• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Applied Microbiology >Conserved Eukaryotic Kinase CK2 Chaperone Intrinsically Disordered Protein Interactions
【24h】

Conserved Eukaryotic Kinase CK2 Chaperone Intrinsically Disordered Protein Interactions

机译：保守真核激酶CK2伴侣内无序蛋白质相互作用

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

CK2, a serine/threonine (Ser/Thr) kinase present in eukaryotic cells, is known to have a vast number of substrates. We have recently shown that it localizes to nuclei and at pores between hyphal compartments in Magnaporthe oryzae . We performed a pulldown proteomics analysis of M. oryzae CK2 catalytic subunit MoCKa to detect interacting proteins. The MoCKa pulldown was enriched for septum and nucleolus proteins and intrinsically disordered proteins (IDPs) containing a CK2 phosphorylation motif that is proposed to destabilize and unfold α-helices. This points to a function for CK2 phosphorylation and corresponding phosphatase dephosphorylation in the formation of functional protein-protein aggregates and protein-RNA/DNA binding. To test this as widely as possible, we used secondary data downloaded from databases from a large range of M. oryzae experiments, as well as data for a relatively closely related plant-pathogenic fungus, Fusarium graminearum . We found that CKa expression was strongly positively correlated with Ser/Thr phosphatases, as well as with disaggregases (HSP104, YDJ1, and SSA1) and an autophagy-indicating protein (ATG8). The latter points to increased protein aggregate formation at high levels of CKa expression. Our results suggest a general role for CK2 in chaperoning aggregation and disaggregation of IDPs and their binding to proteins, DNA, and RNA.IMPORTANCE CK2 is a eukaryotic conserved kinase enzyme complex that phosphorylates proteins. CK2 is known to phosphorylate a large number of proteins and is constitutively active, and thus a “normal” role for a kinase in a signaling cascade might not be the case for CK2. Previous results on localization and indications from the literature point to a function for CK2 phosphorylation in shaping and folding of proteins, especially intrinsically disordered proteins, which constitute about 30% of eukaryotic proteins. We used pulldown of interacting proteins and data downloaded from a large range of transcriptomic experiments in M. oryzae and complemented these with data downloaded from a large range of transcriptomic experiments in Fusarium graminearum . We found support for a general role for CK2 in aggregation and disaggregation of IDPs and their binding to proteins, DNA, and RNA—interactions that could explain the importance of CK2 in eukaryotic cell function and disease.
机译：CK2，已知在真核细胞中存在的丝氨酸/苏氨酸（SER / THR）激酶具有大量的基材。我们最近表明它定位于核心和Magnaporthe Oryzae的亚腿室之间的核心。我们对M. Oryzae CK2催化亚单元Mocka进行了下拉蛋白质组学分析以检测相互作用的蛋白质。 Mocka Pulldown富集用于隔膜和核仁蛋白质和含有CK2磷酸化基序的本质上无序的蛋白质（IDP），所述CK2磷酸化基序被提出以使α-螺旋稳定并展开α-螺旋。这指向CK2磷酸化的功能和相应的磷酸酶去磷酸化在形成功能蛋白 - 蛋白质聚集体和蛋白质-RNA / DNA结合中。为了尽可能广泛地测试这一点，我们使用从数据库中下载的二级数据从大量的M. Oryzae实验以及相对密切相关的植物致病真菌，镰刀酸纤维素的数据。我们发现CKA表达与Ser / Thr磷酸酶以及分解酶（HSP104，YDJ1和SSA1）和自噬 - 指示蛋白（ATG8）强烈呈正相关。后者在高水平的CKA表达中增加蛋白质聚集体形成。我们的研究结果表明CK2在陪伴的聚集体中的一般作用和IDP的分解及其与蛋白质，DNA和RNA的结合。分析CK2是磷酸化蛋白质的真核保守激酶酶络合物。已知CK2磷酸化大量蛋白质并且是组成型活性的，因此信号级联中的激酶的“正常”作用可能不是CK2的情况。先前的结果，从文献中的定位和适应症对CK2磷酸化在成型和折叠蛋白质，尤其是内在无序蛋白质的函数，其构成约30％的真核蛋白。我们使用从M. Oryzae中的大量转录组实验下载的相互作用蛋白质和数据的下拉，并将这些数据与来自Fusarium Graminearum的大量转录组实验中下载的数据进行了补充。我们发现支持CK2在IDP的聚集和分解中的一般作用及其与蛋白质，DNA和RNA相互作用的结合，这可以解释CK2在真核细胞功能和疾病中的重要性。

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