Evidence map›Paper›PMID 9671049›Full record

ArticleRNA (New York, N.Y.)1998

Binding of the 60-kDa Ro autoantigen to Y RNAs: evidence for recognition in the major groove of a conserved helix.

C D Green, K S Long, H Shi, S L Wolin

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
1.4field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

48 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Y RNAs: Biogenesis, Function and Implications for the Cardiovascular System.Advances in experimental medicine and biology · 2020
    Review
  13. The vault RNA ofThe Journal of biological chemistry · 2019
    Article
  14. Ro60 and Y RNAs: structure, functions, and roles in autoimmunity.Critical reviews in biochemistry and molecular biology · 2019
    Review
  15. Structural Basis for tRNA Mimicry by a Bacterial Y RNA.Structure (London, England : 1993) · 2018
    Article
  16. Review
  17. Review
  18. RAIN: RNA-protein Association and Interaction Networks.Database : the journal of biological databases and curation · 2017
    Article
  19. Functional roles of non-coding Y RNAs.The international journal of biochemistry & cell biology · 2015
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

C D GreenDepartment of Cell Biology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
K S Long
H Shi
S L Wolin
Howard Hughes Medical Institute · USSepragen Corporation (United States) · US

Funding

Biogenesis of Small RNAsR01GM048410 · NIGMS · YALE UNIVERSITY · PI WOLIN, SANDRA L. · 1998 to 2009
$2.2M
NIGMS NIH HHS R01 GM048410
6 · The paper itself

Abstract

The 60-kDa Ro autoantigen is normally complexed with small cytoplasmic RNAs known as Y RNAs. In Xenopus oocytes, the Ro protein is also complexed with a large class of variant 5S rRNA precursors that are folded incorrectly. Using purified baculovirus-expressed protein, we show that the 60-kDa Ro protein binds directly to both Y RNAs and misfolded 5S rRNA precursors. To understand how the protein recognizes these two distinct classes of RNAs, we investigated the features of Y RNA sequence and structure that are necessary for protein recognition. We identified a truncated Y RNA that is stably bound by the 60-kDa Ro protein. Within this 39-nt RNA is a conserved helix that is proposed to be the binding site for the Ro protein. Mutagenesis of this minimal Y RNA revealed that binding by the 60-kDa Ro protein requires specific base pairs within the conserved helix, a singly bulged nucleotide that disrupts the helix, and a three-nucleotide bulge on the opposing strand. Chemical probing experiments using diethyl pyrocarbonate demonstrated that, in the presence of the two bulges, the major groove of the conserved helix is accessible to protein side chains. These data are consistent with a model in which the Ro protein recognizes specific base pairs in the conserved helix by binding in the major groove of the RNA. Furthermore, experiments in which dimethyl sulfate was used to probe a naked and protein-bound Y RNA revealed that a structural alteration occurs in the RNA upon Ro protein binding.

Indexed as

AnimalsAutoantigensBase SequenceBinding SitesConserved SequenceMolecular ProbesMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingRecombinant ProteinsRibonucleoproteinsRNARNA, Small CytoplasmicSequence DeletionSS-A AntigenAutoantigensMolecular ProbesRecombinant ProteinsRibonucleoproteinsRNARNA, Small CytoplasmicRO60 protein, humanSS-A Antigen

Identifiers

PMID9671049
PMCPMC1369656
OpenAlexW2150392192

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.