The Crystal Structure of the N-Terminal Region of BUB1 Provides Insight into the Mechanism of BUB1 Recruitment to Kinetochores
The interaction of the central mitotic checkpoint component BUB1 with the mitotic kinetochore protein Blinkin is required for the kinetochore localization and function of BUB1 in the mitotic spindle assembly checkpoint, the regulatory mechanism of the cell cycle that ensures the even distribution of...
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Published in | Structure (London) Vol. 17; no. 1; pp. 105 - 116 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
14.01.2009
Cell Press |
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Abstract | The interaction of the central mitotic checkpoint component BUB1 with the mitotic kinetochore protein Blinkin is required for the kinetochore localization and function of BUB1 in the mitotic spindle assembly checkpoint, the regulatory mechanism of the cell cycle that ensures the even distribution of chromosomes during the transition from metaphase to anaphase. Here, we report the 1.74 Å resolution crystal structure of the N-terminal region of BUB1. The structure is organized as a tandem arrangement of three divergent units of the tetratricopeptide motif. Functional assays in vivo of native and site-specific mutants identify the residues of human BUB1 important for the interaction with Blinkin and define one region of potential therapeutic interest. The structure provides insight into the molecular basis of Blinkin-specific recognition by BUB1 and, on a broader perspective, of the mechanism that mediates kinetochore localization of BUB1 in checkpoint-activated cells. |
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AbstractList | The interaction of the central mitotic checkpoint component BUB1 with the mitotic kinetochore protein Blinkin is required for the kinetochore localization and function of BUB1 in the mitotic spindle assembly checkpoint, the regulatory mechanism of the cell cycle that ensures the even distribution of chromosomes during the transition from metaphase to anaphase. Here, we report the 1.74 A resolution crystal structure of the N-terminal region of BUB1. The structure is organized as a tandem arrangement of three divergent units of the tetratricopeptide motif. Functional assays in vivo of native and site-specific mutants identify the residues of human BUB1 important for the interaction with Blinkin and define one region of potential therapeutic interest. The structure provides insight into the molecular basis of Blinkin-specific recognition by BUB1 and, on a broader perspective, of the mechanism that mediates kinetochore localization of BUB1 in checkpoint-activated cells. The interaction of the central mitotic checkpoint component BUB1 with the mitotic kinetochore protein Blinkin is required for the kinetochore localization and function of BUB1 in the mitotic spindle assembly checkpoint, the regulatory mechanism of the cell cycle that ensures the even distribution of chromosomes during the transition from metaphase to anaphase. Here, we report the 1.74 Å resolution crystal structure of the N-terminal region of BUB1. The structure is organized as a tandem arrangement of three divergent units of the tetratricopeptide motif. Functional assays in vivo of native and site-specific mutants identify the residues of human BUB1 important for the interaction with Blinkin and define one region of potential therapeutic interest. The structure provides insight into the molecular basis of Blinkin-specific recognition by BUB1 and, on a broader perspective, of the mechanism that mediates kinetochore localization of BUB1 in checkpoint-activated cells. The interaction of the central mitotic checkpoint component BUB1 with the mitotic kinetochore protein Blinkin is required for the kinetochore localization and function of BUB1 in the mitotic spindle assembly checkpoint, the regulatory mechanism of the cell cycle that ensures the even distribution of chromosomes during the transition from metaphase to anaphase. Here, we report the 1.74 angstroms resolution crystal structure of the N-terminal region of BUB1. The structure is organized as a tandem arrangement of three divergent units of the tetratricopeptide motif. Functional assays in vivo of native and site-specific mutants identify the residues of human BUB1 important for the interaction with Blinkin and define one region of potential therapeutic interest. The structure provides insight into the molecular basis of Blinkin-specific recognition by BUB1 and, on a broader perspective, of the mechanism that mediates kinetochore localization of BUB1 in checkpoint-activated cells. |
Author | Bolanos-Garcia, Victor M. D'Arcy, Sheena Grossmann, J. Günter Kiyomitsu, Tomomi Chirgadze, Dimitri Y. Yanagida, Mitsuhiro Blundell, Tom L. Robinson, Carol V. Matak-Vinkovic, Dijana Venkitaraman, Ashok R. |
AuthorAffiliation | 2 CREST Research Program JST, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan 5 Hutchison/MRC Research Centre, Cambridge CB2 0XZ, UK 1 Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK 3 Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, UK 4 Department of Chemistry, University of Cambridge, Cambridge, UK |
AuthorAffiliation_xml | – name: 1 Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK – name: 5 Hutchison/MRC Research Centre, Cambridge CB2 0XZ, UK – name: 3 Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, UK – name: 2 CREST Research Program JST, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan – name: 4 Department of Chemistry, University of Cambridge, Cambridge, UK |
Author_xml | – sequence: 1 givenname: Victor M. surname: Bolanos-Garcia fullname: Bolanos-Garcia, Victor M. email: victor@cryst.bioc.cam.ac.uk organization: Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK – sequence: 2 givenname: Tomomi surname: Kiyomitsu fullname: Kiyomitsu, Tomomi organization: CREST Research Program JST, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan – sequence: 3 givenname: Sheena surname: D'Arcy fullname: D'Arcy, Sheena organization: Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK – sequence: 4 givenname: Dimitri Y. surname: Chirgadze fullname: Chirgadze, Dimitri Y. organization: Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK – sequence: 5 givenname: J. Günter surname: Grossmann fullname: Grossmann, J. Günter organization: Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, UK – sequence: 6 givenname: Dijana surname: Matak-Vinkovic fullname: Matak-Vinkovic, Dijana organization: Department of Chemistry, University of Cambridge, Cambridge, UK – sequence: 7 givenname: Ashok R. surname: Venkitaraman fullname: Venkitaraman, Ashok R. organization: Hutchison/MRC Research Centre, Cambridge CB2 0XZ, UK – sequence: 8 givenname: Mitsuhiro surname: Yanagida fullname: Yanagida, Mitsuhiro organization: CREST Research Program JST, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan – sequence: 9 givenname: Carol V. surname: Robinson fullname: Robinson, Carol V. organization: Department of Chemistry, University of Cambridge, Cambridge, UK – sequence: 10 givenname: Tom L. surname: Blundell fullname: Blundell, Tom L. organization: Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK |
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SubjectTerms | Amino Acid Sequence CELLBIO Crystallography, X-Ray Kinetochores - metabolism Models, Molecular Molecular Sequence Data Mutation Protein Conformation Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism PROTEINS Sequence Homology, Amino Acid |
Title | The Crystal Structure of the N-Terminal Region of BUB1 Provides Insight into the Mechanism of BUB1 Recruitment to Kinetochores |
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