Dresden 2011 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 33: Biological Machines \& Motor Proteins
BP 33.2: Vortrag
Freitag, 18. März 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 Gheber2,3 — 1Drittes 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.