Evidence map›Paper›PMID 28192411›Full record

ArticleNature chemical biology2017

The GlcN6P cofactor plays multiple catalytic roles in the glmS ribozyme.

Jamie L Bingaman, Sixue Zhang, David R Stevens, Neela H Yennawar, Sharon Hammes-Schiffer, Philip C Bevilacqua

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Investigation of the pThe journal of physical chemistry. B · 2021
    Article
  9. Review
  10. Synthesis of Oligoribonucleotides Containing a 2'-Amino-5'-The Journal of organic chemistry · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Riboswitches and Translation Control.Cold Spring Harbor perspectives in biology · 2018
    Review
  17. Cellular Small Molecules Contribute to Twister Ribozyme Catalysis.Journal of the American Chemical Society · 2018
    Article
  18. Article
  19. Review
  20. 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

6 authors at 2 institutions in 1 country.

Jamie L BingamanDepartment of Chemistry and Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania, USA.
Sixue ZhangDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
David R StevensDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Neela H YennawarX-ray Crystallography Facility, Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, Pennsylvania, USA.
Sharon Hammes-SchifferDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Philip C BevilacquaDepartment of Chemistry and Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania, USA.
Pennsylvania State University · USUniversity of Illinois Urbana-Champaign · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
Simulation of Proton and Hydride Transfer in EnzymesR37GM056207 · NIGMS · YALE UNIVERSITY · PI HAMMES-SCHIFFER, SHARON · 2011 to 2020
$3.2M
SIMULATION OF PROTON AND HYDRIDE TRANSFER IN ENZYMESR01GM056207 · NIGMS · UNIVERSITY OF NOTRE DAME · PI HAMMES-SCHIFFER, SHARON · 1998 to 2010
$2.7M
NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM056207NIGMS NIH HHS R37 GM056207NIGMS NIH HHS T32 GM070421
6 · The paper itself

Abstract

RNA enzymes (ribozymes) have remarkably diverse biological roles despite having limited chemical diversity. Protein enzymes enhance their reactivity through recruitment of cofactors; likewise, the naturally occurring glmS ribozyme uses the glucosamine-6-phosphate (GlcN6P) organic cofactor for phosphodiester bond cleavage. Prior structural and biochemical studies have implicated GlcN6P as the general acid. Here we describe new catalytic roles of GlcN6P through experiments and calculations. Large stereospecific normal thio effects and a lack of metal-ion rescue in the holoribozyme indicate that nucleobases and the cofactor play direct chemical roles and align the active site for self-cleavage. Large stereospecific inverse thio effects in the aporibozyme suggest that the GlcN6P cofactor disrupts an inhibitory interaction of the nucleophile. Strong metal-ion rescue in the aporibozyme reveals that this cofactor also provides electrostatic stabilization. Ribozyme organic cofactors thus perform myriad catalytic roles, thereby allowing RNA to compensate for its limited functional diversity.

Indexed as

BiocatalysisGlucosamineGlucose-6-PhosphateModels, MolecularMolecular Docking SimulationRNA, CatalyticGlucosamineglucosamine 6-phosphateGlucose-6-PhosphateRNA, Catalytic

Identifiers

PMID28192411
PMCPMC5362308
OpenAlexW2588496355

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.