Arents G, Moudrianakis E N
Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.
Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):11170-4. doi: 10.1073/pnas.92.24.11170.
The histones of all eukaryotes show only a low degree of primary structure homology, but our earlier crystallographic results defined a three-dimensional structural motif, the histone fold, common to all core histones. We now examine the specific architectural patterns within the fold and analyze the nature of the amino acid residues within its functional segments. The histone fold emerges as a fundamental protein dimerization motif while the differentiations of the tips of the histone dimers appear to provide the rules of core octamer assembly and the basis for nucleosome regulation. We present evidence for the occurrence of the fold from archaebacteria to mammals and propose the use of this structural motif to define a distinct family of proteins, the histone fold superfamily. It appears that evolution has conserved the conformation of the fold even through variations in primary structure and among proteins with various functional roles.
所有真核生物的组蛋白仅显示出较低程度的一级结构同源性，但我们早期的晶体学研究结果确定了一种三维结构基序——组蛋白折叠，它是所有核心组蛋白共有的。我们现在研究该折叠结构内的特定结构模式，并分析其功能片段内氨基酸残基的性质。组蛋白折叠成为一种基本的蛋白质二聚化基序，而组蛋白二聚体末端的差异似乎为核心八聚体组装规则和核小体调控奠定了基础。我们提供了从古细菌到哺乳动物存在该折叠结构的证据，并建议利用这种结构基序来定义一个独特的蛋白质家族——组蛋白折叠超家族。即使在一级结构存在差异以及具有各种功能作用的蛋白质之间，进化似乎也保留了该折叠结构的构象。
