Evidence map›Paper›PMID 26857547›Full record

ArticleNucleic acids research2016

Kinetic mechanism and fidelity of nick sealing by Escherichia coli NAD+-dependent DNA ligase (LigA).

Mathieu Chauleau, Stewart Shuman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Episomal and chromosomal DNA replication and recombination inFrontiers in molecular biosciences · 2023
    Review
  3. Alleviation of C⋅C Mismatches in DNA by theFrontiers in microbiology · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Excision of the doubly methylated basePhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
  9. Article
  10. The Sole DNA Ligase inFrontiers in cellular and infection microbiology · 2018
    Article
  11. Article
  12. Lethality of MalE-LacZ hybrid protein shares mechanistic attributes with oxidative component of antibiotic lethality.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NADProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. 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

2 authors at 1 institution in 1 country.

Mathieu ChauleauMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Stewart ShumanMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA s-shuman@ski.mskcc.org.
Kettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Viral DNA and RNA LigasesR01GM063611 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 2001 to 2017
$5.4M
NCI NIH HHS P30 CA008748NCI NIH HHS P30-CA008748NIGMS NIH HHS GM63611NIGMS NIH HHS R01 GM063611
6 · The paper itself

Abstract

Escherichia coli DNA ligase (EcoLigA) repairs 3'-OH/5'-PO4 nicks in duplex DNA via reaction of LigA with NAD(+) to form a covalent LigA-(lysyl-Nζ)-AMP intermediate (step 1); transfer of AMP to the nick 5'-PO4 to form an AppDNA intermediate (step 2); and attack of the nick 3'-OH on AppDNA to form a 3'-5' phosphodiester (step 3). A distinctive feature of EcoLigA is its stimulation by ammonium ion. Here we used rapid mix-quench methods to analyze the kinetic mechanism of single-turnover nick sealing by EcoLigA-AMP. For substrates with correctly base-paired 3'-OH/5'-PO4 nicks, kstep2 was fast (6.8-27 s(-1)) and similar to kstep3 (8.3-42 s(-1)). Absent ammonium, kstep2 and kstep3 were 48-fold and 16-fold slower, respectively. EcoLigA was exquisitely sensitive to 3'-OH base mispairs and 3' N:abasic lesions, which elicited 1000- to >20000-fold decrements in kstep2. The exception was the non-canonical 3' A:oxoG configuration, which EcoLigA accepted as correctly paired for rapid sealing. These results underscore: (i) how EcoLigA requires proper positioning of the nick 3' nucleoside for catalysis of 5' adenylylation; and (ii) EcoLigA's potential to embed mutations during the repair of oxidative damage. EcoLigA was relatively tolerant of 5'-phosphate base mispairs and 5' N:abasic lesions.

Indexed as

DNA RepairAdenosine MonophosphateAmmonium SulfateBase Pair MismatchBase SequenceDNADNA Breaks, Double-StrandedDNA LigasesEnzyme AssaysEscherichia coliEscherichia coli ProteinsGene ExpressionKineticsMolecular Sequence DataNADRecombinant Fusion ProteinsAdenosine MonophosphateAmmonium SulfateDNADNA LigasesEscherichia coli ProteinsLigA protein, E coliNADRecombinant Fusion Proteins

Identifiers

PMID26857547
PMCPMC4797296
OpenAlexW2265043575

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.