Cargando…
Dynamics of inner kinetochore assembly and maintenance in living cells
To investigate the dynamics of centromere organization, we have assessed the exchange rates of inner centromere proteins (CENPs) by quantitative microscopy throughout the cell cycle in human cells. CENP-A and CENP-I are stable centromere components that are incorporated into centromeres via a “loadi...
Autores principales: | , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2290840/ https://www.ncbi.nlm.nih.gov/pubmed/18347072 http://dx.doi.org/10.1083/jcb.200710052 |
_version_ | 1782152379139883008 |
---|---|
author | Hemmerich, Peter Weidtkamp-Peters, Stefanie Hoischen, Christian Schmiedeberg, Lars Erliandri, Indri Diekmann, Stephan |
author_facet | Hemmerich, Peter Weidtkamp-Peters, Stefanie Hoischen, Christian Schmiedeberg, Lars Erliandri, Indri Diekmann, Stephan |
author_sort | Hemmerich, Peter |
collection | PubMed |
description | To investigate the dynamics of centromere organization, we have assessed the exchange rates of inner centromere proteins (CENPs) by quantitative microscopy throughout the cell cycle in human cells. CENP-A and CENP-I are stable centromere components that are incorporated into centromeres via a “loading-only” mechanism in G1 and S phase, respectively. A subfraction of CENP-H also stays stably bound to centromeres. In contrast, CENP-B, CENP-C, and some CENP-H and hMis12 exhibit distinct and cell cycle–specific centromere binding stabilities, with residence times ranging from seconds to hours. CENP-C and CENP-H are immobilized at centromeres specifically during replication. In mitosis, all inner CENPs become completely immobilized. CENPs are highly mobile throughout bulk chromatin, which is consistent with a binding-diffusion behavior as the mechanism to scan for vacant high-affinity binding sites at centromeres. Our data reveal a wide range of cell cycle–specific assembly plasticity of the centromere that provides both stability through sustained binding of some components and flexibility through dynamic exchange of other components. |
format | Text |
id | pubmed-2290840 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22908402008-09-24 Dynamics of inner kinetochore assembly and maintenance in living cells Hemmerich, Peter Weidtkamp-Peters, Stefanie Hoischen, Christian Schmiedeberg, Lars Erliandri, Indri Diekmann, Stephan J Cell Biol Research Articles To investigate the dynamics of centromere organization, we have assessed the exchange rates of inner centromere proteins (CENPs) by quantitative microscopy throughout the cell cycle in human cells. CENP-A and CENP-I are stable centromere components that are incorporated into centromeres via a “loading-only” mechanism in G1 and S phase, respectively. A subfraction of CENP-H also stays stably bound to centromeres. In contrast, CENP-B, CENP-C, and some CENP-H and hMis12 exhibit distinct and cell cycle–specific centromere binding stabilities, with residence times ranging from seconds to hours. CENP-C and CENP-H are immobilized at centromeres specifically during replication. In mitosis, all inner CENPs become completely immobilized. CENPs are highly mobile throughout bulk chromatin, which is consistent with a binding-diffusion behavior as the mechanism to scan for vacant high-affinity binding sites at centromeres. Our data reveal a wide range of cell cycle–specific assembly plasticity of the centromere that provides both stability through sustained binding of some components and flexibility through dynamic exchange of other components. The Rockefeller University Press 2008-03-24 /pmc/articles/PMC2290840/ /pubmed/18347072 http://dx.doi.org/10.1083/jcb.200710052 Text en Copyright © 2008, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Hemmerich, Peter Weidtkamp-Peters, Stefanie Hoischen, Christian Schmiedeberg, Lars Erliandri, Indri Diekmann, Stephan Dynamics of inner kinetochore assembly and maintenance in living cells |
title | Dynamics of inner kinetochore assembly and maintenance in living cells |
title_full | Dynamics of inner kinetochore assembly and maintenance in living cells |
title_fullStr | Dynamics of inner kinetochore assembly and maintenance in living cells |
title_full_unstemmed | Dynamics of inner kinetochore assembly and maintenance in living cells |
title_short | Dynamics of inner kinetochore assembly and maintenance in living cells |
title_sort | dynamics of inner kinetochore assembly and maintenance in living cells |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2290840/ https://www.ncbi.nlm.nih.gov/pubmed/18347072 http://dx.doi.org/10.1083/jcb.200710052 |
work_keys_str_mv | AT hemmerichpeter dynamicsofinnerkinetochoreassemblyandmaintenanceinlivingcells AT weidtkamppetersstefanie dynamicsofinnerkinetochoreassemblyandmaintenanceinlivingcells AT hoischenchristian dynamicsofinnerkinetochoreassemblyandmaintenanceinlivingcells AT schmiedeberglars dynamicsofinnerkinetochoreassemblyandmaintenanceinlivingcells AT erliandriindri dynamicsofinnerkinetochoreassemblyandmaintenanceinlivingcells AT diekmannstephan dynamicsofinnerkinetochoreassemblyandmaintenanceinlivingcells |