Evidence map›Paper›PMID 12166648›Full record

ArticleRNA (New York, N.Y.)2002

Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P.

Sharon M Crary, Jeffrey C Kurz, Carol A Fierke

Open access · greenAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 56 citations in OpenAlex.

  1. Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Coevolution of RNase P and the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. NMR and XAS reveal an inner-sphere metal binding site in the P4 helix of the metallo-ribozyme ribonuclease P.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

3 authors at 3 institutions in 1 country.

Sharon M CraryBiochemistry Department, Duke University Medical Center, Durham, North Carolina 27710, USA.
Jeffrey C Kurz
Carol A Fierke
Archemix (United States) · USDuke Medical Center · USDuke University Hospital · US

Funding

ENZYMOLOGY OF RNA PROCESSING ENZYMESR01GM055387 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FIERKE, CAROL A · 1997 to 2014
$4.3M
Structural Biology and Biphysics Training ProgramT32GM008487 · NIGMS · DUKE UNIVERSITY · PI OAS, TERRENCE GILBERT · 1994 to 2014
$2.9M
CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008558 · NIGMS · DUKE UNIVERSITY · PI PIRRUNG, MICHAEL C · 1994 to 2003
$1.2M
NIGMS NIH HHS GM08487NIGMS NIH HHS GM08558NIGMS NIH HHS GM55387NIGMS NIH HHS R01 GM055387
6 · The paper itself

Abstract

Ribonuclease P (RNase P) is a ribonucleoprotein that requires magnesium ions to catalyze the 5' maturation of transfer RNA. To identify interactions essential for catalysis, the properties of RNase P containing single sulfur substitutions for nonbridging phosphodiester oxygens in helix P4 of Bacillus subtilis RNase P were analyzed using transient kinetic experiments. Sulfur substitution at the nonbridging oxygens of the phosphodiester bond of nucleotide U51 only modestly affects catalysis. However, phosphorothioate substitutions at A49 and G50 decrease the cleavage rate constant enormously (300-4,000-fold for P RNA and 500-15,000-fold for RNase P holoenzyme) in magnesium without affecting the affinity of pre-tRNA(Asp), highlighting the importance of this region for catalysis. Furthermore, addition of manganese enhances pre-tRNA cleavage catalyzed by B. subtilis RNase P RNA containing an Sp phosphorothioate modification at A49, as observed for Escherichia coli P RNA [Christian et al., RNA, 2000, 6:511-519], suggesting that an essential metal ion may be coordinated at this site. In contrast, no manganese rescue is observed for the A49 Sp phosphorothioate modification in RNase P holoenzyme. These differential manganese rescue effects, along with affinity cleavage, suggest that the protein component may interact with a metal ion bound near A49 in helix P4 of P RNA.

Indexed as

Escherichia coli ProteinsBacillus subtilisBase SequenceCatalytic DomainEndoribonucleasesHoloenzymesKineticsMetalsModels, MolecularMolecular Sequence DataNucleic Acid ConformationRibonuclease PRNA, BacterialRNA, CatalyticThionucleotidesEndoribonucleasesEscherichia coli ProteinsHoloenzymesMetalsRibonuclease Pribonuclease P, E coliRNA, BacterialRNA, CatalyticThionucleotides

Identifiers

PMID12166648
PMCPMC1370310
OpenAlexW2170202924

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.