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The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes
The kinetochore is a large, macromolecular assembly that is essential for connecting chromosomes to microtubules during mitosis. Despite the recent identification of multiple kinetochore components, the nature and organization of the higher-order kinetochore structure remain unknown. The outer kinet...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4294671/ https://www.ncbi.nlm.nih.gov/pubmed/25411336 http://dx.doi.org/10.1091/mbc.E14-06-1125 |
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author | Kern, David M. Kim, Taekyung Rigney, Mike Hattersley, Neil Desai, Arshad Cheeseman, Iain M. |
author_facet | Kern, David M. Kim, Taekyung Rigney, Mike Hattersley, Neil Desai, Arshad Cheeseman, Iain M. |
author_sort | Kern, David M. |
collection | PubMed |
description | The kinetochore is a large, macromolecular assembly that is essential for connecting chromosomes to microtubules during mitosis. Despite the recent identification of multiple kinetochore components, the nature and organization of the higher-order kinetochore structure remain unknown. The outer kinetochore KNL-1/Mis12 complex/Ndc80 complex (KMN) network plays a key role in generating and sensing microtubule attachments. Here we demonstrate that Caenorhabditis elegans KNL-1 exists as an oligomer, and we identify a specific domain in KNL-1 responsible for this activity. An N-terminal KNL-1 domain from both C. elegans and the related nematode Caenorhabditis remanei oligomerizes into a decameric assembly that appears roughly circular when visualized by electron microscopy. On the basis of sequence and mutational analysis, we identify a small hydrophobic region as responsible for this oligomerization activity. However, mutants that precisely disrupt KNL-1 oligomerization did not alter KNL-1 localization or result in the loss of embryonic viability based on gene replacements in C. elegans. In C. elegans, KNL-1 oligomerization may coordinate with other kinetochore activities to ensure the proper organization, function, and sensory capabilities of the kinetochore–microtubule attachment. |
format | Online Article Text |
id | pubmed-4294671 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42946712015-03-30 The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes Kern, David M. Kim, Taekyung Rigney, Mike Hattersley, Neil Desai, Arshad Cheeseman, Iain M. Mol Biol Cell Articles The kinetochore is a large, macromolecular assembly that is essential for connecting chromosomes to microtubules during mitosis. Despite the recent identification of multiple kinetochore components, the nature and organization of the higher-order kinetochore structure remain unknown. The outer kinetochore KNL-1/Mis12 complex/Ndc80 complex (KMN) network plays a key role in generating and sensing microtubule attachments. Here we demonstrate that Caenorhabditis elegans KNL-1 exists as an oligomer, and we identify a specific domain in KNL-1 responsible for this activity. An N-terminal KNL-1 domain from both C. elegans and the related nematode Caenorhabditis remanei oligomerizes into a decameric assembly that appears roughly circular when visualized by electron microscopy. On the basis of sequence and mutational analysis, we identify a small hydrophobic region as responsible for this oligomerization activity. However, mutants that precisely disrupt KNL-1 oligomerization did not alter KNL-1 localization or result in the loss of embryonic viability based on gene replacements in C. elegans. In C. elegans, KNL-1 oligomerization may coordinate with other kinetochore activities to ensure the proper organization, function, and sensory capabilities of the kinetochore–microtubule attachment. The American Society for Cell Biology 2015-01-15 /pmc/articles/PMC4294671/ /pubmed/25411336 http://dx.doi.org/10.1091/mbc.E14-06-1125 Text en © 2015 Kern et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Kern, David M. Kim, Taekyung Rigney, Mike Hattersley, Neil Desai, Arshad Cheeseman, Iain M. The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes |
title | The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes |
title_full | The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes |
title_fullStr | The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes |
title_full_unstemmed | The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes |
title_short | The outer kinetochore protein KNL-1 contains a defined oligomerization domain in nematodes |
title_sort | outer kinetochore protein knl-1 contains a defined oligomerization domain in nematodes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4294671/ https://www.ncbi.nlm.nih.gov/pubmed/25411336 http://dx.doi.org/10.1091/mbc.E14-06-1125 |
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