期刊
JOURNAL OF CELL BIOLOGY
卷 173, 期 6, 页码 867-877出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200603153
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- Medical Research Council [MC_U105184308, MC_U105184282] Funding Source: Medline
- MRC [MC_U105184308, MC_U105184282] Funding Source: UKRI
- Medical Research Council [MC_U105184308, MC_U105184282] Funding Source: researchfish
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 a 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. laments 60 nm long, compatible with all the S. 1 repeats as a continuous alpha helix. Immuno-EM localization of the Sfi1p N and C termini showed Sfi1p-centrin. laments 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.
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