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A CENP-S/X complex assembles at the centromere in S and G2 phases of the human cell cycle.

Dornblut, Carsten ; Quinn, Nadine ; Monajambashi, Shamci ; Prendergast, Lisa ; van Vuuren, Chelly ; Münch, Sandra ; Deng, Wen ; Leonhardt, Heinrich ; Cardoso, M. Cristina ; Hoischen, Christian ; Diekmann, Stephan ; Sullivan, Kevin F. (2014)
A CENP-S/X complex assembles at the centromere in S and G2 phases of the human cell cycle.
In: Open biology, 4
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

The functional identity of centromeres arises from a set of specific nucleoprotein particle subunits of the centromeric chromatin fibre. These include CENP-A and histone H3 nucleosomes and a novel nucleosome-like complex of CENPs -T, -W, -S and -X. Fluorescence cross-correlation spectroscopy and Förster resonance energy transfer (FRET) revealed that human CENP-S and -X exist principally in complex in soluble form and retain proximity when assembled at centromeres. Conditional labelling experiments show that they both assemble de novo during S phase and G2, increasing approximately three- to fourfold in abundance at centromeres. Fluorescence recovery after photobleaching (FRAP) measurements documented steady-state exchange between soluble and assembled pools, with CENP-X exchanging approximately 10 times faster than CENP-S (t1/2 ∼ 10 min versus 120 min). CENP-S binding to sites of DNA damage was quite distinct, with a FRAP half-time of approximately 160 s. Fluorescent two-hybrid analysis identified CENP-T as a uniquely strong CENP-S binding protein and this association was confirmed by FRET, revealing a centromere-bound complex containing CENP-S, CENP-X and CENP-T in proximity to histone H3 but not CENP-A. We propose that deposition of the CENP-T/W/S/X particle reveals a kinetochore-specific chromatin assembly pathway that functions to switch centromeric chromatin to a mitosis-competent state after DNA replication. Centromeres shuttle between CENP-A-rich, replication-competent and H3-CENP-T/W/S/X-rich mitosis-competent compositions in the cell cycle.

Typ des Eintrags: Artikel
Erschienen: 2014
Autor(en): Dornblut, Carsten ; Quinn, Nadine ; Monajambashi, Shamci ; Prendergast, Lisa ; van Vuuren, Chelly ; Münch, Sandra ; Deng, Wen ; Leonhardt, Heinrich ; Cardoso, M. Cristina ; Hoischen, Christian ; Diekmann, Stephan ; Sullivan, Kevin F.
Art des Eintrags: Bibliographie
Titel: A CENP-S/X complex assembles at the centromere in S and G2 phases of the human cell cycle.
Sprache: Englisch
Publikationsjahr: 2014
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Open biology
Jahrgang/Volume einer Zeitschrift: 4
Kurzbeschreibung (Abstract):

The functional identity of centromeres arises from a set of specific nucleoprotein particle subunits of the centromeric chromatin fibre. These include CENP-A and histone H3 nucleosomes and a novel nucleosome-like complex of CENPs -T, -W, -S and -X. Fluorescence cross-correlation spectroscopy and Förster resonance energy transfer (FRET) revealed that human CENP-S and -X exist principally in complex in soluble form and retain proximity when assembled at centromeres. Conditional labelling experiments show that they both assemble de novo during S phase and G2, increasing approximately three- to fourfold in abundance at centromeres. Fluorescence recovery after photobleaching (FRAP) measurements documented steady-state exchange between soluble and assembled pools, with CENP-X exchanging approximately 10 times faster than CENP-S (t1/2 ∼ 10 min versus 120 min). CENP-S binding to sites of DNA damage was quite distinct, with a FRAP half-time of approximately 160 s. Fluorescent two-hybrid analysis identified CENP-T as a uniquely strong CENP-S binding protein and this association was confirmed by FRET, revealing a centromere-bound complex containing CENP-S, CENP-X and CENP-T in proximity to histone H3 but not CENP-A. We propose that deposition of the CENP-T/W/S/X particle reveals a kinetochore-specific chromatin assembly pathway that functions to switch centromeric chromatin to a mitosis-competent state after DNA replication. Centromeres shuttle between CENP-A-rich, replication-competent and H3-CENP-T/W/S/X-rich mitosis-competent compositions in the cell cycle.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Cell Biology and Epigenetics
Hinterlegungsdatum: 08 Apr 2014 12:46
Letzte Änderung: 02 Mär 2022 14:02
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