Cryoelectron tomography of radial spokes in cilia and flagella

Author:

Pigino Gaia1,Bui Khanh Huy1,Maheshwari Aditi12,Lupetti Pietro3,Diener Dennis4,Ishikawa Takashi1

Affiliation:

1. Biomolecular Research Laboratory, Paul Scherrer Institute, 5232 Villigen PSI, Switzerland

2. Swiss Federal Institute of Technology Zürich, CH-8093 Zürich, Switzerland

3. Department of Evolutionary Biology, University of Siena, 53100 Siena, Italy

4. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520

Abstract

Radial spokes (RSs) are ubiquitous components in the 9 + 2 axoneme thought to be mechanochemical transducers involved in local control of dynein-driven microtubule sliding. They are composed of >23 polypeptides, whose interactions and placement must be deciphered to understand RS function. In this paper, we show the detailed three-dimensional (3D) structure of RS in situ in Chlamydomonas reinhardtii flagella and Tetrahymena thermophila cilia that we obtained using cryoelectron tomography (cryo-ET). We clarify similarities and differences between the three spoke species, RS1, RS2, and RS3, in T. thermophila and in C. reinhardtii and show that part of RS3 is conserved in C. reinhardtii, which only has two species of complete RSs. By analyzing C. reinhardtii mutants, we identified the specific location of subsets of RS proteins (RSPs). Our 3D reconstructions show a twofold symmetry, suggesting that fully assembled RSs are produced by dimerization. Based on our cryo-ET data, we propose models of subdomain organization within the RS as well as interactions between RSPs and with other axonemal components.

Publisher

Rockefeller University Press

Subject

Cell Biology

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