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• W2155456424 startingPage "146" @default.
• W2155456424 abstract "Noncoding sequences regulate the function of mRNA and and DNA. In animal mRNAs, iron responsive elements (IREs) regulate the synthesis of proteins for iron storage, uptake and red cell heme formation. Folding of the IRE was indicated previously by reactivity with chemical and enzymatic probes. 1 H- and 31 P-NMR s ectra now confirm the IRE folding; an atypical 31 P-spectrum, differential accessibility of imino protons to solvents, multiple long-range NOES and heat stable subdomains were observed. Biphasic hyperchromic transitions occurred (52 and 73°C). A G-C base pair occurs in the hairpin loop (HL) (based on dimethylsulfate, RNAase T 1 previously used, and changes in NMR imino proton resonances typical of G-C base pairs after G/A substitution). Mutation of the hairpin loop also decreased temperature stability and changed the 31 P-NMR spectrum; regulation and protein (IRP) binding were previously shown to change. Alteration of IRE structure shown by NMR spectroscopy, occurred at temperatures used in studies of IRE function, explaining loss of IRP binding. The effect of the HL mutation on the IRE emphasizes the importance of HL structure in other mRNAs, viral RNAs (e.g. HIV-TAR), and ribozymes." @default.
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• W2155456424 date "1995-01-01" @default.
• W2155456424 modified "2023-10-03" @default.
• W2155456424 title "The importance of a single G in the hairpin loop of the iron responsive element (IRE) in ferritin mRNA for structure: an NMR spectroscopy study" @default.
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• W2155456424 doi "https://doi.org/10.1093/nar/23.1.146" @default.
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