PROTEINS FROM THE PROKARYOTIC NUCLEOID - PRIMARY AND QUATERNARY STRUCTURE OF THE 15-KD ESCHERICHIA-COLI DNA-BINDING PROTEIN H-NS
PROTEINS FROM THE PROKARYOTIC NUCLEOID - PRIMARY AND QUATERNARY STRUCTURE OF THE 15-KD ESCHERICHIA-COLI DNA-BINDING PROTEIN H-NS
复制标题
DOI：
10.1111/j.1365-2958.1988.tb00035.x
复制
发表时间：
1988-05-01
影响因子：
3.6
通讯作者：
PON, CL
中科院分区：
文献类型：
--
作者：
FALCONI, M;GUALTIERI, MT;PON, CL
一种丰富的大肠杆菌DNA结合蛋白H-NS(136个氨基酸残基，MR=15,402)的一级序列已经被阐明，并通过蛋白质-蛋白质交联反应研究了它的四级结构。结果发现，即使在很低的浓度下，H-NS也主要以二聚体的形式存在，但在较高的浓度下也可能形成四聚体，导致二聚化的蛋白质-蛋白质相互作用主要是疏水的。
The primary sequence of H-NS (136 amino acid residues, Mr = 15,402), an abundant Escherichia coli DNA-binding protein, has been elucidated and its quaternary structure has been investigated by protein-protein cross-linking reactions. It was found that H-NS exists predominantly as a dimer, even at very low concentrations, but may form tetramers at higher concentrations and that the protein-protein interaction responsible for the dimerization is chiefly hydrophobic.