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Updated: Jul 11, 2026

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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
PLAUF binding to the 3'UTR of the H3.3 histone transcript affects mRNA stability.
G Pulcrano1, R Leonardo, M Piscopo
1Department of Structural and Functional Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia, Naples, Italy.
Gene
|September 11, 2007
Summary
The P. lividus sea urchin H3.3 histone mRNA
Area of Science:
- Molecular Biology
- Gene Regulation
- Marine Biology
Background:
- The H3.3 histone variant mRNA in P. lividus sea urchins possesses a lengthy 3' untranslated region (3'UTR).
- This 3'UTR contains AU-Rich Element (ARE) motifs, known regulators of mRNA stability.
Purpose of the Study:
- To investigate the role of the H3.3 mRNA 3'UTR in transcript degradation.
- To identify proteins that bind to the H3.3 3'UTR and determine their function in mRNA stability.
Main Methods:
- RNA stability assays using chimeric transcripts in rabbit reticulocyte lysate.
- Identification of RNA-binding proteins via Western blot and supershift assays.
- In vitro binding assays with recombinant proteins and in situ hybridization.
Main Results:
- The H3.3 3'UTR significantly affects mRNA degradation rates.
- A protein, PLAUF (similar to AUF1), was identified as a specific binder to the H3.3 3'UTR.
- Recombinant PLAUF binds the H3.3 3'UTR and impacts transcript half-life in vitro.
- PLAUF and H3.3 histone mRNAs show co-localization in developing embryos.
Conclusions:
- PLAUF binds the H3.3 histone mRNA 3'UTR in vivo.
- PLAUF likely plays a role in regulating H3.3 mRNA stability during development.
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