TY - JOUR
T1 - The bipolar assembly domain of the mitotic motor kinesin-5
AU - Acar, Seyda
AU - Carlson, David B.
AU - Budamagunta, Madhu S.
AU - Yarov-Yarovoy, Vladimir
AU - Correia, John J.
AU - Niñonuevo, Milady R.
AU - Jia, Weitao
AU - Tao, Li
AU - Leary, Julie A.
AU - Voss, John C
AU - Evans, James E.
AU - Scholey, Jonathan M.
PY - 2013
Y1 - 2013
N2 - An outstanding unresolved question is how does the mitotic spindle utilize microtubules and mitotic motors to coordinate accurate chromosome segregation during mitosis? This process depends upon the mitotic motor, kinesin-5, whose unique bipolar architecture, with pairs of motor domains lying at opposite ends of a central rod, allows it to crosslink microtubules within the mitotic spindle and to coordinate their relative sliding during spindle assembly, maintenance and elongation. The structural basis of kinesin-5's bipolarity is, however, unknown, as protein asymmetry has so far precluded its crystallization. Here we use electron microscopy of single molecules of kinesin-5 and its subfragments, combined with hydrodynamic analysis plus mass spectrometry, circular dichroism and site-directed spin label electron paramagnetic resonance spectroscopy, to show how a staggered antiparallel coiled-coil 'BASS' (bipolar assembly) domain directs the assembly of four kinesin-5 polypeptides into bipolar minifilaments.
AB - An outstanding unresolved question is how does the mitotic spindle utilize microtubules and mitotic motors to coordinate accurate chromosome segregation during mitosis? This process depends upon the mitotic motor, kinesin-5, whose unique bipolar architecture, with pairs of motor domains lying at opposite ends of a central rod, allows it to crosslink microtubules within the mitotic spindle and to coordinate their relative sliding during spindle assembly, maintenance and elongation. The structural basis of kinesin-5's bipolarity is, however, unknown, as protein asymmetry has so far precluded its crystallization. Here we use electron microscopy of single molecules of kinesin-5 and its subfragments, combined with hydrodynamic analysis plus mass spectrometry, circular dichroism and site-directed spin label electron paramagnetic resonance spectroscopy, to show how a staggered antiparallel coiled-coil 'BASS' (bipolar assembly) domain directs the assembly of four kinesin-5 polypeptides into bipolar minifilaments.
UR - http://www.scopus.com/inward/record.url?scp=84879168530&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84879168530&partnerID=8YFLogxK
U2 - 10.1038/ncomms2348
DO - 10.1038/ncomms2348
M3 - Article
C2 - 23299893
AN - SCOPUS:84879168530
VL - 4
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 1343
ER -