线虫秀丽隐杆线虫组蛋白H2A的一级结构。
The primary structure of histone H2A from the nematode Caenorhabditis elegans.
作者信息
Vanfleteren J R, Van Bun S M, Van Beeumen J J
出版信息
Biochem J. 1987 Apr 1;243(1):297-300. doi: 10.1042/bj2430297.
Abstract
The complete primary structure of histone H2A from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 126 amino acid residues and has a blocked N-terminus. By comparison with calf thymus histone H2A, the nematode protein shows five deletions, two insertions and 16 substitutions. Most of the changes occur in the N- and C-terminal regions of the molecule, whereas the central part covering the residues 21-120 is quite well conserved. The lysine residues 5, 8 and 10 were found to be partially acetylated.
摘要
线虫秀丽隐杆线虫组蛋白H2A的完整一级结构已被确定。氨基酸链由126个氨基酸残基组成，N端封闭。与小牛胸腺组蛋白H2A相比，线虫蛋白有5处缺失、2处插入和16处替换。大多数变化发生在分子的N端和C端区域，而覆盖第21至120位残基的中央部分相当保守。发现赖氨酸残基5、8和10部分被乙酰化。
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