Evidence map›Paper›PMID 36623584›Full record

ArticleJournal of molecular biology2023

Fork-Remodeling Helicase Rad5 Preferentially Reverses Replication Forks with Gaps in the Leading Strand.

Justin A Ling, Melissa S Gildenberg, Masayoshi Honda, Christine M Kondratick, Maria Spies, M Todd Washington

Abstract read
In one paragraph

Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

6 authors.

Justin A LingDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States. Electronic address: https://twitter.com/Biochem_Ling.
Melissa S GildenbergDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States. Electronic address: https://twitter.com/MGild01.
Masayoshi HondaDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States.
Christine M KondratickDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States.
Maria SpiesDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States. Electronic address: https://twitter.com/maria_spies.
M Todd WashingtonDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States. Electronic address: todd-washington@uiowa.edu.

Funding

Mechanisms of Damaged DNA Replication in EukaryotesR01GM081433 · NIGMS · UNIVERSITY OF IOWA · PI WASHINGTON, M. TODD · 2008 to 2021
$4.2M
The Role of Human RAD52 Protein in Genome StabilityR01CA232425 · NCI · UNIVERSITY OF IOWA · PI Maria Spies · 2019 to 2026
$3.1M
Structural and Mechanistic Studies of DNA Damage Bypass Pathways in EukaryotesR35GM148186 · NIGMS · UNIVERSITY OF IOWA · PI M. TODD WASHINGTON · 2023 to 2026
$1.5M
Iowa Biotech-TP: Predoctoral Program in BiotechnologyT32GM152268 · NIGMS · UNIVERSITY OF IOWA · PI MARK A. ARNOLD, Michael John Schnieders · 2024 to 2026
$1.3M
NCI NIH HHS R01 CA232425NIGMS NIH HHS R01 GM081433NIGMS NIH HHS R35 GM148186NIGMS NIH HHS T32 GM152268
6 · The paper itself

Abstract

DNA damage bypass pathways promote the replication of damaged DNA when replication forks stall at sites of DNA damage. Template switching is a DNA damage bypass pathway in which fork-reversal helicases convert stalled replication forks into four-way DNA junctions called chicken foot intermediates, which are subsequently extended by replicative DNA polymerases. In yeast, fork-reversal is carried out by the Rad5 helicase using an unknown mechanism. To better understand the mechanism of Rad5 and its specificity for different fork DNA substrates, we used a FRET-based assay to observe fork reversal in real time. We examined the ability of Rad5 to bind and catalyze the reversal of various fork DNA substrates in the presence of short gaps in the leading or lagging strand as well as in the presence or absence of RPA and RNA primers in the lagging strand. We found that Rad5 preferentially reverses fork DNA substrates with short gaps (10 to 30 nt.) in the leading strand. Thus, Rad5 preferentially reverses fork DNA substrates that form chicken foot intermediates with 5' overhangs that can be extended by replicative DNA polymerases during the subsequent steps of template switching.

Indexed as

DNA DamageDNA HelicasesDNA ReplicationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA HelicasesRAD5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsDNA repairDNA replicationreplication fork reversaltemplate switchingtranslesion synthesis

Identifiers

PMID36623584
PMCPMC9915103

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Registered trials

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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.