Evidence map›Paper›PMID 22795082›Full record

ArticleStructure (London, England : 1993)2012

Binding mechanism of metal⋅NTP substrates and stringent-response alarmones to bacterial DnaG-type primases.

Richard U Rymer, Francisco A Solorio, Ashley K Tehranchi, Clement Chu, Jacob E Corn, James L Keck, Jue D Wang, James M Berger

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

47 citing papers in PubMed, 74 citations in OpenAlex.

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  8. mLife · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Richard U RymerCalifornia Institute for Quantitative Biosciences, 374D Stanley Hall #3220, University of California, Berkeley, Berkeley, CA 94720-3220, USA.
Francisco A Solorio
Ashley K Tehranchi
Clement Chu
Jacob E Corn
James L Keck
Jue D Wang
James M Berger
QB3 · USUniversity of California, San Francisco · US

Funding

Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
Structure/Function Studies of DNA Replication InitiationR01GM071747 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 2005 to 2016
$4.0M
Control of GTP Homeostasis by (p)ppGppR01GM084003 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI WANG, JUE D. · 2009 to 2017
$2.2M
NIGMS NIH HHS GM071747NIGMS NIH HHS GM084003NIGMS NIH HHS R01 GM071747NIGMS NIH HHS R01 GM084003NIGMS NIH HHS R37 GM071747
6 · The paper itself

Abstract

Primases are DNA-dependent RNA polymerases found in all cellular organisms. In bacteria, primer synthesis is carried out by DnaG, an essential enzyme that serves as a key component of DNA replication initiation, progression, and restart. How DnaG associates with nucleotide substrates and how certain naturally prevalent nucleotide analogs impair DnaG function are unknown. We have examined one of the earliest stages in primer synthesis and its control by solving crystal structures of the S. aureus DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp. These structures, together with both biochemical analyses and comparative studies of enzymes that use the same catalytic fold as DnaG, pinpoint the predominant nucleotide-binding site of DnaG and explain how the induction of the stringent response in bacteria interferes with primer synthesis.

Indexed as

Bacterial ProteinsCatalytic DomainCoenzymesConserved SequenceCoordination ComplexesCrystallography, X-RayDeoxyribonucleotidesDNA PrimaseGuanosine PentaphosphateGuanosine TetraphosphateManganeseModels, MolecularProtein BindingProtein Structure, SecondaryStaphylococcus aureusStress, PhysiologicalBacterial ProteinsCoenzymesCoordination ComplexesDeoxyribonucleotidesDNA PrimaseGuanosine PentaphosphateGuanosine TetraphosphateManganese

Identifiers

PMID22795082
PMCPMC3438381
OpenAlexW2026828254

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.