Evidence map›Paper›PMID 17194721›Full record

ArticleRNA (New York, N.Y.)2007

Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation.

Melissa M Getz, Andy J Andrews, Carol A Fierke, Hashim M Al-Hashimi

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  9. Article
  10. Review
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  12. Article
  13. Hierarchy of RNA functional dynamics.Annual review of biochemistry · 2014
    Review
  14. NMR studies of nucleic acid dynamics.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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
  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.

Melissa M GetzDepartment of Chemistry, University of Michigan, Ann Arbor 48109, USA.
Andy J Andrews
Carol A Fierke
Hashim M Al-Hashimi
University of Michigan · US

Funding

ENZYMOLOGY OF RNA PROCESSING ENZYMESR01GM055387 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FIERKE, CAROL A · 1997 to 2014
$4.3M
Targeting HIV-1 Regulatory RNA ElementsR01AI066975 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI AL-HASHIMI, HASHIM M · 2005 to 2014
$2.6M
NIAID NIH HHS R01 AI066975NIGMS NIH HHS R01 GM055387NIGMS NIH HHS R01 GM55387
6 · The paper itself

Abstract

The P4 helix is an essential element of ribonuclease P (RNase P) that is believed to bind catalytically important metals. Here, we applied a combination of NMR residual dipolar couplings (RDCs) and a recently introduced domain-elongation strategy for measuring "motionally decoupled" relaxation data to characterize the structural dynamics of the P4 helix from Bacillus subtilis RNase P. In the absence of divalent ions, the two P4 helical domains undergo small amplitude (approximately 13 degrees) collective motions about an average interhelical angle of 10 degrees. The highly conserved U7 bulge and helical residue C8, which are proposed to be important for substrate recognition and metal binding, are locally mobile at pico- to nanosecond timescales and together form the pivot point for the collective domain motions. Chemical shift mapping reveals significant association of Mg2+ ions at the P4 major groove near the flexible pivot point at residues (A5, G22, G23) previously identified to bind catalytically important metals. The Mg2+ ions do not, however, significantly alter the structure or dynamics of P4. Analysis of results in the context of available X-ray structures of the RNA component of RNase P and structural models that include the pre-tRNA substrate suggest that the internal motions observed in P4 likely facilitate adaptive changes in conformation that take place during folding and substrate recognition, possibly aided by interactions with Mg2+ ions. Our results add to a growing view supporting the existence of functionally important internal motions in RNA occurring at nanosecond timescales.

Indexed as

Bacillus subtilisCrystallography, X-RayGeobacillus stearothermophilusMagnesiumModels, MolecularNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationRibonuclease PRNA, BacterialRNA, CatalyticRNA PrecursorsRNA, TransferStatic ElectricityMagnesiumRibonuclease PRNA, BacterialRNA, CatalyticRNA PrecursorsRNA, Transfer

Identifiers

PMID17194721
PMCPMC1781369
OpenAlexW2123605996

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.