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Updated: Jul 12, 2026
11:34
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
Two structurally different RNA molecules are bound by the spliceosomal protein U1A using the same recognition
L Jovine1, C Oubridge, J M Avis
1MRC Laboratory of Molecular Biology, Cambridge, UK.
Structure (London, England : 1993)
|May 15, 1996
Summary
Human U1A protein binds to its own pre-mRNA 3' untranslated region (3'UTR), downregulating expression. A structural model reveals specific interactions and protein dimerization crucial for regulating polyadenylation.
Area of Science:
- Molecular Biology
- Structural Biology
- RNA Biology
Background:
- Human U1A protein is essential for pre-mRNA splicing via U1 small nuclear ribonucleoprotein (snRNP) formation.
- U1A protein autoregulates its expression by binding to its own 3' untranslated region (3'UTR), inhibiting polyadenylation.
- The 3'UTR contains conserved secondary structures with specific heptanucleotide sequences recognized by U1A protein.
Purpose of the Study:
- To understand the molecular control mechanism of polyadenylation.
- To build a structural model of the U1A protein-3'UTR complex.
- To elucidate the sequence-specific interactions between U1A protein and its 3'UTR.
Main Methods:
- Utilized crystal structure of U1A protein-hairpin II RNA complex.
- Developed a model of the U1A protein-3'UTR complex.
- Analyzed sequence conservation and RNA secondary structure.
Main Results:
- Identified tight binding of the AUUGCAC sequence to a groove on the U1A protein surface.
- Confirmed sequence-specific contacts between U1A protein and the 3'UTR heptanucleotide.
- Established U1A protein-3'UTR complex model based on crystal structure and RNA symmetry.
Conclusions:
- Sequence-specific interactions involve the conserved heptanucleotide and the terminal C:G base pair.
- Protein-protein contacts and electrostatic interactions stabilize the complex.
- RNA binding induces conformational changes leading to U1A dimerization, inhibiting poly(A) polymerase and preventing autoregulation.
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