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酵母内部组蛋白与组蛋白-组蛋白相互作用的进化保守性

Yeast inner histones and the evolutionary conservation of histone-histone interactions.

作者信息

Mardian J K, Isenberg I

出版信息

Biochemistry. 1978 Sep 5;17(18):3825-33. doi: 10.1021/bi00611a023.

Abstract

The inner histones of the yeast, Saccharomyces cerevisiae, have been isolated and identified by their amino acid compositions. H4 appears to be close to its calf and pea counterparts. H2a, H2b, and H3 have diverged. The isolation of the histones was accomplished by consecutive slab-gel fractionation, and a number of novel features of the method are described. These appear to be generally useful for preparing many types of protein. The binding pattern of the yeast inner histones is identical to the binding pattern for calf and for pea histones. Data on interspecies complexing indicate that the surfaces across which the histones interact are very highly conserved.

摘要

酿酒酵母的核心组蛋白已通过氨基酸组成进行分离和鉴定。H4似乎与小牛和豌豆的对应物相近。H2a、H2b和H3则有所分化。组蛋白的分离是通过连续的平板凝胶分级分离完成的,并描述了该方法的一些新特点。这些特点似乎普遍适用于制备多种类型的蛋白质。酵母核心组蛋白的结合模式与小牛和豌豆组蛋白的结合模式相同。种间复合的数据表明,组蛋白相互作用的表面高度保守。

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