RNA-Binding Proteins in Trichomonas vaginalis: Atypical Multifunctional Proteins
AbstractIron homeostasis is highly regulated in vertebrates through a regulatory system mediated by RNA-protein interactions between the iron regulatory proteins (IRPs) that interact with an iron responsive element (IRE) located in certain mRNAs, dubbed the IRE-IRP regulatory system. Trichomonas vaginalis, the causal agent of trichomoniasis, presents high iron dependency to regulate its growth, metabolism, and virulence properties. Although T. vaginalis lacks IRPs or proteins with aconitase activity, possesses gene expression mechanisms of iron regulation at the transcriptional and posttranscriptional levels. However, only one gene with iron regulation at the transcriptional level has been described. Recently, our research group described an iron posttranscriptional regulatory mechanism in the T. vaginalis tvcp4 and tvcp12 cysteine proteinase mRNAs. The tvcp4 and tvcp12 mRNAs have a stem-loop structure in the 5'-coding region or in the 3'-UTR, respectively that interacts with T. vaginalis multifunctional proteins HSP70, α-Actinin, and Actin under iron starvation condition, causing translation inhibition or mRNA stabilization similar to the previously characterized IRE-IRP system in eukaryotes. Herein, we summarize recent progress and shed some light on atypical RNA-binding proteins that may participate in the iron posttranscriptional regulation in T. vaginalis. View Full-Text
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Figueroa-Angulo, E.E.; Calla-Choque, J.S.; Mancilla-Olea, M.I.; Arroyo, R. RNA-Binding Proteins in Trichomonas vaginalis: Atypical Multifunctional Proteins. Biomolecules 2015, 5, 3354-3395.
Figueroa-Angulo EE, Calla-Choque JS, Mancilla-Olea MI, Arroyo R. RNA-Binding Proteins in Trichomonas vaginalis: Atypical Multifunctional Proteins. Biomolecules. 2015; 5(4):3354-3395.Chicago/Turabian Style
Figueroa-Angulo, Elisa E.; Calla-Choque, Jaeson S.; Mancilla-Olea, Maria I.; Arroyo, Rossana. 2015. "RNA-Binding Proteins in Trichomonas vaginalis: Atypical Multifunctional Proteins." Biomolecules 5, no. 4: 3354-3395.