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Article

Investigation of a conserved stacking interaction in target site recognition by the U1A protein.

Nucleic acids research - 15 Jan 2002

Shiels Jerome C, Tuite Jacob B, Nolan Scott J, Baranger Anne M

Abstract excerpt

Three highly conserved aromatic residues in RNA recognition motifs (RRM) participate in stacking interactions with RNA bases upon binding RNA. We have investigated the contribution of one of these aromatic residues, Phe56, to the complex formed between the N-terminal RRM of the spliceosomal protein U1A and stem-loop 2 of U1 snRNA. Previous work showed that the aromatic group is important for high affinity...

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Identifiers

PMID: 11788718
DOI: 10.1093/nar/30.2.550
PMCID: PMC99821

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Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Investigation of a conserved stacking interaction in target site recognition by the U1A protein.PMID 11788718Read ↗

Design of an adenosine analogue that selectively improves the affinity of a mutant U1A protein for RNA.Semantic proximity Read ↗

Substitution of an essential adenine in the U1A-RNA complex with a non-polar isostere.Semantic proximity Read ↗

Molecular dynamics and thermodynamics of protein-RNA interactions: mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex.Semantic proximity Read ↗

U1A protein-stem loop 2 RNA recognition: prediction of structural differences from protein mutations.Semantic proximity Read ↗

Structural requirements for protein-catalyzed annealing of U4 and U6 RNAs during di-snRNP assembly.Semantic proximity Read ↗

Sequences upstream of the branch site are required to form helix II between U2 and U6 snRNA in a trans-splicing reaction.Semantic proximity Read ↗

Multiple roles for U6 snRNA in the splicing pathway.Semantic proximity Read ↗

Determinants within an 18-amino-acid U1A autoregulatory domain that uncouple cooperative RNA binding, inhibition of polyadenylation, and homodimerization.Semantic proximity Read ↗

The role of positively charged amino acids and electrostatic interactions in the complex of U1A protein and U1 hairpin II RNA.Semantic proximity Read ↗

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The role of the C-terminal helix of U1A protein in the interaction with U1hpII RNA.Semantic proximity Read ↗

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