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TitleThe structure and symmetry of the radial spoke protein complex in flagella.
Journal, issue, pagesJ Cell Sci, Vol. 133, Issue 16, Year 2020
Publish dateAug 21, 2020
AuthorsEmiliya Poghosyan / Ioan Iacovache / Lenka Faltova / Alexander Leitner / Pinfen Yang / Dennis R Diener / Ruedi Aebersold / Benoit Zuber / Takashi Ishikawa /
PubMed AbstractThe radial spoke is a key element in a transducer apparatus controlling the motility of eukaryotic cilia. The transduction biomechanics is a long-standing question in cilia biology. The radial spoke ...The radial spoke is a key element in a transducer apparatus controlling the motility of eukaryotic cilia. The transduction biomechanics is a long-standing question in cilia biology. The radial spoke has three regions - a spoke head, a bifurcated neck and a stalk. Although the neck and the stalk are asymmetric, twofold symmetry of the head has remained controversial. In this work we used single particle cryo-electron microscopy (cryo-EM) analysis to generate a 3D structure of the whole radial spoke at unprecedented resolution. We show the head region at 15 Å (1.5 nm) resolution and confirm twofold symmetry. Using distance constraints generated by cross-linking mass spectrometry, we locate two components, RSP2 and RSP4, at the head and neck regions. Our biophysical analysis of isolated RSP4, RSP9, and RSP10 affirmed their oligomeric state. Our results enable us to redefine the boundaries of the regions and propose a model of organization of the radial spoke component proteins.
External linksJ Cell Sci / PubMed:32694165
MethodsEM (single particle)
Resolution15.0 - 20.0 Å
Structure data

EMDB-11085:
Radial spoke head structure with 2-fold symmetization
Method: EM (single particle) / Resolution: 15.0 Å

EMDB-11086:
Radial spoke from cilia (before symmetrization)
Method: EM (single particle) / Resolution: 20.0 Å

Source
  • Chlamydomonas reinhardtii (plant)

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