Kmiécik D, Bélaïche D, Sautière P, Loucheux-Lefebvre M H, Kerckaert J P
Centre National de la Recherche Scientifique, Université de Lille II, France.
Eur J Biochem. 1991 Jun 1;198(2):275-83. doi: 10.1111/j.1432-1033.1991.tb16012.x.
The complete amino acid sequence (122 residues) of histone H2B from erythrocytes of the marine worm Sipunculus nudus, has been established from sequence analysis of peptides generated by highly specific cleavage of the protein and from the nucleotide sequence of the encoding gene. The isolation of the H2B gene was facilitated by using a highly specific nucleotide probe, devised from amino acids 58-68 of the protein. The presence of an N,N-dimethylproline residue at the amino-terminus of the protein was established from data provided by mass spectrometry and NMR spectroscopy. This unusual post-translational modification of histone H2B generates a stable positive charge which could strongly interact with the linker DNA.
通过对由该蛋白质高度特异性切割产生的肽段进行序列分析以及对编码基因的核苷酸序列分析，已确定了海蚯蚓光裸方格星虫红细胞中组蛋白H2B的完整氨基酸序列（122个残基）。利用从该蛋白质第58 - 68位氨基酸设计的高度特异性核苷酸探针，有助于分离H2B基因。通过质谱和核磁共振光谱提供的数据确定了该蛋白质氨基末端存在N，N - 二甲基脯氨酸残基。组蛋白H2B这种不寻常的翻译后修饰产生了一个稳定的正电荷，它可能与连接DNA发生强烈相互作用。
