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Biochem Biophys Res Commun. 2012 Oct 5;426(4):539-43. doi: 10.1016/j.bbrc.2012.08.123. Epub 2012 Sep 7.

CUG binding protein 1 binds to a specific region within the human albumin 3' untranslated region.

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Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.


3' Untranslated regions (3'UTRs) of messenger RNAs have important roles in post-transcriptional regulation of gene expression and this is partly achieved through binding of specific proteins to sequences or structures within these regions. Previously, replacement of a native luciferase 3'UTR with the human albumin 3'UTR has been found to lead to a 10-fold increase in luciferase reporter activity. In this work we investigated protein binding to the human albumin 3'UTR. Electrophoretic mobility shift and UV cross-linking assays indicate that a ∼50kDa protein from Chinese Hamster Ovary (CHO) cells binds to the albumin 3'UTR, and affinity experiments followed by proteomics identified this protein as CUG binding protein 1 (CUG-BP1, also known as CELF1). Deletion analysis of the albumin 3'UTR showed that nucleotides 1-50 and nucleotides 101-150 are not required for binding but that removal of nucleotides 51-100 caused a loss in binding. The results suggest that CUG-BP1 binds to nucleotides 51-100 of the human albumin 3'UTR. In human cells CUG-BP1 binding may thus play a role in regulation of albumin expression and, additionally, it may have a function in post-transcriptional control in CHO cells.

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