¹H, ¹³C and ¹⁵N resonance assignments of the kinetochore localisation domain of BUBR1, a central component of the spindle assembly checkpoint.
Human BUBR1 is a 120 kDa protein that plays a central role in the spindle assembly checkpoint (SAC), the evolutionary conserved and self-regulatory system of higher organisms that monitors and repairs defects in chromosome segregation in mitotic cells. BUBR1 is organised into several domains, with an N-terminal region responsible for its localisation into the kinetochore, the multi-component proteinaceous network that assembles onto chromosomes upon mitotic entry. We have expressed and purified uniformly-(15)N/(13)C N-terminal BUBR1 and assigned backbone and side-chain resonances bound to an unlabelled peptide from the protein Blinkin, an element essential for recruitment of BUBR1 to the kinetochore. These assignments provide insights on the Blinkin interaction interface and form the basis of the three-dimensional structure determination of a BUBR1-Blinkin complex.
Division of Molecular Biosciences, Department of Life Sciences, Imperial College London, Exhibition Rd., South Kensington, London SW7 2AZ, UK.
Peter J
PJ
Simpson
Ernesto
E
Cota
Victor M
VM
Bolanos-Garcia
D000595:Amino Acid Sequence; D001665:Binding Sites; D059447:Cell Cycle Checkpoints; D006801:Humans; D018386:Kinetochores / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000378:metabolism*; D021381:Protein Transport
C472643:Knl1 protein, human; D008869:Microtubule-Associated Proteins; C584277:BUB1 protein, human; C090464:Bub1 spindle checkpoint protein; D017346:Protein Serine-Threonine Kinases