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Structure and expression of a cDNA encoding a histone H2A from Euglena gracilis
Authors:Agnes Saint-Guily  Marie-Luce Schantz  Rodolphe Schantz
Affiliation:(1) Physlologie et Génétique végétales, Université Blaise Pascal, 4 rue Ledru, 63038 Clermont-Ferrand cédex 1, France;(2) Institut de Biologie Moleculaire des Plantes, 12 rue du General Zimmer, 67084 Strasbourg, France
Abstract:Screening of a lambdagt11 cDNA expression library of Euglena gracilis with antibodies directed against histones H2 from maize resulted in the isolation of a full-length cDNA for a histone H2A. The open-reading frame of 408 bp corresponded to a protein of 136 amino acid residues (14 kDa). Despite the presence of a poly(A) tail, which is typical of plant histone mRNA but not of animal histone mRNA, the size of the deduced protein and its percentage of homology were closer to animal histone H2As than to plant or lower eukaryotic histone H2A.Sequence alignment revealed that the Euglena H2A protein was characterized by a shorter C-terminus and a N-terminus which extended 10 residues past the animal H2A.
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