COMPLETE SEQUENCE OF SIPUNCULUS-NUDUS ERYTHROCYTE HISTONE-H2B AND ITS GENE - IDENTIFICATION OF AN N,N-DIMETHYLPROLINE RESIDUE AT THE AMINO-TERMINUS
COMPLETE SEQUENCE OF SIPUNCULUS-NUDUS ERYTHROCYTE HISTONE-H2B AND ITS GENE - IDENTIFICATION OF AN N,N-DIMETHYLPROLINE RESIDUE AT THE AMINO-TERMINUS
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DOI：
10.1111/j.1432-1033.1991.tb16012.x
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发表时间：
1991-06-01
期刊：
影响因子：
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通讯作者：
KERCKAERT, JP
中科院分区：
文献类型：
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作者：
KMIECIK, D;BELAICHE, D;KERCKAERT, JP
从海洋蠕虫红细胞组蛋白H_2B高度特异性裂解产生的多肽和编码基因的核苷酸序列分析中，确定了该蛋白的完整氨基酸序列(122个残基)。通过使用从蛋白质的58-68个氨基酸中设计的高度特异的核苷酸探针，可以方便地分离出H2B基因。根据质谱学和核磁共振波谱提供的数据，确定了蛋白质氨基末端存在N，N-二甲基脯氨酸残基。这种不寻常的组蛋白H2B翻译后修饰产生稳定的正电荷，可以与连接物DNA强烈相互作用。
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.