulated by this modification [Montminy and Biliezikjian (1987); Yamamotoet al. (1988)]. We report here on a plant nuclear protein, the DNA-binding activity of which is strongly affected by phosphorylation. This protein, AT-1, binds to specific AT-rich elements (the AT-1 box) within promoters of certain nuclear genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase and the polypeptide components of the light-harvesting chlorophyll a/b protein complex. A consensus sequence of AATATTTTTATT was derived for the AT-1 box. We deomonstrate that the DNA-binding ability of AT-1, from nuclear extracts of pea, can be reversibly modulated by phosphorylation. AT-1 is active in the nonphosphorylated form and loses all DNA-binding ability as a result of phosphorylation. The kinase that phosphorylates AT-1 uses both Mg-ATP and Mg-GTP as a substrate and is inhibited by heparin and spermine, indicative of an NII-type casein kinase.