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TitleMechanisms controlling replication fork stalling and collapse at topoisomerase 1 cleavage complexes.
Journal, issue, pagesMol Cell, Vol. 84, Issue 18, Page 3469-33481.e7, Year 2024
Publish dateSep 19, 2024
AuthorsRose Westhorpe / Johann J Roske / Joseph T P Yeeles /
PubMed AbstractTopoisomerase 1 cleavage complexes (Top1-ccs) comprise a DNA-protein crosslink and a single-stranded DNA break that can significantly impact the DNA replication machinery (replisome). Consequently, ...Topoisomerase 1 cleavage complexes (Top1-ccs) comprise a DNA-protein crosslink and a single-stranded DNA break that can significantly impact the DNA replication machinery (replisome). Consequently, inhibitors that trap Top1-ccs are used extensively in research and clinical settings to generate DNA replication stress, yet how the replisome responds upon collision with a Top1-cc remains obscure. By reconstituting collisions between budding yeast replisomes, assembled from purified proteins, and site-specific Top1-ccs, we have uncovered mechanisms underlying replication fork stalling and collapse. We find that stalled replication forks are surprisingly stable and that their stability is influenced by the template strand that Top1 is crosslinked to, the fork protection complex proteins Tof1-Csm3 (human TIMELESS-TIPIN), and the convergence of replication forks. Moreover, nascent-strand mapping and cryoelectron microscopy (cryo-EM) of stalled forks establishes replisome remodeling as a key factor in the initial response to Top1-ccs. These findings have important implications for the use of Top1 inhibitors in research and in the clinic.
External linksMol Cell / PubMed:39236719 / PubMed Central
MethodsEM (single particle)
Resolution4.7 - 6.2 Å
Structure data

EMDB-50392: Structure of a eukaryotic replisome stalled at a lagging-strand Topoisomerase 1 cleavage complex with Tof1-Csm3
Method: EM (single particle) / Resolution: 6.2 Å

EMDB-50393: Structure of a eukaryotic replisome stalled at a lagging-strand Topoisomerase 1 cleavage complex missing Tof1-Csm3.
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-50395: Structure of a eukaryotic replisome stalled at a leading-strand Topoisomerase 1 cleavage complex.
Method: EM (single particle) / Resolution: 4.9 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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