DOI: 10.1091/mbc.e05-03-0214. The Organization of the Core Proteins of the Yeast Spindle Pole Body

The Organization of the Core Proteins of the Yeast Spindle Pole Body

10.1091/mbc.e05-03-0214

Crossref journal-article

American Society for Cell Biology (ASCB)

Molecular Biology of the Cell (1076)

Abstract

The spindle pole body (SPB) is the microtubule organizing center of Saccharomyces cerevisiae. Its core includes the proteins Spc42, Spc110 (kendrin/pericentrin ortholog), calmodulin (Cmd1), Spc29, and Cnm67. Each was tagged with CFP and YFP and their proximity to each other was determined by fluorescence resonance energy transfer (FRET). FRET was measured by a new metric that accurately reflected the relative extent of energy transfer. The FRET values established the topology of the core proteins within the architecture of SPB. The N-termini of Spc42 and Spc29, and the C-termini of all the core proteins face the gap between the IL2 layer and the central plaque. Spc110 traverses the central plaque and Cnm67 spans the IL2 layer. Spc42 is a central component of the central plaque where its N-terminus is closely associated with the C-termini of Spc29, Cmd1, and Spc110. When the donor-acceptor pairs were ordered into five broad categories of increasing FRET, the ranking of the pairs specified a unique geometry for the positions of the core proteins, as shown by a mathematical proof. The geometry was integrated with prior cryoelectron tomography to create a model of the interwoven network of proteins within the central plaque. One prediction of the model, the dimerization of the calmodulin-binding domains of Spc110, was confirmed by in vitro analysis.

Bibliography

Muller, E. G. D., Snydsman, B. E., Novik, I., Hailey, D. W., Gestaut, D. R., Niemann, C. A., OâToole, E. T., Giddings, T. H., Sundin, B. A., & Davis, T. N. (2005). The Organization of the Core Proteins of the Yeast Spindle Pole Body. Molecular Biology of the Cell, 16(7), 3341â3352.

Authors 10

Eric G.D. Muller (first)
Brian E. Snydsman (additional)
Isabella Novik (additional)
Dale W. Hailey (additional)
Daniel R. Gestaut (additional)
Christine A. Niemann (additional)
Eileen T. O'Toole (additional)
Tom H. Giddings (additional)
Bryan A. Sundin (additional)
Trisha N. Davis (additional)

References 32 Referenced 113

Dates

Type	When
Created	20 years, 3 months ago (May 4, 2005, 8:33 p.m.)
Deposited	4 years, 1 month ago (July 10, 2021, 11:44 a.m.)
Indexed	1 year ago (Aug. 4, 2024, 12:31 a.m.)
Issued	20 years, 2 months ago (July 1, 2005)
Published	20 years, 2 months ago (July 1, 2005)
Published Print	20 years, 2 months ago (July 1, 2005)

Funders 0

None

BibTeX

@article{Muller_2005, title={The Organization of the Core Proteins of the Yeast Spindle Pole Body}, volume={16}, ISSN={1939-4586}, url={http://dx.doi.org/10.1091/mbc.e05-03-0214}, DOI={10.1091/mbc.e05-03-0214}, number={7}, journal={Molecular Biology of the Cell}, publisher={American Society for Cell Biology (ASCB)}, author={Muller, Eric G.D. and Snydsman, Brian E. and Novik, Isabella and Hailey, Dale W. and Gestaut, Daniel R. and Niemann, Christine A. and O’Toole, Eileen T. and Giddings, Tom H. and Sundin, Bryan A. and Davis, Trisha N.}, year={2005}, month=jul, pages={3341–3352} }

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  "abstract": "<jats:p>The spindle pole body (SPB) is the microtubule organizing center of Saccharomyces cerevisiae. Its core includes the proteins Spc42, Spc110 (kendrin/pericentrin ortholog), calmodulin (Cmd1), Spc29, and Cnm67. Each was tagged with CFP and YFP and their proximity to each other was determined by fluorescence resonance energy transfer (FRET). FRET was measured by a new metric that accurately reflected the relative extent of energy transfer. The FRET values established the topology of the core proteins within the architecture of SPB. The N-termini of Spc42 and Spc29, and the C-termini of all the core proteins face the gap between the IL2 layer and the central plaque. Spc110 traverses the central plaque and Cnm67 spans the IL2 layer. Spc42 is a central component of the central plaque where its N-terminus is closely associated with the C-termini of Spc29, Cmd1, and Spc110. When the donor-acceptor pairs were ordered into five broad categories of increasing FRET, the ranking of the pairs specified a unique geometry for the positions of the core proteins, as shown by a mathematical proof. The geometry was integrated with prior cryoelectron tomography to create a model of the interwoven network of proteins within the central plaque. One prediction of the model, the dimerization of the calmodulin-binding domains of Spc110, was confirmed by in vitro analysis.</jats:p>",
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