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Dresden 2011 – scientific programme

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BP: Fachverband Biologische Physik

BP 33: Biological Machines \& Motor Proteins

BP 33.2: Talk

Friday, March 18, 2011, 10:45–11:00, ZEU 250

Exceptional in vitro and in vivo motility of the S. cerevisiae Kinesin-5 Cin8 — •Christina Thiede1, Adina Gerson-Gurwitz2, Natalia Movshovich2, Vladimir Fridman3, Maria Podolskaya3, Tsafi Danieli4, Stefan Lakämper1, Christoph F. Schmidt1, and Larisa Gheber2,31Drittes Physikalisches Institut, Georg-August-Universität Göttingen, Göttingen, Germany — 2Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel — 3Department of Clinical Biochemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel — 4Protein Expression Facility, Wolfson Centre for Applied Structural Biology, Hebrew University of Jerusalem, Jerusalem, Israel

Members of the conserved Kinesin-5 family fulfill essential roles in mitotic spindle morphogenesis and dynamics. The mechanisms that regulate Kinesin-5 function are not well understood. In this study, we have examined in vitro and in vivo functions and regulation of the Saccharomyces cerevisiae Kinesin-5 Cin8. Using in vitro single-molecule fluorescence motility assay in whole-cell extracts, we found that Cin8 motility is exceptional in the Kinesin-5 family. In high salt, Cin8 moved fast along microtubules (∼ 22 µm/min) for a Kinesin-5. In low salt, Cin8 was slower and moved more diffusively. We further found that a unique 99 amino acid insert, located in the Cin8 motor domain, increased Cin8 binding to microtubules, affected its motile properties and in vivo controlled its localization and function during anaphase spindle elongation.

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