Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA.

doi:10.1073/pnas.87.16.6393

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Article

Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA.

Proceedings of the National Academy of Sciences of the United States of America - 1 Aug 1990

Lutz-Freyermuth C, Query C C, Keene J D

Abstract excerpt

Many RNA-associated proteins contain a ribonucleoprotein (RNP) consensus octamer encompassed by a conserved 80 amino acid sequence, which we have termed an RNA recognition motif (RRM). RRM family members contain either one (class I) or multiple (class II) copies of this motif. We report here that a class II component of the U1 small nuclear RNP (snRNP), the A protein of U1 snRNP (U1snRNP-A), contains two RRMs...

Topics

Binding Sites
Electrophoresis, Polyacrylamide Gel
Epitopes
Gene Library
HeLa Cells
Humans
Kinetics
Macromolecular Substances
Mutation
Nucleic Acid Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligonucleotide Probes

Protein Biosynthesis

RNA, Small Nuclear

Ribonucleoproteins

Ribonucleoproteins, Small Nuclear

Transcription, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 1696729
DOI: 10.1073/pnas.87.16.6393
PMCID: PMC54540

Genes

RRM1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1696729-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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