cDNA cloning of Entamoeba histolytica histone H3.
E. histolytica has an unusual nuclear structure. 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 lambda Zap library of pathogenic E. histolytica. The complete cDNA encodes a 15 kDa polypeptide, which is shorter by one residue than the human homologue. The amino acid sequence has only 69% identity with human H3.3 histone. 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
D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics*; D016054:DNA, Protozoan / Q000235:genetics*; D004748:Entamoeba histolytica / Q000235:genetics* / Q000472:pathogenicity; D006657:Histones / Q000235:genetics*; D015800:Protozoan Proteins / Q000235:genetics*; D016053:RNA, Protozoan / Q000235:genetics
D018076:DNA, Complementary; D016054:DNA, Protozoan; D006657:Histones; D015800:Protozoan Proteins; D016053:RNA, Protozoan