The molecular architecture of axonemes revealed by cryoelectron tomography - PubMed (original) (raw)
. 2006 Aug 18;313(5789):944-8.
doi: 10.1126/science.1128618.
Affiliations
- PMID: 16917055
- DOI: 10.1126/science.1128618
The molecular architecture of axonemes revealed by cryoelectron tomography
Daniela Nicastro et al. Science. 2006.
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.
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