Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Molecular characterization of the histone H2A gene from the parasite Trypanosoma rangeli

  • 41 Accesses

  • 6 Citations

Abstract

The sequence, genomic organization, and transcription of the gene encoding the H2A histone protein of the protozoan parasite Trypanosoma rangeli is described in this paper. The locus encoding the T. rangeli H2A protein is formed by at least 11 gene units measuring 790 nucleotides in length, organized in tandem, and located in a single chromosome of approximately 1.9 Mb. The gene units actively transcribe only one size class of mRNA measuring 0.7 kb in length. The T. rangeli H2A protein contains in the amino-terminal the AGLXFPV motif, which is conserved in a broad range of H2A proteins, and the RSAK motif, which is implicated in repression of the histone's basal transcription in yeast. The carboxyl-terminal of the protein contains a two-lysine residue described as the ubiquitin binding site and the histidine residue implicated in DNA binding.

This is a preview of subscription content, log in to check access.

Author information

Additional information

Received: 17 May 2000 / Accepted: 18 May 2000

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Puerta, C., Cuervo, P., Thomas, M. et al. Molecular characterization of the histone H2A gene from the parasite Trypanosoma rangeli . Parasitol Res 86, 916–922 (2000). https://doi.org/10.1007/s004360000270

Download citation

Keywords

  • Histidine
  • Size Class
  • Molecular Characterization
  • Genomic Organization
  • Trypanosoma