title: Molecular cloning of a pea H1 histone cDNA.
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.
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000235:genetics*; D005822:Genetic Vectors; D006657:Histones / Q000235:genetics*; D007120:Immunochemistry; D008239:Lysine / Q000032:analysis; D010940:Plant Proteins / Q000235:genetics*; D010946:Plants, Medicinal
chemical_list: D006657:Histones; D010940:Plant Proteins; D004247:DNA; D008239:Lysine