首页> 外文学位 >NMR analysis of the thymidylate synthase mRNA binding site 1-paromomycin interaction, Moorella thermoacetica selenocysteine elongation factor binding surface for its SECIS RNA, and the nucleocapsid hairpin loop structure of the Ebola virus.

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NMR analysis of the thymidylate synthase mRNA binding site 1-paromomycin interaction, Moorella thermoacetica selenocysteine elongation factor binding surface for its SECIS RNA, and the nucleocapsid hairpin loop structure of the Ebola virus.

机译：胸苷酸合酶mRNA结合位点1-巴龙霉素相互作用，Moorella thermoacetica硒代半胱氨酸延伸因子与其SECIS RNA的结合表面以及埃博拉病毒的核衣壳发夹环结构的NMR分析。

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1. Structural elucidation of the thymidylate synthase mRNA binding site 1 construct (TSMC) and investigation of the paromomycin-TSMC interaction via NMR analysis. The chemical shift perturbations of the H6/H5 protons of TSMC upon paromomycin binding were analyzed via TOCSY experiments. The sum of incremental displacements in delta1H H5 and delta1HH6 for cytosine residues monitoring the high and low affinity binding of paromomycin were fit to a sequential two site binding model. The specific and non-specific dissociation constants were calculated 101 +/- 79.1 muM, and 706 +/- 301 muM, respectively. The CC mismatch and its surrounding GC basepairs experienced the highest degree of chemical shift change. Specifically, paromomycin approached the major groove side of these residues. The solution state structure of TSMC free was determined. The CC mismatch is stabilized by a non-canonical one hydrogen bond basepair and its hydrogen bonding pattern reveals its structural relationship with its flanking GC basepairs. Regarding paromomycin, rings I and II exhibit the highest degree of chemical shift change.;3. NMR evidence of an internal basepair in the 'pseudoheptaloop' of the Ebola viral Nucleocapsid Hairpin. The most studied protein of the Ebola genome, VP30, has a transcriptional activation role on the first gene of this virus. This biochemical event is important for regulating levels of a nucleoprotein. Specifically, VP30 is thought to interact with an AU rich 'seven-membered' loop of this nucleocapsid hairpin. Complete proton assignments of this RNA, including those obtained from hydrogen bond experiments were used to identify an internal AU basepair in this 'pseudoheptaloop'.;2. A study of the Moorella thermoacetica SelB/SECIS hairpin interaction via NMR analysis. Measurement of the chemical shift changes of SelB-MT508--634 (i.e. Winged Helix Domain (WHD) 3 and 4) due to SECIS-MT RNA binding was sufficient to map out the binding surface of this protein. NMR data also showed a region in the 3rd WHD that was affected by SECIS-MT binding. This secondary site is located at exactly a position where a bulged out uridine residue of the E. coli SECIS RNA would make a closer contact. This was used to propose the higher affinity observed for the SelB-EC/SECIS-EC complex over the SelB-MT/SECIS-MT pair.

机译：1.胸苷酸合酶mRNA结合位点1构建体（TSMC）的结构解析，以及通过核磁共振分析研究巴龙霉素-TSMC相互作用。通过TOCSY实验分析了巴龙霉素结合后TSMC H6 / H5质子的化学位移扰动。监测巴龙霉素的高和低亲和力结合的胞嘧啶残基在delta1H H5和delta1HH6中增量位移的总和适合于连续的两个位点结合模型。分别计算出101和/或79.1μM和706和/或301μM的特异性和非特异性解离常数。 CC不匹配及其周围的GC碱基对经历了最高程度的化学位移变化。具体而言，巴龙霉素接近这些残基的主要沟侧。确定了无台积电的溶液状态结构。 CC错配由一个非规范的一个氢键碱基对稳定，其氢键模式揭示了其与侧翼GC碱基对的结构关系。关于巴龙霉素，环I和环II表现出最高的化学位移变化程度； 3。核磁共振的证据表明，埃博拉病毒核壳型发夹的“假七趾oop”内部存在一个碱基对。埃博拉病毒基因组中研究最多的蛋白质VP30在该病毒的第一个基因上具有转录激活作用。这种生化事件对于调节核蛋白的水平很重要。具体而言，认为VP30与该核衣壳发夹的AU丰富的“七元”环相互作用。该RNA的完整质子分配，包括从氢键实验获得的质子分配，被用于识别该“伪七足动物”中的内部AU碱基对； 2。通过NMR分析研究Moorella thermoacetica SelB / SECIS发夹相互作用。由于SECIS-MT RNA结合而导致的SelB-MT508--634（即双螺旋结构域（WHD）3和4）的化学位移变化的测量足以绘制出该蛋白的结合表面。 NMR数据还显示了第三WHD中受SECIS-MT结合影响的区域。该第二位点恰好位于大肠杆菌SECIS RNA的膨出的尿苷残基紧密接触的位置。这被用于提出在SelB-MT / SECIS-MT对上观察到的SelB-EC / SECIS-EC复合物更高的亲和力。

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作者
Tavares, Tony.;
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York University (Canada).;

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授予单位 York University (Canada).;
学科 Biochemistry.
学位 Ph.D.
年度 2008
页码 288 p.
总页数 288
原文格式 PDF
正文语种 eng
中图分类
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入库时间 2022-08-17 11:39:33

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1. The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB [J] . Beribisky AV, Tavares TJ, Amborski AN, RNA . 2007,第11期

机译：热乙酸穆尔氏菌硒代半胱氨酸插入序列RNA发夹的三维结构及其与延伸因子SelB的相互作用
2. Solution Structure of SECIS, the Mrna Element Required for Eukaryotic Selenocysteine Insertion -Interaction Studies With the SECIS-Binding Protein SBP [J] . 生物医学与环境科学（英文版） . 1997,第002期

机译：SECIS的溶液结构，真核硒代半胱氨酸插入所需的Mrna元素-与SECIS结合蛋白SBP的相互作用研究
3. Solution Structure of SECIS, the Mrna Element Required for Eukaryotic Selenocysteine Insertion -Interaction Studies With the SECIS-Binding Protein SBP [J] . 生物医学与环境科学（英文版） . 1997,第003期

机译：SECIS的溶液结构，真核硒代半胱氨酸插入所需的Mrna元素-与SECIS结合蛋白SBP的相互作用研究
4. The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB [O] . Alexander V. Beribisky, Tony J. Tavares, Andrew N. Amborski, 2007

机译：热乙酸穆尔氏菌硒代半胱氨酸插入序列RNA发夹的三维结构及其与延伸因子SelB的相互作用
5. The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB [O] . Beribisky, Alexander V., Tavares, Tony J., Amborski, Andrew N., 2007

机译：热乙酸穆尔氏菌硒代半胱氨酸插入序列RNA发夹的三维结构及其与延伸因子SelB的相互作用

NMR analysis of the thymidylate synthase mRNA binding site 1-paromomycin interaction, Moorella thermoacetica selenocysteine elongation factor binding surface for its SECIS RNA, and the nucleocapsid hairpin loop structure of the Ebola virus.

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