Molecular cloning of a pea H1 histone cDNA.
Molecular cloning of a pea H1 histone cDNA.
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DOI：
10.1111/j.1432-1033.1987.tb13490.x
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发表时间：
1987-07
期刊：
影响因子：
--
通讯作者：
J. Gantt;J. L. Key
中科院分区：
文献类型：
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作者：
J. Gantt;J. L. Key
豌豆（Pisum sativum，var. Little Marvel）H1组蛋白cDNA已从λ gt11表达载体文库中分离。该cDNA已被测序，并显示代表mRNA的整个蛋白质编码区。推导的蛋白质序列长265个氨基酸（28018 Da），含有70个赖氨酸和3个赖氨酸。编码的蛋白质的结构与动物富含赖氨酸的组蛋白相当。中心区域的氨基酸组成与动物富含赖氨酸的组蛋白的球状结构域中发现的氨基酸组成相似，其两侧是富含赖氨酸、谷氨酸和脯氨酸的氨基末端区域和富含赖氨酸、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蛋白是不寻常的，因为前40个氨基酸中有12个是谷氨酸。
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.