Evidence map›Paper›PMID 16092891›Full record

ArticlePLoS biology2005

Functional identification of catalytic metal ion binding sites within RNA.

James L Hougland, Alexander V Kravchuk, Daniel Herschlag, Joseph A Piccirilli

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.7field-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

31 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Calcium inhibition of ribonuclease H1 two-metal ion catalysis.Journal of the American Chemical Society · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  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

4 authors at 2 institutions in 1 country.

James L HouglandDepartment of Chemistry, University of Chicago, Illinois, USA.
Alexander V Kravchuk
Daniel Herschlag
Joseph A Piccirilli
Stanford University · USUniversity of Chicago · US

Funding

Predoctoral Training Program in Chemistry & BiologyT32GM008720 · NIGMS · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 1999 to 2020
$4.7M
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
NIGMS NIH HHS 2 T32 GM008720-06NIGMS NIH HHS GM49243NIGMS NIH HHS R01 GM049243NIGMS NIH HHS R37 GM049243NIGMS NIH HHS T32 GM008720
6 · The paper itself

Abstract

The viability of living systems depends inextricably on enzymes that catalyze phosphoryl transfer reactions. For many enzymes in this class, including several ribozymes, divalent metal ions serve as obligate cofactors. Understanding how metal ions mediate catalysis requires elucidation of metal ion interactions with both the enzyme and the substrate(s). In the Tetrahymena group I intron, previous work using atomic mutagenesis and quantitative analysis of metal ion rescue behavior identified three metal ions (MA, MB, and MC) that make five interactions with the ribozyme substrates in the reaction's transition state. Here, we combine substrate atomic mutagenesis with site-specific phosphorothioate substitutions in the ribozyme backbone to develop a powerful, general strategy for defining the ligands of catalytic metal ions within RNA. In applying this strategy to the Tetrahymena group I intron, we have identified the pro-SP phosphoryl oxygen at nucleotide C262 as a ribozyme ligand for MC. Our findings establish a direct connection between the ribozyme core and the functionally defined model of the chemical transition state, thereby extending the known set of transition-state interactions and providing information critical for the application of the recent group I intron crystallographic structures to the understanding of catalysis.

Indexed as

AnimalsBinding SitesCatalysisCations, DivalentMetalsRNA, CatalyticTetrahymenaCations, DivalentMetalsRNA, Catalytic

Identifiers

PMID16092891
PMCPMC1184590
OpenAlexW1990578006

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.