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Structure of the motor subunit of type I restriction-modification complex EcoR124I

Nature Structural & Molecular Biology volume 16, pages 9495 (2009) | Download Citation

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Abstract

Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.

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Acknowledgements

We gratefully acknowledge support from the Ministry of Education, Youth and Sports of the Czech Republic (MSM6007665808, LC06010), Academy of Sciences of the Czech Republic (AVOZ60870520), Grant Agency of the Czech Republic (203/08/0114 to R.E), the European Molecular Biology Organization (to M.L.), the Swiss National Science Foundation (to P.J.) and joint Czech and US National Science Foundation International Research Cooperation (INT03-09049 to J.C.). We thank the European Molecular Biology Laboratory for access to the X12 beamline at the DORIS storage ring, DESY, Hamburg. J.C. and R.E. thank F. Hughson, T. Lohman, B. Matthews, L. Raleigh and S. Weller for insightful discussion during preparation of the manuscript.

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Affiliations

  1. Department of Structure and Function of Proteins, Institute of Systems Biology and Ecology, Academy of Sciences of the Czech Republic

    • Mikalai Lapkouski
    • , Ivana Kuta Smatanova
    • , Rüdiger Ettrich
    •  & Eva Csefalvay
  2. Institute of Physical Biology, University of South Bohemia in Ceske Budejovice, Zamek 136, CZ-373 33 Nove Hrady, Czech Republic.

    • Mikalai Lapkouski
    • , Ivana Kuta Smatanova
    • , Rüdiger Ettrich
    •  & Eva Csefalvay
  3. EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D22603 Hamburg, Germany.

    • Santosh Panjikar
  4. Institute of Molecular Cancer Research, University of Zürich, Wintherthurerstrasse 190, CH-8057 Zürich, Switzerland.

    • Pavel Janscak
  5. Chemistry Department, Princeton University, Princeton, New Jersey 08544-1009, USA.

    • Jannette Carey

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Correspondence to Jannette Carey or Rüdiger Ettrich.

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DOI

https://doi.org/10.1038/nsmb.1523

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