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豌豆H1组蛋白cDNA的分子克隆

Molecular cloning of a pea H1 histone cDNA.

作者信息

Gantt J S, Key J L

出版信息

Eur J Biochem. 1987 Jul 1;166(1):119-25. doi: 10.1111/j.1432-1033.1987.tb13490.x.

Abstract

A pea (Pisum sativum, var. Little Marvel) H1 histone cDNA has been isolated from a lambda gt11 expression vector library. This cDNA has been sequenced and shown to represent the entire protein-coding region of the mRNA. The deduced protein sequence is 265 amino acids long (28018 Da) and contains 70 lysines and 3 arginines. The structure of the encoded protein is comparable to animal lysine-rich histones. The central region, which has an amino acid composition similar to that found in the globular domains of animal lysine-rich histones, is flanked by an amino-terminal region rich in lysine, glutamic acid and proline and by a carboxyl-terminal region rich in lysine, alanine, valine and proline. Despite the structural similarities, the protein has little sequence homology with animal lysine-rich histones. This H1 protein is unusual because 12 of the first 40 amino acids are glutamic acid.

摘要

已从λgt11表达载体文库中分离出豌豆(Pisum sativum,变种Little Marvel)H1组蛋白cDNA。对该cDNA进行了测序,结果表明它代表了mRNA的整个蛋白质编码区。推导的蛋白质序列长度为265个氨基酸(28018道尔顿),包含70个赖氨酸和3个精氨酸。编码蛋白的结构与动物富含赖氨酸的组蛋白相当。中央区域的氨基酸组成与动物富含赖氨酸组蛋白的球状结构域中的氨基酸组成相似,其两侧分别是富含赖氨酸、谷氨酸和脯氨酸的氨基末端区域以及富含赖氨酸、丙氨酸、缬氨酸和脯氨酸的羧基末端区域。尽管结构相似,但该蛋白质与动物富含赖氨酸的组蛋白几乎没有序列同源性。这种H1蛋白不同寻常,因为前40个氨基酸中有12个是谷氨酸。

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