Conserved eukaryotic histone-fold residues substituted into an archaeal histone increase DNA affinity but reduce complex flexibility.
Conserved eukaryotic histone-fold residues substituted into an archaeal histone increase DNA affinity but reduce complex flexibility.
复制标题
保守的真核组蛋白折叠残基取代古细菌组蛋白可增加 DNA 亲和力，但会降低复合物的灵活性。
DOI：
10.1128/jb.185.11.3453-3457.2003
复制
发表时间：
2003
影响因子：
3.2
通讯作者：
Reeve,JohnN
中科院分区：
文献类型：
--
作者：
Soares,DivyaJ;Marc,Frédéric;Reeve,JohnN
虽然古细菌和真核细胞核小体核心组蛋白从一个共同的祖先进化而来，但保守的赖氨酸残基存在于所有四种真核细胞组蛋白中不存在于古细菌组蛋白中的DNA结合位置。在古细菌组蛋白HMfB的相应位置引入赖氨酸残基，产生了对DNA亲和力增加的变体，与DNA形成更紧密的复合物。然而，这些复合物不再促进短DNA分子的环化，并且已经失去了将DNA交替地包裹在负或正超螺旋中的灵活性。
Although the archaeal and eukaryotic nucleosome core histones evolved from a common ancestor, conserved lysine residues are present at DNA-binding locations in all four eukaryotic histones that are not present in the archaeal histones. Introduction of lysine residues at the corresponding locations into an archaeal histone, HMfB, generated a variant with increased affinity for DNA that formed more compact complexes with DNA. However, these complexes no longer facilitated the circularization of short DNA molecules and had lost the flexibility to wrap DNA alternatively in either a negative or positive supercoil.