Interaction of small ribosomal and transfer RNAs with a protein from Leishmania donovani.
AUTOR(ES)
Ghosh, A
RESUMO
Using synthetic antisense RNA from the 5'-untranslated region of the beta-tubulin gene as probe in gel retardation assays, a heat stable RNA-binding factor was identified in promastigotes of the kinetoplastid protozoan Leishmania donovani. The same or similar factors interact with several small ribosomal RNA (srRNA) species and, more weakly, with tRNA, as shown by binding and competition experiments. Deletion analysis indicated involvement of repeated purine-rich motifs on the antisense RNA, in the reaction. Related, conserved motifs occur on at least two of the srRNAs. By a modified Western blot assay, the RNA-binding species was identified as a single, small polypeptide. The activity is apparently specific for the promastigote stage of the parasite, being undetectable in amastigotes. The properties of this RNA-binding factor suggest that it is a novel, previously uncharacterized protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=308046Documentos Relacionados
- Purification and characterization of an 80-kilodalton membrane protein from Leishmania donovani.
- Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani.
- Functional expression of a myo-inositol/H+ symporter from Leishmania donovani.
- Antileishmanial activity of licochalcone A in mice infected with Leishmania major and in hamsters infected with Leishmania donovani.
- Genetic analysis of nucleoside transport in Leishmania donovani.