Evidence map›Paper›PMID 9482748›Full record

ArticleThe EMBO journal1998

Comparative photocross-linking analysis of the tertiary structures of Escherichia coli and Bacillus subtilis RNase P RNAs.

J L Chen, J M Nolan, M E Harris, N R Pace

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 114 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Solution structure of RNase P RNA.RNA (New York, N.Y.) · 2011
    Article
  5. Predicting and modeling RNA architecture.Cold Spring Harbor perspectives in biology · 2011
    Review
  6. Review
  7. RNA crosslinking methods.Methods in enzymology · 2009
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Crystal structure of a bacterial ribonuclease P RNA.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 1 institution in 1 country.

J L ChenDepartments Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley, CA 94720-3102, USA.
J M Nolan
M E Harris
N R Pace
University of California, Berkeley · US

Funding

METABOLISM OF RNA IN PROKARYOTES AND EUKARYOTESR01GM034527 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI PACE, NORMAN R · 1985 to 2011
$2.6M
FUNCTION AND METABOLISM OF RNAR37GM034527 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI PACE, NORMAN R · 1993 to 2003
$1.8M
NIGMS NIH HHS GM34527NIGMS NIH HHS R01 GM034527
6 · The paper itself

Abstract

Bacterial ribonuclease P contains a catalytic RNA subunit that cleaves precursor sequences from the 5' ends of pre-tRNAs. The RNase P RNAs from Bacillus subtilis and Escherichia coli each contain several unique secondary structural elements not present in the other. To understand better how these phylogenetically variable elements affect the global architecture of the ribozyme, photoaffinity cross-linking studies were carried out. Photolysis of photoagents attached at homologous sites in the two RNAs results in nearly identical cross-linking patterns, consistent with the homology of the RNAs and indicating that these RNAs contain a common, core tertiary structure. Distance constraints were used to derive tertiary structure models using a molecular mechanics-based modeling protocol. The resulting superimposition of large sets of equivalent models provides a low resolution (5-10 A) structure for each RNA. Comparison of these structure models shows that the conserved core helices occupy similar positions in space. Variably present helical elements that may play a role in global structural stability are found at the periphery of the core structure. The P5.1 and P15.1 helical elements, unique to the B.subtilis RNase P RNA, and the P6/16/17 helices, unique to the E.coli RNA, occupy similar positions in the structure models and, therefore, may have analogous structural function.

Indexed as

Escherichia coli ProteinsNucleic Acid ConformationAzidesBacillus subtilisBase SequenceComputer SimulationCross-Linking ReagentsEndoribonucleasesEscherichia coliModels, MolecularMolecular Sequence DataPhotolysisRibonuclease PRNA, BacterialRNA, Catalytic4-azidophenacyl bromideAzidesCross-Linking ReagentsEndoribonucleasesEscherichia coli ProteinsRibonuclease Pribonuclease P, E coliRNA, BacterialRNA, Catalytic

Identifiers

PMID9482748
PMCPMC1170499
OpenAlexW2093499822

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.