title: The Leishmania infantum histone H3 possesses an extremely divergent N-terminal domain.
abstract: The isolation of a Leishmania cDNA clone coding for an antigen identified as the histone H3 is described. The nucleotide sequence of the cDNA predicts that the Leishmania histone H3 contains 129 residues and that it has a molecular mass of 14,620 Da. Comparison of the amino acid sequence with the consensus sequence of the eukaryotic histone H3 shows that the Leishmania protein has a highly conserved globular region and an extremely divergent amino-terminal portion.
authors.affiliation: Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Universidad Autonoma de Madrid, Spain.
authors.forename: M
authors.initials: M
authors.lastname: Soto
authors.forename: J M
authors.initials: JM
authors.lastname: Requena
authors.forename: G
authors.initials: G
authors.lastname: Morales
authors.forename: C
authors.initials: C
authors.lastname: Alonso
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000953:Antigens, Protozoan / Q000276:immunology; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D017125:Genes, Protozoan; D006657:Histones / Q000235:genetics*; D018314:Leishmania infantum / Q000235:genetics*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D000953:Antigens, Protozoan; D018076:DNA, Complementary; D006657:Histones