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

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2000
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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.
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Authors Puerta, C;Cuervo, P;Thomas, M C;Lopez, M C;
Journal parasitology research
Year 2000
DOI DOI not found
URL URL not found
Keywords
pichia pastoris high-level expression methanol codon optimization staphylokinase specific activity

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