Resonance assignments of the microtubule-binding domain of the C. elegans spindle and kinetochore-associated protein 1
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Author(s)
Boeszoermenyi, Andras
Cheeseman, Iain M
Oberer, Monika
Wagner, Gerhard
Arthanari, Haribabu
Schmidt, Jens Christopher
Date Issued
June 2013
Journal
Biomolecular NMR Assignments
Publisher
Springer Netherlands
Citation
Boeszoermenyi, Andras, Jens C. Schmidt, Iain M. Cheeseman, Monika Oberer, Gerhard Wagner, and Haribabu Arthanari. “Resonance Assignments of the Microtubule-Binding Domain of the C. Elegans Spindle and Kinetochore-Associated Protein 1.” Biomol NMR Assign 8, no. 2 (June 14, 2013): 275–278.
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Abstract
During mitosis, kinetochores coordinate the attachment of centromeric DNA to the dynamic plus ends of microtubules, which is hypothesized to pull sister chromatids toward opposing poles of the mitotic spindle. The outer kinetochore Ndc80 complex acts synergistically with the Ska (spindle and kinetochore-associated) complex to harness the energy of depolymerizing microtubules and power chromosome movement. The Ska complex is a hexamer consisting of two copies of the proteins Ska1, Ska2 and Ska3, respectively. The C-terminal domain of the spindle and kinetochore-associated protein 1 (Ska1) is the microtubule-binding domain of the Ska complex. We solved the solution structure of the C. elegans microtubule-binding domain (MTBD) of the protein Ska1 using NMR spectroscopy. Here, we report the resonance assignments of the MTBD of C. elegans Ska1.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1007/s12104-013-9499-x
