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首页> 外文期刊>Cell Research >The in vitro reconstitution of nucleosome and its binding patterns with HMG1/2 and HMG14/17 proteins
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The in vitro reconstitution of nucleosome and its binding patterns with HMG1/2 and HMG14/17 proteins

机译：HMG1 / 2和HMG14 / 17蛋白的核小体的体外重建及其结合模式

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Using atomic force microscopy (AFM), the dynamic process of the in vitro nucleosome reconstitution followed by slow dilution from high salt to low salt was visualized. Data showed that the histone octamers were dissociated from DNA at 1M NaCl. Whenthe salt concentration was slowly reduced to 650 mM and 300 mM, the core histones bound to the naked DNA gradually. Once the salt concentration was reduced to 50 mM the classic "beads-on-astring" structure was clearly visualized. Furthermore, using the technique of the in vitro reconstitution of nucleosome, the mono- and di- nucleosomes were assembled in vitro with both HS2core (-10681 to -10970 bp) and NCR2 (-372 to -194 bp) DNA sequences in the 5'flanking sequence of human b-globin gene. Data revealedthat HMG 1/2 and HMG14/17 proteins binding to both DNA sequences are changeable following the assembly and disassembly of nucleosomes. We suggest that the changeable binding patterns of HMG 14/17 and HMG1/2 proteins with these regulatory elements may becritical in the process of nucleosome assembly, recruitment of chromatin-modirying activities, and the regulation of human b-globin gene expression.
机译：使用原子力显微镜（AFM），可以看到体外核小体重构的动态过程，然后从高盐缓慢稀释到低盐。数据显示，在1M NaCl下，组蛋白八聚体与DNA分离。当盐浓度缓慢降低至650 mM和300 mM时，核心组蛋白逐渐与裸露的DNA结合。一旦盐浓度降低到50 mM，就可以清楚地看到经典的“串珠”结构。此外，使用核小体的体外重组技术，在体外组装了单核糖体和双核小体，并在5条序列中同时含有HS2core（-10681至-10970 bp）和NCR2（-372至-194 bp）DNA序列。人b-珠蛋白基因的侧翼序列。数据显示与核糖体结合的HMG 1/2和HMG14 / 17蛋白质可在组装和拆卸核小体后发生变化。我们建议，HMG 14/17和HMG1 / 2蛋白与这些调控元件的可变结合模式可能在核小体装配，染色质修饰活性募集和人类b珠蛋白基因表达的调控过程中至关重要。

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