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Published 19 June 2006. doi:10.1083/jcb.200603153
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 6, 867-877
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Article

 Structural role of Sfi1p–centrin filaments in budding yeast spindle pole body duplication

Sam Li1, Alan M. Sandercock2, Paul Conduit1, Carol V. Robinson2, Roger L. Williams1, and John V. Kilmartin1

1 Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK
2 Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, England, UK

Correspondence to John V. Kilmartin: jvk{at}mrc-lmb.cam.ac.uk

Centrins are calmodulin-like proteins present in centrosomes and yeast spindle pole bodies (SPBs) and have essential functions in their duplication. The Saccharomyces cerevisiae centrin, Cdc31p, binds Sfi1p on multiple conserved repeats; both proteins localize to the SPB half-bridge, where the new SPB is assembled. The crystal structures of Sfi1p–centrin complexes containing several repeats show Sfi1p as an {alpha} helix with centrins wrapped around each repeat and similar centrin–centrin contacts between each repeat. Electron microscopy (EM) shadowing of an Sfi1p–centrin complex with 15 Sfi1 repeats and 15 centrins bound showed filaments 60 nm long, compatible with all the Sfi1 repeats as a continuous {alpha} helix. Immuno-EM localization of the Sfi1p N and C termini showed Sfi1p–centrin filaments spanning the length of the half-bridge with the Sfi1p N terminus at the SPB. This suggests a model for SPB duplication where the half-bridge doubles in length by association of the Sfi1p C termini, thereby providing a new Sfi1p N terminus to initiate SPB assembly.

Abbreviations used in this paper: MTOC, microtubule organizing center; rmsd, root mean square deviation; SPB, spindle pole body; ts, temperature-sensitive.


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