Access

Article

Nature 457, 446-450 (22 January 2009) | doi:10.1038/nature07637; Received 14 May 2008; Accepted 11 November 2008; Published online 7 January 2009

Open Innovation Challenges

  • Optimizing Sub-cellular Localization Tags

    • Deadline: Nov 29 2009
    • Reward: $20,000 USD

    The Seeker is looking for methods to optimize sub-cellular localization tags for protein expression....

  • Single-cell Analysis Platform

    • Deadline: Dec 02 2009
    • Reward: $5,000 USD

    This Challenge is looking for novel approaches to analyzing changes at a single-cell level. This is...

naturejobs

Intersubunit coordination in a homomeric ring ATPase

Jeffrey R. Moffitt1,6, Yann R. Chemla1,6,7, K. Aathavan2, Shelley Grimes3, Paul J. Jardine3, Dwight L. Anderson3,4 & Carlos Bustamante1,2,5

  1. Department of Physics and Jason L. Choy Laboratory of Single Molecule Biophysics,
  2. Biophysics Graduate Group, University of California, Berkeley, California 94720, USA
  3. Department of Diagnostic and Biological Sciences,
  4. Department of Microbiology, University of Minnesota, Minneapolis, Minnesota 55455, USA
  5. Departments of Molecular and Cell Biology, Chemistry, and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA
  6. These authors contributed equally to this work.
  7. Present address: Department of Physics and Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Correspondence to: Carlos Bustamante1,2,5 Correspondence and requests for materials should be addressed to C.B. (Email: carlos@alice.berkeley.edu).

Top

Homomeric ring ATPases perform many vital and varied tasks in the cell, ranging from chromosome segregation to protein degradation. Here we report the direct observation of the intersubunit coordination and step size of such a ring ATPase, the double-stranded-DNA packaging motor in the bacteriophage phi29. Using high-resolution optical tweezers, we find that packaging occurs in increments of 10 base pairs (bp). Statistical analysis of the preceding dwell times reveals that multiple ATPs bind during each dwell, and application of high force reveals that these 10-bp increments are composed of four 2.5-bp steps. These results indicate that the hydrolysis cycles of the individual subunits are highly coordinated by means of a mechanism novel for ring ATPases. Furthermore, a step size that is a non-integer number of base pairs demands new models for motor–DNA interactions.

  1. Department of Physics and Jason L. Choy Laboratory of Single Molecule Biophysics,
  2. Biophysics Graduate Group, University of California, Berkeley, California 94720, USA
  3. Department of Diagnostic and Biological Sciences,
  4. Department of Microbiology, University of Minnesota, Minneapolis, Minnesota 55455, USA
  5. Departments of Molecular and Cell Biology, Chemistry, and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA
  6. These authors contributed equally to this work.
  7. Present address: Department of Physics and Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Correspondence to: Carlos Bustamante1,2,5 Correspondence and requests for materials should be addressed to C.B. (Email: carlos@alice.berkeley.edu).

MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.

NEWS AND VIEWS

Molecular biology Concealed enzyme coordination

Nature News and Views (22 Jan 2009)