Recombinant Trichomonas vaginalis eIF-5A protein expressed from a eukaryotic system binds specifically to mammalian and putative trichomonal eIF-5A response elements (EREs)

dc.creatorCarvajal Gamez, Bertha Isabel
dc.creatorVázquez Carrillo, Laura
dc.creatorTorres Romero, Julio César
dc.creatorCamacho Nuez, Minerva
dc.creatorPonce Regalado, María Dolores
dc.creatorLópez Camarillo, César
dc.creatorÁlvarez Sánchez, María Elizbeth
dc.date2022-06-20T18:25:20Z
dc.date2022-06-20T18:25:20Z
dc.date2016-12
dc.date.accessioned2023-07-21T21:45:23Z
dc.date.available2023-07-21T21:45:23Z
dc.identifierCarvajal-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.
dc.identifier1383-5769
dc.identifierDOI: 10.1016/j.parint.2016.09.004
dc.identifierPMID: 27620329
dc.identifierhttp://repositorio.cualtos.udg.mx:8080/jspui/handle/123456789/1347
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7752821
dc.descriptionArtículo
dc.descriptionAbstract 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 .
dc.languageen
dc.publisherElsevier - Science Direct
dc.relationParasitology International;Volume 65, Issue 6, Part A, December 2016, Pages 625-631
dc.subjecttrichomonas vaginalis
dc.subjecteukaryotic translation initiation factor 5A
dc.subjectTveIF-5A
dc.subjectpolyamines
dc.subjecteIF-5A response elements EREs
dc.titleRecombinant Trichomonas vaginalis eIF-5A protein expressed from a eukaryotic system binds specifically to mammalian and putative trichomonal eIF-5A response elements (EREs)
dc.typeArticle


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