a conserved stem loop motif in the 5′untranslated region regulates transforming growth factor-β1 translation守恒的干细胞循环调节改变主题的5u2032端非翻译区增长factor-β1翻译.pdfVIP

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2017-09-07 发布于上海
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a conserved stem loop motif in the 5′untranslated region regulates transforming growth factor-β1 translation守恒的干细胞循环调节改变主题的5u2032端非翻译区增长factor-β1翻译.pdf

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a conserved stem loop motif in the 5′untranslated region regulates transforming growth factor-β1 translation守恒的干细胞循环调节改变主题的5u2032端非翻译区增长factor-β1翻译

A Conserved Stem Loop Motif in the 59Untranslated Region Regulates Transforming Growth Factor-b1 Translation 1 1 1 1 2 Robert H. Jenkins , Rasha Bennagi , John Martin , Aled O. Phillips , James E. Redman , Donald J. Fraser1* 1 Institute of Nephrology, School of Medicine, Cardiff University, Heath Park, Cardiff, Wales, United Kingdom, 2 School of Chemistry, Cardiff University, Park Place, Cardiff, Wales, United Kingdom Abstract Transforming growth factor- b (TGF-b ) regulates cellular proliferation, differentiation, migration, and survival. The human 1 1 TGF- b1 transcript is inherently poorly translated, and translational activation has been documented in relation to several stimuli. In this paper, we have sought to identify in cis regulatory elements within the TGF-b1 59Untranslated Region (59UTR). In silico analysis predicted formation of stable secondary structure in a G/C-rich element between nucleotides +77 to + 106, and demonstrated that this element is highly conserved across species. Circular dichroism spectroscopy confirmed the presence of secondary structure in this region. The proximal 59UTR was inhibitory to translation in reporter gene experiments, and mutation of the secondary structure motif increased translational efficiency. Translational regulation of TGF-b1 mRNA is linked to altered binding of YB-1 protein to its 59UTR. Immunoprecipitation-RT-qPCR demonstrated a high basal association of YB-1 with TGF-b1 mRNA. However, mutation of the secondary structure motif did not prevent interaction of YB-1 with the 59UTR, suggesting that YB-1 binds to