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Biochemical evidence for diverse strategies in the inner kinetochore
The kinetochore is a complex structure whose function is absolutely essential. Unlike the centromere, the kinetochore at first appeared remarkably well conserved from yeast to humans, especially the microtubule-binding outer kinetochore. However, recent efforts towards biochemical reconstitution of...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7729030/ https://www.ncbi.nlm.nih.gov/pubmed/33202170 http://dx.doi.org/10.1098/rsob.200284 |
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author | Hamilton, G. E. Davis, T. N. |
author_facet | Hamilton, G. E. Davis, T. N. |
author_sort | Hamilton, G. E. |
collection | PubMed |
description | The kinetochore is a complex structure whose function is absolutely essential. Unlike the centromere, the kinetochore at first appeared remarkably well conserved from yeast to humans, especially the microtubule-binding outer kinetochore. However, recent efforts towards biochemical reconstitution of diverse kinetochores challenge the notion of a similarly conserved architecture for the constitutively centromere-associated network of the inner kinetochore. This review briefly summarizes the evidence from comparative genomics for interspecific variability in inner kinetochore composition and focuses on novel biochemical evidence indicating that even homologous inner kinetochore protein complexes are put to different uses in different organisms. |
format | Online Article Text |
id | pubmed-7729030 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-77290302020-12-11 Biochemical evidence for diverse strategies in the inner kinetochore Hamilton, G. E. Davis, T. N. Open Biol Review The kinetochore is a complex structure whose function is absolutely essential. Unlike the centromere, the kinetochore at first appeared remarkably well conserved from yeast to humans, especially the microtubule-binding outer kinetochore. However, recent efforts towards biochemical reconstitution of diverse kinetochores challenge the notion of a similarly conserved architecture for the constitutively centromere-associated network of the inner kinetochore. This review briefly summarizes the evidence from comparative genomics for interspecific variability in inner kinetochore composition and focuses on novel biochemical evidence indicating that even homologous inner kinetochore protein complexes are put to different uses in different organisms. The Royal Society 2020-11-18 /pmc/articles/PMC7729030/ /pubmed/33202170 http://dx.doi.org/10.1098/rsob.200284 Text en © 2020 The Authors. http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Review Hamilton, G. E. Davis, T. N. Biochemical evidence for diverse strategies in the inner kinetochore |
title | Biochemical evidence for diverse strategies in the inner kinetochore |
title_full | Biochemical evidence for diverse strategies in the inner kinetochore |
title_fullStr | Biochemical evidence for diverse strategies in the inner kinetochore |
title_full_unstemmed | Biochemical evidence for diverse strategies in the inner kinetochore |
title_short | Biochemical evidence for diverse strategies in the inner kinetochore |
title_sort | biochemical evidence for diverse strategies in the inner kinetochore |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7729030/ https://www.ncbi.nlm.nih.gov/pubmed/33202170 http://dx.doi.org/10.1098/rsob.200284 |
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