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Nucleic Acids Research Advance Access first published online on September 18, 2006
This version published online on October 5, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl666
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© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Binding of human SLBP on the 3'-UTR of histone precursor H4-12 mRNA induces structural rearrangements that enable U7 snRNA anchoring

Sophie Jaeger, Franck Martin, Joëlle Rudinger-Thirion, Richard Giegé and Gilbert Eriani*

UPR 9002 ‘Architecture et Réactivité des ARN’ du CNRS, Université Louis Pasteur, Institut de Biologie Moléculaire et Cellulaire 15 rue René Descartes, F-67084 Strasbourg cedex, France

*To whom correspondence should be addressed: Tel: +33 3 88 41 70 42; Fax: +33 3 88 60 22 18; Email: g.eriani{at}ibmc.u-strasbg.fr

Received July 19, 2006. Revised August 28, 2006. Accepted August 29, 2006.

In metazoans, cell-cycle-dependent histones are produced from poly(A)-lacking mRNAs. The 3' end of histone mRNAs is formed by an endonucleolytic cleavage of longer precursors between a conserved stem–loop structure and a purine-rich histone downstream element (HDE). The cleavage requires at least two trans-acting factors: the stem–loop binding protein (SLBP), which binds to the stem–loop and the U7 snRNP, which anchors to histone pre-mRNAs by annealing to the HDE. Using RNA structure-probing techniques, we determined the secondary structure of the 3'-untranslated region (3'-UTR) of mouse histone pre-mRNAs H4–12, H1t and H2a–614. Surprisingly, the HDE is embedded in hairpin structures and is therefore not easily accessible for U7 snRNP anchoring. Probing of the 3'-UTR in complex with SLBP revealed structural rearrangements leading to an overall opening of the structure especially at the level of the HDE. Electrophoretic mobility shift assays demonstrated that the SLBP-induced opening of HDE actually facilitates U7 snRNA anchoring on the histone H4–12 pre-mRNAs 3' end. These results suggest that initial binding of the SLBP functions in making the HDE more accessible for U7 snRNA anchoring.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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