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Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10

The centromere binding factor 3 (CBF3) complex binds the third centromere DNA element in organisms with point centromeres, such as S. cerevisiae. It is an essential complex for assembly of the kinetochore in these organisms, as it facilitates genetic centromere specification and allows association o...

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Detalles Bibliográficos
Autores principales: Zhang, Wenjuan, Lukoynova, Natalya, Miah, Shomon, Lucas, Jonathan, Vaughan, Cara K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6077249/
https://www.ncbi.nlm.nih.gov/pubmed/30021170
http://dx.doi.org/10.1016/j.celrep.2018.06.068
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author Zhang, Wenjuan
Lukoynova, Natalya
Miah, Shomon
Lucas, Jonathan
Vaughan, Cara K.
author_facet Zhang, Wenjuan
Lukoynova, Natalya
Miah, Shomon
Lucas, Jonathan
Vaughan, Cara K.
author_sort Zhang, Wenjuan
collection PubMed
description The centromere binding factor 3 (CBF3) complex binds the third centromere DNA element in organisms with point centromeres, such as S. cerevisiae. It is an essential complex for assembly of the kinetochore in these organisms, as it facilitates genetic centromere specification and allows association of all other kinetochore components. We determined high-resolution structures of the core complex of CBF3 alone and in association with a monomeric construct of Ndc10, using cryoelectron microscopy (cryo-EM). We identify the DNA-binding site of the complex and present a model in which CBF3 induces a tight bend in centromeric DNA, thus facilitating assembly of the centromeric nucleosome.
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spelling pubmed-60772492018-08-10 Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10 Zhang, Wenjuan Lukoynova, Natalya Miah, Shomon Lucas, Jonathan Vaughan, Cara K. Cell Rep Article The centromere binding factor 3 (CBF3) complex binds the third centromere DNA element in organisms with point centromeres, such as S. cerevisiae. It is an essential complex for assembly of the kinetochore in these organisms, as it facilitates genetic centromere specification and allows association of all other kinetochore components. We determined high-resolution structures of the core complex of CBF3 alone and in association with a monomeric construct of Ndc10, using cryoelectron microscopy (cryo-EM). We identify the DNA-binding site of the complex and present a model in which CBF3 induces a tight bend in centromeric DNA, thus facilitating assembly of the centromeric nucleosome. Cell Press 2018-07-17 /pmc/articles/PMC6077249/ /pubmed/30021170 http://dx.doi.org/10.1016/j.celrep.2018.06.068 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Wenjuan
Lukoynova, Natalya
Miah, Shomon
Lucas, Jonathan
Vaughan, Cara K.
Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10
title Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10
title_full Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10
title_fullStr Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10
title_full_unstemmed Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10
title_short Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10
title_sort insights into centromere dna bending revealed by the cryo-em structure of the core centromere binding factor 3 with ndc10
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6077249/
https://www.ncbi.nlm.nih.gov/pubmed/30021170
http://dx.doi.org/10.1016/j.celrep.2018.06.068
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