Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 944-948 |
| Number of pages | 5 |
| Journal | Science |
| Volume | 313 |
| Issue number | 5789 |
| DOIs | |
| State | Published - Aug 18 2006 |