Evidence map›Paper›PMID 19220053›Full record

ArticleJournal of the American Chemical Society2009

Motions of the substrate recognition duplex in a group I intron assessed by site-directed spin labeling.

Gian Paola G Grant, Nathan Boyd, Daniel Herschlag, Peter Z Qin

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
7.6field-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

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  10. Hierarchy of RNA functional dynamics.Annual review of biochemistry · 2014
    Review
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  19. Article
  20. RNA dynamics: perspectives from spin labels.Wiley interdisciplinary reviews. RNA
    Review
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.

Gian Paola G GrantDepartment of Chemistry, University of Southern California, Los Angeles, California 90089-0744, USA.
Nathan Boyd
Daniel Herschlag
Peter Z Qin
University of Southern California · USStanford University · US

Funding

Time-resolved small angle X-ray scatteringP01GM066275 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2003 to 2017
$17.8M
Enzymology of a Catalytic RNA MoleculeR37GM049243 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2002 to 2011
$4.2M
ENZYMOLOGY OF A CATALYTIC RNA MOLECULER01GM049243 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 1993 to 2016
$2.3M
Structure, dynamics, and function of the packaging RNAR01GM069557 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI QIN, PETER Z · 2006 to 2010
$1.4M
NIGMS NIH HHS GM066275NIGMS NIH HHS GM069557NIGMS NIH HHS GM49243NIGMS NIH HHS P01 GM066275NIGMS NIH HHS R01 GM049243NIGMS NIH HHS R01 GM069557NIGMS NIH HHS R37 GM049243
6 · The paper itself

Abstract

The Tetrahymena group I intron recognizes its oligonucleotide substrate in a two-step process. First, a substrate recognition duplex, called the P1 duplex, is formed. The P1 duplex then docks into the prefolded ribozyme core by forming tertiary contacts. P1 docking controls both the rate and the fidelity of substrate cleavage and has been extensively studied as a model for the formation of RNA tertiary structure. However, previous work has been limited to studying millisecond or slower motions. Here we investigated nanosecond P1 motions in the context of the ribozyme using site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) spectroscopy. A nitroxide spin label (R5a) was covalently attached to a specific site of the substrate oligonucleotide, the labeled substrate was bound to a prefolded ribozyme to form the P1 duplex, and X-band EPR spectroscopy was used to monitor nitroxide motions in the 0.1-50 ns regime. Using substrates that favor the docked or the undocked states, it was established that R5a was capable of reporting P1 duplex motions. Using R5a-labeled substrates it was found that the J1/2 junction connecting P1 to the ribozyme core controls nanosecond P1 mobility in the undocked state. This may account for previous observations that J1/2 mutations weaken substrate binding and give rise to cryptic cleavage. This study establishes the use of SDSL to probe nanosecond dynamic behaviors of individual helices within large RNA and RNA/protein complexes. This approach may help in understanding the relationship between RNA structure, dynamics, and function.

Indexed as

Spin LabelsElectron Spin Resonance SpectroscopyExonsIntronsModels, MolecularProtein ConformationRNA, CatalyticSubstrate SpecificityTetrahymena thermophilaRNA, CatalyticSpin Labels

Identifiers

PMID19220053
PMCPMC2788000
OpenAlexW1964184395

What OpenQuestion holds

Textmetadata
LicenceTDM
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.