caa a22 4500 378849611 CHVBK 20180305123320.0 cr unu---uuuuu 161128e20030127xx s 000 0 eng 10.1515/BC.2003.002 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.002 3'UTRs of Glutathione PeroxidasesDifferentially Affect Selenium-DependentmRNA Stability and SelenocysteineIncorporation Efficiency [Elektronische Daten] [C. Müller, K. Wingler, R. Brigelius-Flohé] Selenoprotein mRNAs are particular in several aspects. They contain a specific secondary structure in their 3'UTR, called Secis (selenocysteine inserting sequence), which is indispensable for selenocysteine incorporation, and they are degraded under seleniumlimiting conditions according to their ranking in the hierarchy of selenoproteins. In the familiy of seleniumdependent glutathione peroxidases (GPx) the ranking is GIGPx ≥ PHGPx> cGPx= pGPx. This phenomenon was studied by mutually combining the coding regions of GI-GPx, PHGPx and cGPx with their 3'UTRs. HepG2 cells were stably transfected with the resulting constructs. Expression of glutathione peroxidases was estimated by activity measurement and Western blotting, the selenium-dependent mRNA stability by real-time PCR. Whereas 3'UTRs from stable PHGPx and GI-GPx could be exchanged without loss of stability, they were not able to stabilize cGPx mRNA. cGPx 3'UTR rendered GI-GPx and PHGPx mRNA unstable. Thus, cGPx mRNA contains selenium-responsive instability elements in both the translated and the untranslated region, which cannot be compensated by one of the stable homologs. Stabilizing efficiency of an individual GPx 3'UTR did not correlate with the efficiency of selenocysteine incorporation. PHGPx 3'UTR was equally effective as cGPx 3'UTR in enhancing GPx activity in all constructs, while GI-GPx 3'UTR showed a markedly lower efficacy. We conclude that different mRNA sequences and/or RNA-binding proteins might regulate mRNA stability and translation of selenoprotein mRNA. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Müller C. aut Wingler K. aut Brigelius-Flohé R. aut Biological Chemistry Walter de Gruyter 384/1(2003-01-27), 11-18 1431-6730 384:1<11 2003 384 bchm https://doi.org/10.1515/BC.2003.002 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.002 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Müller C. aut NATIONALLICENCE 700 1- Wingler K. aut NATIONALLICENCE 700 1- Brigelius-Flohé R. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/1(2003-01-27), 11-18 1431-6730 384:1<11 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter