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Science 18 August 2006:
Vol. 313. no. 5789, pp. 944 - 948
DOI: 10.1126/science.1128618
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Research Articles

The Molecular Architecture of Axonemes Revealed by Cryoelectron Tomography

Daniela Nicastro,1*{dagger} Cindi Schwartz,1 Jason Pierson,1 Richard Gaudette,1 Mary E. Porter,2 J. Richard McIntosh1

Eukaryotic flagella and cilia are built on a 9 + 2 array of microtubules plus >250 accessory proteins, forming a biological machine called the axoneme. Here we describe the three-dimensional structure of rapidly frozen axonemes from Chlamydomonas and sea urchin sperm, using cryoelectron tomography and image processing to focus on the motor enzyme dynein. Our images suggest a model for the way dynein generates force to slide microtubules. They also reveal two dynein linkers that may provide "hard-wiring" to coordinate motor enzyme action, both circumferentially and along the axoneme. Periodic densities were also observed inside doublet microtubules; these may contribute to doublet stability.

1 Laboratory for 3D Electron Microscopy of Cells, Department of Molecular, Cellular, and Developmental Biology, CB 347, University of Colorado, Boulder, CO 80309–0347, USA.
2 Department of Genetics, Cell Biology, and Development, 6–160 Jackson Hall, 321 Church Street SE, University of Minnesota, Minneapolis, MN 55455, USA.

* Present address: Brandeis University, Rosenstiel, 415 South Street, Waltham, MA 02454, USA.

{dagger} To whom correspondence should be addressed. E-mail: nicastro{at}colorado.edu

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