Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha

Horjales, Sofía; Cota, Germán; Señorale-Pose, Mario; Rovira, Carlos; Román, Estela; Artagaveytia, Nora; Ehrlich, Ricardo; Marı́n, Mónica

doi:10.1016/j.abb.2007.07.029

Cited by 13 publications

(13 citation statements)

References 23 publications

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“…The G-quadruplex formed by the QFP sequence might cause the production of the short hERα by inducing an mRNA surveillance mechanism termed no-go mRNA decay, which was recently discovered in yeast and is thought to be caused by an artificially introduced stable duplex (41,42). A previous study demonstrated that the hERα translated in vitro using rabbit reticulocyte and wheat germ extracts exhibited different properties against proteolysis by chymotrypsin (43). This observation suggests an alternative possibility that the production of the short hERα might due to the proteolysis of the full-length product.…”

Section: Resultsmentioning

confidence: 99%

Stability of RNA quadruplex in open reading frame determines proteolysis of human estrogen receptor α

Endoh

Kawasaki

Sugimoto

2013

Nucleic Acids Research

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mRNAs encodes not only information that determines amino acid sequences but also additional layers of information that regulate the translational processes. Notably, translational halt at specific position caused by rare codons or stable RNA structures is one of the potential factors regulating the protein expressions and structures. In this study, a quadruplex-forming potential (QFP) sequence derived from an open reading frame of human estrogen receptor α (hERα) mRNA was revealed to form parallel G-quadruplex and halt the translation elongation in vitro. Moreover, when the full-length hERα and variants containing synonymous mutations in the QFP sequence were expressed in cells, translation products cleaved at specific site were observed in quantities dependent on the thermodynamic stability of the G-quadruplexes. These results suggest that the G-quadruplex formation in the coding region of the hERα mRNA impacts folding and proteolysis of hERα protein by slowing down or temporarily stalling the translation elongation.

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Section: Resultsmentioning

confidence: 99%

Stability of RNA quadruplex in open reading frame determines proteolysis of human estrogen receptor α

Endoh

Kawasaki

Sugimoto

2013

Nucleic Acids Research

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“…[35][36][37] The influence of translational processes on protein folding has been amply debated, and a recent study suggests its influence on the relative abundance of some proteins, including CAT. 35,38 These peculiarities may be related to the different expression behavior of these proteins in the strains we have tested. We propose that the change in the stability of the ribosome is probably the main difference between the MC1061 and the other strains that permit the proper expression of our fused proteins, but more experiments are needed to corroborate this hypothesis.…”

Section: Discussionmentioning

confidence: 95%

Protein Design through Systematic Catalytic Loop Exchange in the (β/α)8 Fold

Ochoa-Leyva

Soberón

Sánchez

et al. 2009

Journal of Molecular Biology

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“…In comparison to the transcript, the level of ESR1 is lower in the proximal segment when compared to the corpus and cauda epididymidis. ESR1 is detected as two isoforms: a major band at 66 kDa, and a minor band at 31 kDa [47]. These two isoforms exhibit a minimum level of expression in the caput region, which contrasts with the transcript distribution.…”

Section: Discussionmentioning

confidence: 97%

“…As previously described, ESR1 is revealed as a band at 66 kDa [46], together with a secondary band at 31 kDa generated by protein degradation [47]. ESR1 was detected in the three epididymal segments from normal men, with a maximum level in corpus and a minimum detection in caput epididymidis.…”

Section: Quantitative Rt-pcr and Western Blot Validations Of Selectedmentioning

confidence: 98%

Effects of Vasectomy on Gene Expression Profiling along the Human Epididymis1

Thimon¹,

Calvo²,

Koukoui³

et al. 2008

Biology of Reproduction

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Worldwide, almost 100 million men rely on vasectomy for male contraceptive purposes. Due to changes in their personal lives, an increasing number of these men request surgical vasectomy reversal. Unfortunately, a significant proportion of these men remain infertile, despite the reestablishment of patent ducts, possibly due to epididymal damage caused by vasectomy. In animal models, vasectomy affects different epididymal physiological and biochemical parameters. However, the consequences of vasectomy on epididymal function are poorly understood. Furthermore, results obtained with animal models cannot be extrapolated to humans to understand the consequences of vasectomy on epididymal function. Gene expression along the epididymis is highly regulated. We previously showed that the human epididymal expression pattern of two genes is altered after vasectomy. To complete the list of epididymal genes affected by vasectomy, we analyzed the epididymal gene expression pattern of three vasectomized donors using the Affymetrix human GeneChip U133 Plus 2. These results were compared with the gene expression pattern of three "normal" donors. The data generated allowed the identification of many human epididymal genes for which expression is modified after vasectomy. Quantitative (Qt)-PCR and Western blot analysis of six selected genes known to be expressed in specific epididymal segments were performed. The Qt-PCR results confirmed the selected transcripts expression pattern deduced from microarray data. However, Western blot analysis revealed some differences in protein distribution along the epididymis when compared with the encoding transcripts expression pattern. These results contribute to an understanding of the reasons why fertility is not recovered in vasovasostomized men, even though spermogram values suggest surgical success of vasectomy reversal.

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Translational machinery and protein folding: Evidence of conformational variants of the estrogen receptor alpha

Cited by 13 publications

References 23 publications

Stability of RNA quadruplex in open reading frame determines proteolysis of human estrogen receptor α

Stability of RNA quadruplex in open reading frame determines proteolysis of human estrogen receptor α

Protein Design through Systematic Catalytic Loop Exchange in the (β/α)8 Fold

Effects of Vasectomy on Gene Expression Profiling along the Human Epididymis1

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