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The unconventional kinetoplastid kinetochore: from discovery toward functional understanding

The kinetochore is the macromolecular protein complex that drives chromosome segregation in eukaryotes. Its most fundamental function is to connect centromeric DNA to dynamic spindle microtubules. Studies in popular model eukaryotes have shown that centromere protein (CENP)-A is critical for DNA-bin...

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Autor principal: Akiyoshi, Bungo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5095916/
https://www.ncbi.nlm.nih.gov/pubmed/27911702
http://dx.doi.org/10.1042/BST20160112
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author Akiyoshi, Bungo
author_facet Akiyoshi, Bungo
author_sort Akiyoshi, Bungo
collection PubMed
description The kinetochore is the macromolecular protein complex that drives chromosome segregation in eukaryotes. Its most fundamental function is to connect centromeric DNA to dynamic spindle microtubules. Studies in popular model eukaryotes have shown that centromere protein (CENP)-A is critical for DNA-binding, whereas the Ndc80 complex is essential for microtubule-binding. Given their conservation in diverse eukaryotes, it was widely believed that all eukaryotes would utilize these components to make up a core of the kinetochore. However, a recent study identified an unconventional type of kinetochore in evolutionarily distant kinetoplastid species, showing that chromosome segregation can be achieved using a distinct set of proteins. Here, I review the discovery of the two kinetochore systems and discuss how their studies contribute to a better understanding of the eukaryotic chromosome segregation machinery.
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spelling pubmed-50959162016-11-08 The unconventional kinetoplastid kinetochore: from discovery toward functional understanding Akiyoshi, Bungo Biochem Soc Trans Biochemical Society Awards The kinetochore is the macromolecular protein complex that drives chromosome segregation in eukaryotes. Its most fundamental function is to connect centromeric DNA to dynamic spindle microtubules. Studies in popular model eukaryotes have shown that centromere protein (CENP)-A is critical for DNA-binding, whereas the Ndc80 complex is essential for microtubule-binding. Given their conservation in diverse eukaryotes, it was widely believed that all eukaryotes would utilize these components to make up a core of the kinetochore. However, a recent study identified an unconventional type of kinetochore in evolutionarily distant kinetoplastid species, showing that chromosome segregation can be achieved using a distinct set of proteins. Here, I review the discovery of the two kinetochore systems and discuss how their studies contribute to a better understanding of the eukaryotic chromosome segregation machinery. Portland Press Ltd. 2016-10-15 2016-10-19 /pmc/articles/PMC5095916/ /pubmed/27911702 http://dx.doi.org/10.1042/BST20160112 Text en © 2016 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0) .
spellingShingle Biochemical Society Awards
Akiyoshi, Bungo
The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
title The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
title_full The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
title_fullStr The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
title_full_unstemmed The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
title_short The unconventional kinetoplastid kinetochore: from discovery toward functional understanding
title_sort unconventional kinetoplastid kinetochore: from discovery toward functional understanding
topic Biochemical Society Awards
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5095916/
https://www.ncbi.nlm.nih.gov/pubmed/27911702
http://dx.doi.org/10.1042/BST20160112
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