Please use this identifier to cite or link to this item: http://repositorio.cualtos.udg.mx:8080/jspui/handle/123456789/1347
Title: Recombinant Trichomonas vaginalis eIF-5A protein expressed from a eukaryotic system binds specifically to mammalian and putative trichomonal eIF-5A response elements (EREs)
Authors: Carvajal Gamez, Bertha Isabel
Vázquez Carrillo, Laura
Torres Romero, Julio César
Camacho Nuez, Minerva
Ponce Regalado, María Dolores
López Camarillo, César
Álvarez Sánchez, María Elizbeth
Keywords: trichomonas vaginalis
eukaryotic translation initiation factor 5A
TveIF-5A
polyamines
eIF-5A response elements EREs
Issue Date: Dec-2016
Publisher: Elsevier - Science Direct
Citation: Carvajal-Gamez BI, Carrillo LV, Torres-Romero JC, Camacho-Nuez M, Ponce-Regalado MD, Camarillo CL, Alvarez-Sánchez ME. Recombinant Trichomonas vaginalis eIF-5A protein expressed from a eukaryotic system binds specifically to mammalian and putative trichomonal eIF-5A response elements (EREs). Parasitol Int. 2016 Dec;65(6 Pt A):625-631. doi: 10.1016/j.parint.2016.09.004. Epub 2016 Sep 9. PMID: 27620329.
Series/Report no.: Parasitology International;Volume 65, Issue 6, Part A, December 2016, Pages 625-631
Abstract: Abstract Trichomonas vaginalis eIF-5A-like protein (TveIF-5A) belongs to the highly conserved eIF-5A family of proteins that contains a unique polyamine-derived amino acid, hypusine. Recently, we determined that the polyamine putrescine is required for tveif-5a mRNA stability, and it is necessary for stability and maturation of the TveIF-5A protein. Eukaryotic eIF-5A is known to be involved in mRNA turnover and is capable of sequence-specific RNA binding to eIF-5A response elements (EREs). These ERE sequences are present in diverse mammalian mRNAs, including human cyclooxygenase-2 ( cox-2 ). Here, we cloned the complete coding sequence of TveIF-5A and overexpressed it in a eukaryotic system. The recombinant protein (rTveIF-5A) was purified in soluble form using size-exclusion chromatography. Because of the polyamine-dependent regulation of TvCP39 (a protease of T. vaginalis ) at the protein and RNA messenger (mRNA) levels, we looked for an ERE-like structure in the 3′ region of tvcp39 mRNA. In RNA gel-shift assays, rTveIF-5A bound to transcripts at the EREs of cox-2 or tvcp39 mRNAs. This work shows the eIF-5A/ERE-like interaction in T. vaginalis .
Description: Artículo
URI: http://repositorio.cualtos.udg.mx:8080/jspui/handle/123456789/1347
ISSN: 1383-5769
Appears in Collections:3212 Artículos

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