The bipolar assembly domain of the mitotic motor kinesin-5
Copyright policy )The bipolar assembly domain of the mitotic motor kinesin-5
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.
- Pacific Northwest National Laboratory United States
- University of California, Davis United States
- University of California United States
- University of Mississippi Medical Center United States
Structure-Activity Relationship (mesh), Cysteine (mesh), Mass Spectrometry (mesh), Mitosis (mesh), Mass Spectrometry, Drosophila Proteins (mesh), Animals (mesh), Drosophila Proteins, Native Polyacrylamide Gel Electrophoresis (mesh), Mutation (mesh), Drosophila melanogaster (mesh), Biological Sciences, Native Polyacrylamide Gel Electrophoresis, Drosophila melanogaster, Nanoparticles (mesh), Hydrodynamics (mesh), Microtubule-Associated Proteins, 570, Protein Structure, 1.1 Normal biological development and functioning, 34 Chemical Sciences (for-2020), Mitosis, 612, Mutant Proteins (mesh), Electron Spin Resonance Spectroscopy (mesh), Article, Structure-Activity Relationship, Animals, Cysteine, Structural Homology, 1.1 Normal biological development and functioning (hrcs-rac), 31 Biological Sciences (for-2020), Molecular Weight (mesh), Protein, Electron Spin Resonance Spectroscopy, Protein Multimerization (mesh), Microtubule-Associated Proteins (mesh), 3101 Biochemistry and Cell Biology (for-2020), Protein Structure, Tertiary, Tertiary (mesh), Molecular Weight, Structural Homology, Protein, Chemical Sciences, Mutation, Hydrodynamics, Nanoparticles, Mutant Proteins, Biochemistry and Cell Biology, Protein Multimerization, Protein (mesh), Tertiary
Structure-Activity Relationship (mesh), Cysteine (mesh), Mass Spectrometry (mesh), Mitosis (mesh), Mass Spectrometry, Drosophila Proteins (mesh), Animals (mesh), Drosophila Proteins, Native Polyacrylamide Gel Electrophoresis (mesh), Mutation (mesh), Drosophila melanogaster (mesh), Biological Sciences, Native Polyacrylamide Gel Electrophoresis, Drosophila melanogaster, Nanoparticles (mesh), Hydrodynamics (mesh), Microtubule-Associated Proteins, 570, Protein Structure, 1.1 Normal biological development and functioning, 34 Chemical Sciences (for-2020), Mitosis, 612, Mutant Proteins (mesh), Electron Spin Resonance Spectroscopy (mesh), Article, Structure-Activity Relationship, Animals, Cysteine, Structural Homology, 1.1 Normal biological development and functioning (hrcs-rac), 31 Biological Sciences (for-2020), Molecular Weight (mesh), Protein, Electron Spin Resonance Spectroscopy, Protein Multimerization (mesh), Microtubule-Associated Proteins (mesh), 3101 Biochemistry and Cell Biology (for-2020), Protein Structure, Tertiary, Tertiary (mesh), Molecular Weight, Structural Homology, Protein, Chemical Sciences, Mutation, Hydrodynamics, Nanoparticles, Mutant Proteins, Biochemistry and Cell Biology, Protein Multimerization, Protein (mesh), Tertiary
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