Detalle de: The Leishmania infantum histone H3 possesses an extremely divergent N-terminal domain
| 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. |
| Apa Reference | Soto, M., Requena, JoséM., Morales, G., & Alonso, C. (1994). The Leishmania infantum histone H3 possesses an extremely divergent N-terminal domain. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1219(2), 533–535. 10.1016/0167-4781(94)90082-5 |
| Doi | 10.1016/0167-4781(94)90082-5 |
| Publication Date | Oct 1994 |
| Publication Type | Article |
| Researcher | José María Requena Rolanía |
| Ontology | Conservation Analysis, Histone structure and regulation |
| Research Groups | Regulation of gene expression in Leishmania |
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