TY - JOUR
T1 - Molecular characterization of the histone H2A gene from the parasite Trypanosoma rangeli
AU - Puerta, C.
AU - Cuervo, P.
AU - Thomas, M. C.
AU - Lopez, M. C.
N1 - Funding Information:
Acknowledgements We thank Drs. S. Nicholls and M. Montilla for providing the D. marsupialis No. 3 and C-23 strains. This research received financial support from the Programa de Cooperación Cientṍ fica con Iberoamérica-MEC, Spain; the Fundación para la Promoción de la Ciencia y la Tecnologṍ a. Banco de la Republica de Colombia; and the CSIC (Spain)-COLCIENCIAS (Colombia) convenio de cooperación. Dr. M.C. Thomas was supported by FIS no ref 97/4207. The authors declare that the experiments comply with the current laws of the country in which they were performed.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033745634&partnerID=8YFLogxK
U2 - 10.1007/s004360000270
DO - 10.1007/s004360000270
M3 - Article
C2 - 11097300
AN - SCOPUS:0033745634
SN - 0932-0113
VL - 86
SP - 916
EP - 922
JO - Parasitology Research
JF - Parasitology Research
IS - 11
ER -
