Laine B, Bélaïche D, Khanaka H, Sautière P
Eur J Biochem. 1983 Mar 15;131(2):325-31. doi: 10.1111/j.1432-1033.1983.tb07265.x.
The amino acid sequence of protein HRm, a DNA-binding HU-type protein of 90 residues (Mr 9303), isolated from Rhizobium meliloti, has been established from automated sequence analysis of the protein and from structural data provided by peptides derived from cleavage of the protein at arginine and aspartic acid residues. The comparison of the primary structure of protein HRm with that of other HU-type proteins shows that two short sequences, of 7 and 6 residues respectively, located in the median part of the molecule, appear highly conserved and may be important in the function of the protein.
从苜蓿根瘤菌中分离出的蛋白质HRm是一种含90个残基(分子量9303)的DNA结合HU型蛋白质,其氨基酸序列已通过该蛋白质的自动序列分析以及由该蛋白质在精氨酸和天冬氨酸残基处裂解产生的肽段所提供的结构数据得以确定。蛋白质HRm的一级结构与其他HU型蛋白质的一级结构比较表明,位于分子中部的分别由7个和6个残基组成的两个短序列显得高度保守,可能对该蛋白质的功能很重要。