Evidence map›Paper›PMID 35042821›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

CMG helicase can use ATPγS to unwind DNA: Implications for the rate-limiting step in the reaction mechanism.

Nina Y Yao, Dan Zhang, Olga Yurieva, Michael E O'Donnell

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Unlicensed origin DNA melting by MCV and SV40 polyomavirus LT proteins is independent of ATP-dependent helicase activity.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Review
  10. Inhibition of the SARS-CoV-2 helicase at single-nucleotide resolution.bioRxiv : the preprint server for biology · 2022
    Article
  11. 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 1 institution in 1 country.

Nina Y YaoDNA Replication Laboratory, The Rockefeller University, New York, NY 10065.ORCID 0000-0002-4728-6531
Dan ZhangDNA Replication Laboratory, The Rockefeller University, New York, NY 10065.
Olga YurievaDNA Replication Laboratory, The Rockefeller University, New York, NY 10065.ORCID 0000-0001-5869-8921
Michael E O'DonnellDNA Replication Laboratory, The Rockefeller University, New York, NY 10065; odonnel@rockefeller.edu.ORCID 0000-0001-9002-4214
Rockefeller University · US

Funding

Biochemical Mechanism and Structure of the Eukaryotic Replication ForkR01GM115809 · NIGMS · ROCKEFELLER UNIVERSITY · PI O'DONNELL, MICHAEL E · 2015 to 2022
$2.6M
NIGMS NIH HHS R01 GM115809
6 · The paper itself

Abstract

The adenosine triphosphate (ATP) analog ATPγS often greatly slows or prevents enzymatic ATP hydrolysis. The eukaryotic CMG (Cdc45, Mcm2 to 7, GINS) replicative helicase is presumed unable to hydrolyze ATPγS and thus unable to perform DNA unwinding, as documented for certain other helicases. Consequently, ATPγS is often used to "preload" CMG onto forked DNA substrates without unwinding before adding ATP to initiate helicase activity. We find here that CMG does hydrolyze ATPγS and couples it to DNA unwinding. Indeed, the rate of unwinding of a 20- and 30-mer duplex fork of different sequences by CMG is only reduced 1- to 1.5-fold using ATPγS compared with ATP. These findings imply that a conformational change is the rate-limiting step during CMG unwinding, not hydrolysis. Instead of using ATPγS for loading CMG onto DNA, we demonstrate here that nonhydrolyzable adenylyl-imidodiphosphate (AMP-PNP) can be used to preload CMG onto a forked DNA substrate without unwinding.

Indexed as

Adenosine TriphosphateCell Cycle ProteinsDNADNA-Binding ProteinsDNA HelicasesDNA ReplicationMultiprotein ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphateCell Cycle ProteinsDNADNA-Binding ProteinsDNA HelicasesMultiprotein ComplexesSaccharomyces cerevisiae ProteinsATPgammaSCMG helicaseDNA replicationrate-limiting stepstaircase model

Identifiers

PMID35042821
PMCPMC8794833
OpenAlexW4206149049

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.