Evidence map›Paper›PMID 28507156›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

RNA primer-primase complexes serve as the signal for polymerase recycling and Okazaki fragment initiation in T4 phage DNA replication.

Michelle M Spiering, Philip Hanoian, Swathi Gannavaram, Stephen J Benkovic

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Understanding DNA replication by the bacteriophage T4 replisome.The Journal of biological chemistry · 2017
    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

4 authors at 1 institution in 1 country.

Michelle M SpieringDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802.
Philip HanoianDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802.
Swathi GannavaramDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802.
Stephen J BenkovicDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802 sjb1@psu.edu.
Pennsylvania State University · US

Funding

PHOSPHATE ACTIVATION MECHANISMSR01GM013306 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BENKOVIC, STEPHEN J · 1985 to 2022
$10.0M
NIGMS NIH HHS R01 GM013306
6 · The paper itself

Abstract

The opposite strand polarity of duplex DNA necessitates that the leading strand is replicated continuously whereas the lagging strand is replicated in discrete segments known as Okazaki fragments. The lagging-strand polymerase sometimes recycles to begin the synthesis of a new Okazaki fragment before finishing the previous fragment, creating a gap between the Okazaki fragments. The mechanism and signal that initiate this behavior-that is, the signaling mechanism-have not been definitively identified. We examined the role of RNA primer-primase complexes left on the lagging ssDNA from primer synthesis in initiating early lagging-strand polymerase recycling. We show for the T4 bacteriophage DNA replication system that primer-primase complexes have a residence time similar to the timescale of Okazaki fragment synthesis and the ability to block a holoenzyme synthesizing DNA and stimulate the dissociation of the holoenzyme to trigger polymerase recycling. The collision with primer-primase complexes triggering the early termination of Okazaki fragment synthesis has distinct advantages over those previously proposed because this signal requires no transmission to the lagging-strand polymerase through protein or DNA interactions, the mechanism for rapid dissociation of the holoenzyme is always collision, and no unique characteristics need to be assigned to either identical polymerase in the replisome. We have modeled repeated cycles of Okazaki fragment initiation using a collision with a completed Okazaki fragment or primer-primase complexes as the recycling mechanism. The results reproduce experimental data, providing insights into events related to Okazaki fragment initiation and the overall functioning of DNA replisomes.

Indexed as

Bacteriophage T4DNADNA-Directed DNA PolymeraseDNA PrimersDNA ReplicationDNA, Single-StrandedDNA, ViralEscherichia coliMultienzyme ComplexesReplisomesDNADNA-Directed DNA PolymeraseDNA PrimersDNA, Single-StrandedDNA, ViralMultienzyme ComplexesOkazaki fragmentsReplisomesDNA replicationOkazaki fragment initiationpoymerase recyclingstochastic modelingT4 bacteriophage

Identifiers

PMID28507156
PMCPMC5465878
OpenAlexW2616404180

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.