As the microtubule-organizing center of yeast, the spindle pole body (SPB) is essential for cell viability. Structural studies of the SPB are limited by its low copy number in the cell, its large size and heterogeneous composition, and its association with the nuclear membrane. However, low-resolution or indirect structural information about the SPB may be deciphered through a variety of techniques. Interestingly, a large proportion of SPB proteins are predicted to contain one or more coiled coils, a common protein interaction motif. The high frequency of coiled coils suggests that this structure is important for establishing the overall architecture of the complex. Support for this hypothesis was reported previously for coiled coils from some SPB proteins. Here, we extend this approach of isolating and characterizing additional SPB coiled coils to improve our understanding of SPB structure and organization. Self-associating coiled coils from Bbp1, Mps2, and Nbp1 were observed to form stable parallel homodimers in solution. Coiled-coil peptides from Bbp1 and Mps2 were also observed to hetero-associate. Experimental coiled-coil interaction data from this work and previous studies, as well as predicted and experimental structures for other SPB protein fragments and domains, were integrated to generate a model of the SPB structure.
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