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Rtt107 Is a Multi-functional Scaffold Supporting Replication Progression with Partner SUMO and Ubiquitin Ligases

  • Lisa E. Hang
  • , Jie Peng
  • , Wei Tan
  • , Barnabas Szakal
  • , Demis Menolfi
  • , Ziwei Sheng
  • , Kirill Lobachev
  • , Dana Branzei
  • , Wenyi Feng
  • , Xiaolan Zhao
  • Memorial Sloan-Kettering Cancer Center
  • Rockefeller University
  • SUNY Upstate Medical University
  • FIRC Institute of Molecular Oncology
  • Georgia Institute of Technology

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Elucidating the individual and collaborative functions of genome maintenance factors is critical for understanding how genome duplication is achieved. Here, we investigate a conserved scaffold in budding yeast, Rtt107, and its three partners: a SUMO E3 complex, a ubiquitin E3 complex, and Slx4. Biochemical and genetic findings show that Rtt107 interacts separately with these partners and contributes to their individual functions, including a role in replisome sumoylation. We also provide evidence that Rtt107 associates with replisome components, and both itself and its associated E3s are important for replicating regions far from initiation sites. Corroborating these results, replication defects due to Rtt107 loss and genotoxic sensitivities in mutants of Rtt107 and its associated E3s are rescued by increasing replication initiation events through mutating two master repressors of late origins, Mrc1 and Mec1. These findings suggest that Rtt107 functions as a multi-functional platform to support replication progression with its partner E3 enzymes.

Original languageEnglish
Pages (from-to)268-279
Number of pages12
JournalMolecular Cell
Volume60
Issue number2
DOIs
StatePublished - Oct 15 2015

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