Evidence map›Paper›PMID 25550159›Full record

ArticleThe Journal of biological chemistry2015

Crystal structure of the human primase.

Andrey G Baranovskiy, Yinbo Zhang, Yoshiaki Suwa, Nigar D Babayeva, Jianyou Gu, Youri I Pavlov, Tahir H Tahirov

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Article
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  9. Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
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  18. An iron-sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
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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

7 authors.

Andrey G BaranovskiyFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198.
Yinbo ZhangFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198, the Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska 68198, and.
Yoshiaki SuwaFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198.
Nigar D BabayevaFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198.
Jianyou GuFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198.
Youri I PavlovFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198, the Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska 68198, and the Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska 68198.
Tahir H TahirovFrom the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198, ttahirov@unmc.edu.

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI CHIU, WAH · 1985 to 2011
$22.1M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Human DNA Replication Machines: Structure-Function of Polymerase Alpha-PrimaseR01GM101167 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI TAHIROV, TAHIR H · 2013 to 2017
$1.9M
Control of Genome Stability by Replicative DNA PolymerasesR01CA129925 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PAVLOV, YOURI I · 2008 to 2012
$1.2M
NCI NIH HHS CA129925NCI NIH HHS P30 CA036727NCI NIH HHS P30CA036727NCI NIH HHS R01 CA129925NCRR NIH HHS P41 RR002250NIGMS NIH HHS GM101167NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM101167
6 · The paper itself

Abstract

DNA replication in bacteria and eukaryotes requires the activity of DNA primase, a DNA-dependent RNA polymerase that lays short RNA primers for DNA polymerases. Eukaryotic and archaeal primases are heterodimers consisting of small catalytic and large accessory subunits, both of which are necessary for RNA primer synthesis. Understanding of RNA synthesis priming in eukaryotes is currently limited due to the lack of crystal structures of the full-length primase and its complexes with substrates in initiation and elongation states. Here we report the crystal structure of the full-length human primase, revealing the precise overall organization of the enzyme, the relative positions of its functional domains, and the mode of its interaction with modeled DNA and RNA. The structure indicates that the dramatic conformational changes in primase are necessary to accomplish the initiation and then elongation of RNA synthesis. The presence of a long linker between the N- and C-terminal domains of p58 provides the structural basis for the bulk of enzyme's conformational flexibility. Deletion of most of this linker affected the initiation and elongation steps of the primer synthesis.

Indexed as

Models, MolecularProtein Structure, SecondaryProtein Structure, TertiaryBiocatalysisCatalytic DomainCrystallography, X-RayDNADNA PrimaseElectrophoresis, Polyacrylamide GelHumansHydrogen BondingMutationProtein BindingProtein SubunitsRNASubstrate SpecificityDNADNA PrimaseProtein SubunitsRNARNA primersCrystal StructureDNA PrimaseDNA ReplicationIron-Sulfur ProteinProtein ComplexZinc

Identifiers

PMID25550159
PMCPMC4342476

What OpenQuestion holds

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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.