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Genetic screening identifies a SUMO protease dynamically maintaining centromeric chromatin

Author

Listed:
  • Sreyoshi Mitra

    (University of Oxford
    Instituto Gulbenkian de Ciência)

  • Dani L. Bodor

    (Instituto Gulbenkian de Ciência
    UCL)

  • Ana F. David

    (Instituto Gulbenkian de Ciência
    Institute of Molecular Biotechnology)

  • Izma Abdul-Zani

    (University of Oxford)

  • João F. Mata

    (Instituto Gulbenkian de Ciência)

  • Beate Neumann

    (European Molecular Biology Laboratory (EMBL))

  • Sabine Reither

    (European Molecular Biology Laboratory (EMBL))

  • Christian Tischer

    (European Molecular Biology Laboratory (EMBL))

  • Lars E. T. Jansen

    (University of Oxford
    Instituto Gulbenkian de Ciência)

Abstract

Centromeres are defined by a self-propagating chromatin structure based on stable inheritance of CENP-A containing nucleosomes. Here, we present a genetic screen coupled to pulse-chase labeling that allow us to identify proteins selectively involved in deposition of nascent CENP-A or in long-term transmission of chromatin-bound CENP-A. These include factors with known roles in DNA replication, repair, chromatin modification, and transcription, revealing a broad set of chromatin regulators that impact on CENP-A dynamics. We further identify the SUMO-protease SENP6 as a key factor, not only controlling CENP-A stability but virtually the entire centromere and kinetochore. Loss of SENP6 results in hyper-SUMOylation of CENP-C and CENP-I but not CENP-A itself. SENP6 activity is required throughout the cell cycle, suggesting that a dynamic SUMO cycle underlies a continuous surveillance of the centromere complex that in turn ensures stable transmission of CENP-A chromatin.

Suggested Citation

  • Sreyoshi Mitra & Dani L. Bodor & Ana F. David & Izma Abdul-Zani & João F. Mata & Beate Neumann & Sabine Reither & Christian Tischer & Lars E. T. Jansen, 2020. "Genetic screening identifies a SUMO protease dynamically maintaining centromeric chromatin," Nature Communications, Nature, vol. 11(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-019-14276-x
    DOI: 10.1038/s41467-019-14276-x
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