CoChat
Sign Up
Cited by 234RNA Research and SplicingRNA and protein synthesis mechanismsRNA regulation and disease

Structural basis for recognition of AU-rich element RNA by the HuD protein.

Xiaoqiang Wang, Traci M. Tanaka Hall·2001·Nature Structural Biology
DOI 10.1038/84131
Open this paper in CoChat — free account

Abstract

Hu proteins bind to adenosine-uridine (AU)-rich elements (AREs) in the 3' untranslated regions of many short-lived mRNAs, thereby stabilizing them. Here we report the crystal structures of the first two RNA recognition motif (RRM) domains of the HuD protein in complex with an 11-nucleotide fragment of a class I ARE (the c-fos ARE; to 1.8 A), and with an 11-nucleotide fragment of a class II ARE (the tumor necrosis factor alpha ARE; to 2.3 A). These structures reveal a consensus RNA recognition sequence that suggests a preference for pyrimidine-rich sequences and a requirement for a central uracil residue in the clustered AUUUA repeats found in class II AREs. Comparison to structures of other RRM domain-nucleic acid complexes reveals two base recognition pockets in all the structures that interact with bases using residues in conserved ribonucleoprotein motifs and at the C-terminal ends of RRM domains. Different conformations of nucleic acid can be bound by RRM domains by using different combinations of base recognition pockets and multiple RRM domains.

Integrity signals

Registry

Crossref · 10.1038/84131

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The amino acid residues interacting with RNA nucleotides are well conserved among all Hu proteins and the Drosophila ELAV protein.

    “This report also showed that the amino acid residues interacting with RNA nucleotides are well conserved among all Hu proteins and the Drosophila ELAV protein.”

    From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Wang and Tanaka Hall 2001

  • The crystal structure of HuD bound to c-fos or TNFα mRNAs illustrates that specific residues within its first two RRMs preferentially bind the pyrimidine-rich X-U/C-U-X-X-U/C?-U-U/C consensus sequence.

    “The crystal structure of HuD bound to c-fos or tumor necrosis factor α (TNFα) mRNAs illustrates that specific residues within its first two RRMs preferentially bind the pyrimidine-rich X-U/C-U-X-X-U/C?-U-U/C consensus sequence where the “?” denotes ambiguity whether a cytosine in this position is tolerated (Wang and Tanaka Hall 2001).”

    From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Wang and Tanaka Hall 2001

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Wang, X., & Hall, T. M. T.
Affiliations
National Institutes of Health (US)
Corresponding author
Traci M. Tanaka Hall
ORCID
Venue
Nature Structural Biology
Publisher
Springer Science and Business Media LLC
Published
2001-02-01
Volume
8
Issue
2
Pages
141-145
ISSN
1072-8368 (ISSN-L)
DOI
10.1038/84131
OpenAlex
W1864265177
Cited by
234
References
1
Citations by year
2026: 6 · 2025: 8 · 2024: 4 · 2023: 4 · 2022: 9 · 2021: 8 · 2020: 3 · 2019: 6 · 2018: 7 · 2017: 7 · 2016: 1 · 2015: 8 · 2014: 5 · 2013: 10 · 2012: 16
FWCI
4.31
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Structural Biology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
Keywords
AU-rich elements, RNA recognition motif, RRM domain, protein-RNA complex, mRNA stability, 3' untranslated region
MeSH terms
ELAV-Like Protein 4, Amino Acid Sequence, Binding Sites, Humans, Models, Molecular, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, RNA, Messenger, Substrate Specificity, Tumor Necrosis Factor-alpha, Consensus Sequence, Sequence Alignment, RNA-Binding Proteins, Proto-Oncogene Proteins c-fos, Protein Structure, Tertiary, Crystallography, X-Ray, Response Elements, AT Rich Sequence, RNA Stability, Drosophila Proteins, ELAV Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review