Pathogenic Entamoeba histolytica: cDNA cloning of a histone H3 with a divergent primary structure.
Entamoeba histolytica has an unusual nuclear structure characterized by a low degree of chromatin condensation and the absence of stainable metaphase chromosomes. Although nucleosome-like particles were observed, no information about histones was available so far. In this paper we describe a cDNA clone with significant homology to H3 histones that was isolated from a library of pathogenic E. histolytica. The complete cDNA encodes a 15-kDa polypeptide, which like the histone sequence from Volvox carteri is shorter by one residue than the human homologue. The amino acid sequence has only 69% identity with human H3.3 histone and 67% identity with the human H3.1 histone. This is the highest degree of sequence divergence observed for any eukaryote H3 histone sequence. Our results indicate that this divergence may contribute to the unusual chromatin structure of E. histolytica.
Födinger
M
M
Institute of Specific Prophylaxis and Tropical Medicine, University of Vienna, Austria.
Ortner
S
S
Plaimauer
B
B
Wiedermann
G
G
Scheiner
O
O
Duchêne
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002843:Chromatin / Q000502:physiology; D003001:Cloning, Molecular; D016054:DNA, Protozoan / Q000235:genetics* / Q000302:isolation & purification; D004748:Entamoeba histolytica / Q000235:genetics* / Q000472:pathogenicity; D015723:Gene Library; D014644:Genetic Variation; D006657:Histones / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016133:Polymerase Chain Reaction / Q000379:methods; D017386:Sequence Homology, Amino Acid
D002843:Chromatin; D016054:DNA, Protozoan; D006657:Histones