N-terminal region of P protein of Chandipura virus is responsible for phosphorylation-mediated homodimerization
N-terminal region of P protein of Chandipura virus is responsible for phosphorylation-mediated homodimerization
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DOI：
10.1093/protein/13.6.437
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发表时间：
2000-06-01
期刊：
影响因子：
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通讯作者：
Chattopadhyay, DJ
中科院分区：
文献类型：
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作者：
Raha, T;Samal, E;Chattopadhyay, DJ
Chandipura（CHP）病毒，印度分离的弹状病毒的磷蛋白P被发现支持酪蛋白激酶II（CKII）磷酸化后的转录。磷酸化诱导的蛋白质构象的变化被发现发生在N-末端区域的蛋白质。进一步表征这种基于磷酸化的构象改变的生物化学研究表明，磷酸化导致蛋白质从“开放”结构转变为“封闭”结构。CKII引入的磷酸基团被发现对磷酸酶具有抗性，这种基于磷酸化的结构改变改变了蛋白质的可接近疏水表面面积，也改变了不同蛋白酶的可利用消化位点。使用相同的方法，发现N-末端46个氨基酸仅在磷酸化后负责P-P二聚化。
The phosphoprotein P of Chandipura (CHP) virus, an Indian isolate of rhabdovirus, was found to support transcription upon phosphorylation by casein kinase II (CKII). A phosphorylation-induced change in the protein conformation was found to occur at the N-terminal region of the protein. Biochemical studies for further characterization of this phosphorylation-based conformational alteration demonstrated that phosphorylation leads to the transition from an 'open' to 'closed' structure of the protein. The phosphate group introduced by CKII was found to be resistant to phosphatases, This phosphorylation-based structural alteration changes the accessible hydrophobic surface area of the protein and also the available digestion sites of different proteases, The phosphorylated form of P protein was found to be a dimer by His-tag dilution assay. Using the same approach it was found that the N-terminal 46 amino acids are responsible for P-P dimerization, only after phosphorylation.