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首页> 外文期刊>Journal of Molecular Biology >Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancement
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Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancement

机译：酵母Nhp6A的基本N端调节其DNA柔韧性增强的机制

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摘要

HMGB (high-mobility group box) proteins are members of a class of small proteins that are ubiquitous in eukaryotic cells and nonspecifically bind to DNA, inducing large-angle DNA bends, enhancing the flexibility of DNA, and likely facilitating numerous important biological interactions. To determine the nature of this behavior for different HMGB proteins, we used atomic force microscopy to quantitatively characterize the bend angle distributions of DNA complexes with human HMGB2(Box A), yeast Nhp6A, and two chimeric mutants of these proteins. While all of the HMGB proteins bend DNA to preferred angles, Nhp6A promoted the formation of higher-order oligomer structures and induced a significantly broader distribution of angles, suggesting that the mechanism of Nhp6A is like a flexible hinge more than that of HMGB2(Box A). To determine the structural origins of this behavior, we used portions of the cationic N-terminus of Nhp6A to replace corresponding HMGB2(Box A) sequences. We found that the oligomerization and broader angle distribution correlated directly with the length of the N-terminus incorporated into the HMGB2(Box A) construct. Therefore, the basic N-terminus of Nhp6A is responsible for its ability to act as a flexible hinge and to form high-order structures.
机译：HMGB（高迁移率族盒）蛋白是一类小蛋白的成员，这些蛋白在真核细胞中普遍存在，并且非特异性地与DNA结合，诱导大角度DNA弯曲，增强DNA的柔韧性，并可能促进许多重要的生物学相互作用。为了确定这种行为对于不同的HMGB蛋白的性质，我们使用原子力显微镜定量表征了具有人类HMGB2（盒A），酵母Nhp6A和这些蛋白的两个嵌合突变体的DNA复合物的弯曲角分布。尽管所有HMGB蛋白都将DNA弯曲至优选的角度，但Nhp6A促进了高阶寡聚物结构的形成并诱导了角度的明显更宽的分布，这表明Nhp6A的机制比HMGB2更像是一种柔性铰链）。为了确定此行为的结构起源，我们使用Nhp6A阳离子N端的部分替换了相应的HMGB2（Box A）序列。我们发现低聚和更广的角度分布与并入HMGB2（Box A）结构的N末端的长度直接相关。因此，Nhp6A的基本N端负责其充当柔性铰链和形成高阶结构的能力。

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