Evidence map›Paper›PMID 21697085›Full record

ArticleThe Journal of biological chemistry2011

Pyrovanadolysis, a pyrophosphorolysis-like reaction mediated by pyrovanadate, Mn2+, and DNA polymerase of bacteriophage T7.

Barak Akabayov, Arkadiusz W Kulczyk, Sabine R Akabayov, Christopher Theile, Larry W McLaughlin, Benjamin Beauchamp, Antoine M van Oijen, Charles C Richardson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Vanadate Retention by Iron and Manganese Oxides.ACS earth & space chemistry · 2022
    Article
  3. Review
  4. Vanadium. Its role for humans.Metal ions in life sciences · 2013
    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

8 authors at 3 institutions in 2 countries.

Barak AkabayovDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Arkadiusz W KulczykDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Sabine R AkabayovDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Christopher TheileDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Larry W McLaughlinDepartment of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, and.
Benjamin BeauchampDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Antoine M van OijenZernike Institute for Advanced Materials Centre for Synthetic Biology, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Charles C RichardsonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115,. Electronic address: ccr@hms.harvard.edu.
Harvard University · USBoston College · USUniversity of Groningen · NL

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
STRUCTURE AND SYNTHESIS OF DNAR01GM054397 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RICHARDSON, CHARLES C. · 1996 to 2011
$7.6M
NIBIB NIH HHS P30 EB009998NIBIB NIH HHS P30-EB-009998NIGMS NIH HHS GM54397NIGMS NIH HHS R01 GM054397
6 · The paper itself

Abstract

DNA polymerases catalyze the 3'-5'-pyrophosphorolysis of a DNA primer annealed to a DNA template in the presence of pyrophosphate (PP(i)). In this reversal of the polymerization reaction, deoxynucleotides in DNA are converted to deoxynucleoside 5'-triphosphates. Based on the charge, size, and geometry of the oxygen connecting the two phosphorus atoms of PP(i), a variety of compounds was examined for their ability to carry out a reaction similar to pyrophosphorolysis. We describe a manganese-mediated pyrophosphorolysis-like activity using pyrovanadate (VV) catalyzed by the DNA polymerase of bacteriophage T7. We designate this reaction pyrovanadolysis. X-ray absorption spectroscopy reveals a shorter Mn-V distance of the polymerase-VV complex than the Mn-P distance of the polymerase-PP(i) complex. This structural arrangement at the active site accounts for the enzymatic activation by Mn-VV. We propose that the Mn(2+), larger than Mg(2+), fits the polymerase active site to mediate binding of VV into the active site of the polymerase. Our results may be the first documentation that vanadium can substitute for phosphorus in biological processes.

Indexed as

Bacteriophage T7Catalytic DomainDiphosphatesDNA-Directed DNA PolymeraseManganeseVanadatesbacteriophage T7 induced DNA polymeraseDiphosphatesDNA-Directed DNA PolymeraseManganeseVanadates

Identifiers

PMID21697085
PMCPMC3190722
OpenAlexW1966201185

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.