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Smc5/6 Complex Promotes Rad3 Checkpoint Signaling at the Perturbed Replication Fork through Sumoylation of the RecQ Helicase Rqh1. | LitMetric

AI Article Synopsis

  • Smc5/6 is a key structural complex for chromosome stability, equipped with an important subunit, Nse2, that has SUMO E3 ligase activity, setting it apart from similar complexes like cohesin and condensin.
  • Researchers identified new mutants in fission yeast that affect the Smc5/6 complex, revealing that the SUMO modification of the RecQ helicase Rqh1 by Nse2 is crucial for effective DNA replication checkpoint signaling.
  • Remarkably, altering sumoylation sites on Rqh1 in a mutant lacking helicase activity surprisingly enhanced cell survival under stressful conditions, suggesting a complex relationship between sumoylation, helicase function, and DNA damage responses that may also apply to human

Article Abstract

Smc5/6, like cohesin and condensin, is a structural maintenance of chromosomes complex crucial for genome stability. Unlike cohesin and condensin, Smc5/6 carries an essential Nse2 subunit with SUMO E3 ligase activity. While screening for new DNA replication checkpoint mutants in fission yeast, we have identified two previously uncharacterized mutants in Smc5/6. Characterization of the mutants and a series of previously reported Smc5/6 mutants uncovered that sumoylation of the RecQ helicase Rqh1 by Nse2 facilitates the checkpoint signaling at the replication fork. We found that mutations that eliminate the sumoylation sites or the helicase activity of Rqh1 compromised the checkpoint signaling similar to a mutant lacking the ligase activity. Surprisingly, introducing a sumoylation site mutation to a helicase-inactive mutant promoted cell survival under stress. These findings, together with other genetic data, support a mechanism that sumoylation of Rqh1 by Smc5/6-Nse2 recruits Rqh1 or modulates its helicase activity at the fork to facilitate the checkpoint signaling. Since the Smc5/6 complex, Rqh1, and the replication checkpoint are conserved in eukaryotes, a similar checkpoint mechanism may be operating in human cells.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9202435PMC
http://dx.doi.org/10.1128/mcb.00045-22DOI Listing

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