scholarly journals Corrigendum to “α-Actinin TvACTN3 ofTrichomonas vaginalisIs an RNA-Binding Protein That Could Participate in Its Posttranscriptional Iron Regulatory Mechanism”

2016 ◽  
Vol 2016 ◽  
pp. 1-2
Author(s):  
Jaeson Santos Calla-Choque ◽  
Elisa Elvira Figueroa-Angulo ◽  
Leticia Ávila-González ◽  
Rossana Arroyo
2014 ◽  
Vol 2014 ◽  
pp. 1-20 ◽  
Author(s):  
Jaeson Santos Calla-Choque ◽  
Elisa Elvira Figueroa-Angulo ◽  
Leticia Ávila-González ◽  
Rossana Arroyo

Trichomonas vaginalisis a sexually transmitted flagellated protist parasite responsible for trichomoniasis. This parasite is dependent on high levels of iron, favoring its growth and multiplication. Iron also differentially regulates some trichomonad virulence properties by unknown mechanisms. However, there is evidence to support the existence of gene regulatory mechanisms at the transcriptional and posttranscriptional levels that are mediated by iron concentration inT. vaginalis. Thus, the goal of this study was to identify an RNA-binding protein inT. vaginalisthat interacts with the tvcp4 RNA stem-loop structure, which may participate in a posttranscriptional iron regulatory mechanism mediated by RNA-protein interactions. We performed RNA electrophoretic mobility shift assay (REMSA) and supershift, UV cross-linking, Northwestern blot, and western blot (WB) assays using cytoplasmic protein extracts fromT. vaginaliswith the tvcp4 RNA hairpin structure as a probe. We identified a 135-kDa protein isolated by the UV cross-linking assays asα-actinin 3 (TvACTN3) by MALDI-TOF-MS that was confirmed by LS-MS/MS andde novosequencing. TvACTN3 is a cytoplasmic protein that specifically binds to hairpin RNA structures from trichomonads and humans when the parasites are grown under iron-depleted conditions. Thus, TvACTN3 could participate in the regulation of gene expression by iron inT. vaginalisthrough a parallel posttranscriptional mechanism similar to that of the IRE/IRP system.


2020 ◽  
Vol 11 (9) ◽  
Author(s):  
Wei Xin ◽  
Min Zhang ◽  
Yang Yu ◽  
Songlin Li ◽  
Cui Ma ◽  
...  

Abstract Abnormal functional changes in pulmonary artery smooth muscle cells are the main causes of many lung diseases. Among, autophagy plays a crucial role. However, the specific molecular regulatory mechanism of autophagy in PASMCs remains unclear. Here, we first demonstrate that BCAT1 played a key role in the autophagy of hypoxic PASMCs and hypoxic model rats. BCAT1-induced activation and accumulation of the autophagy signaling proteins BECN1 and Atg5 by the endoplasmic reticulum (ER) stress pathway. Interestingly, we discovered that BCAT1 bound IRE1 on the ER to activate expression of its downstream pathway XBP-1-RIDD axis to activate autophagy. More importantly, we identified an RNA-binding protein, zinc finger protein 423, which promoted autophagy by binding adenylate/uridylate (AU)-rich elements in the BCAT1 mRNA 3′-untranslated region. Overall, our results identify BCAT1 as a potential therapeutic target for the clinical treatment of lung diseases and reveal a novel posttranscriptional regulatory mechanism and signaling pathway in hypoxia-induced PASMC autophagy.


2007 ◽  
Vol 177 (4S) ◽  
pp. 78-79
Author(s):  
Lioudmila Sitnikova ◽  
Gary Mendese ◽  
Qin Lui ◽  
Bruce A. Woda ◽  
Di Lu ◽  
...  

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