...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The FEBS journal >In vitro embryonic developmental phosphorylation of the cellular nucleic acid binding protein by cAMP-dependent protein kinase, and its relevance for biochemical activities
【24h】

In vitro embryonic developmental phosphorylation of the cellular nucleic acid binding protein by cAMP-dependent protein kinase, and its relevance for biochemical activities

机译：cAMP依赖性蛋白激酶对细胞核酸结合蛋白的体外胚胎发育磷酸化及其与生化活性的关系

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The zinc-finger cellular nucleic acid binding protein (CNBP) is a strikingly conserved single-stranded nucleic acid binding protein essential for normal forebrain formation during mouse and chick embryogenesis. CNBP cDNAs from a number of vertebrates have been cloned and analysed. CNBP is mainly conformed by seven retroviral Cys-Cys-His-Cys zinc-knuckles and a glycine/arginine rich region box. CNBP amino acid sequences show a putative Pro-Glu-Ser-Thr site of proteolysis and several putative phosphorylation sites. In this study, we analysed CNBP phosphorylation by embryonic kinases and its consequences on CNBP biochemical activities. We report that CNBP is differentially phosphorylated by Danio rerio embryonic extracts. In vitro CNBP phosphorylation is basal and constant at early embryonic developmental stages, it begins to increase after mid-blastula transition stage reaching the highest level at 48 hours postfertilization stage, and decreases thereafter to basal levels at 5 days postfertilization. The cAMP-dependent protein kinase (PKA) was identified as responsible for phosphorylation on the unique CNBP conserved putative phosphorylation site. Site-directed mutagenesis replacing the PKA phospho-acceptor amino acid residue impairs CNBP phosphorylation, suggesting that phosphorylation may not only exist in D. rerio but also in other vertebrates. CNBP phosphorylation does not change single-stranded nucleic acid binding capability. Instead, it promotes in vitro the annealing of complementary oligonucleotides representing the CT element (CCCTCCCC) from the human cellular myelocytomatosis oncogene (c-myc) promoter, an element responsible for c-myc enhancer transcription. Our results suggest that phosphorylation might be a conserved post-translational modification that allows CNBP to perform a fine tune expression regulation of a group of target genes, including c-myc, during vertebrate embryogenesis.
机译：锌指细胞核酸结合蛋白（CNBP）是一种显着保守的单链核酸结合蛋白，对于小鼠和鸡胚发生过程中正常的前脑形成至关重要。已经克隆和分析了来自许多脊椎动物的CNBP cDNA。 CNBP主要由七个逆转录病毒Cys-Cys-His-Cys锌指节和一个富含甘氨酸/精氨酸的区域框组成。 CNBP氨基酸序列显示出一个假定的Pro-Glu-Ser-Thr蛋白水解位点和几个假定的磷酸化位点。在这项研究中，我们分析了胚胎激酶引起的CNBP磷酸化及其对CNBP生化活性的影响。我们报告说，CNBP是由丹尼奥雷里奥胚胎提取物差异磷酸化的。体外CNBP磷酸化在胚胎发育的早期阶段是基础且恒定的，在囊胚中期过渡阶段后开始增加，在受精后48小时达到最高水平，此后在受精后5天降至基础水平。经鉴定，依赖cAMP的蛋白激酶（PKA）负责唯一CNBP保守的假定磷酸化位点上的磷酸化。取代PKA磷酸受体氨基酸残基的定点诱变会损害CNBP磷酸化，这表明磷酸化不仅可能存在于D. rerio中，而且也可能存在于其他脊椎动物中。 CNBP磷酸化不会改变单链核酸结合能力。取而代之的是，它促进了来自人类细胞骨髓细胞瘤癌基因（c-myc）启动子（代表c-myc增强子转录的元件）中代表CT元件（CCCTCCCC）的互补寡核苷酸的体外退火。我们的结果表明，磷酸化可能是保守的翻译后修饰，可使CNBP在脊椎动物胚胎发生过程中对包括c-myc在内的一组靶基因进行微调表达调节。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号