Evidence map›Paper›PMID 39039288›Full record

ArticleThe EMBO journal2024

A common mechanism for recruiting the Rrm3 and RTEL1 accessory helicases to the eukaryotic replisome.

Ottavia Olson, Simone Pelliciari, Emma D Heron, Tom D Deegan

Abstract read
In one paragraph

Article in The EMBO journal, 2024. 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

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2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Ottavia OlsonMRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Western General Hospital, Edinburgh, EH4 2XU, UK.
Simone Pelliciari *MRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Western General Hospital, Edinburgh, EH4 2XU, UK.
Emma D Heron *MRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Western General Hospital, Edinburgh, EH4 2XU, UK.
Tom D DeeganMRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Western General Hospital, Edinburgh, EH4 2XU, UK. tdeegan@ed.ac.uk.ORCID http://orcid.org/0000-0001-9639-7636

Funding

UKRI | Medical Research Council (MRC) MC_UU_00035/4
6 · The paper itself

Abstract

The eukaryotic replisome is assembled around the CMG (CDC45-MCM-GINS) replicative helicase, which encircles the leading-strand DNA template at replication forks. When CMG stalls during DNA replication termination, or at barriers such as DNA-protein crosslinks on the leading strand template, a second helicase is deployed on the lagging strand template to support replisome progression. How these 'accessory' helicases are targeted to the replisome to mediate barrier bypass and replication termination remains unknown. Here, by combining AlphaFold structural modelling with experimental validation, we show that the budding yeast Rrm3 accessory helicase contains two Short Linear Interaction Motifs (SLIMs) in its disordered N-terminus, which interact with CMG and the leading-strand DNA polymerase Polε on one side of the replisome. This flexible tether positions Rrm3 adjacent to the lagging strand template on which it translocates, and is critical for replication termination in vitro and Rrm3 function in vivo. The primary accessory helicase in metazoa, RTEL1, is evolutionarily unrelated to Rrm3, but binds to CMG and Polε in an analogous manner, revealing a conserved docking mechanism for accessory helicases in the eukaryotic replisome.

Indexed as

DNA HelicasesDNA ReplicationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA Polymerase IIModels, MolecularProtein BindingDNA HelicasesDNA Polymerase IIRrm3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsAccessory HelicaseCMG HelicaseDNA ReplicationRrm3RTEL1

Identifiers

PMID39039288
PMCPMC11405395

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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.