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Int. J. Mol. Sci. 2015, 16(3), 5839-5863; doi:10.3390/ijms16035839

The CENP-T C-Terminus Is Exclusively Proximal to H3.1 and not to H3.2 or H3.3

1
Molecular Biology, Fritz Lipmann Institute, Beutenbergstr. 11, D-07745 Jena, Germany
2
Department of Molecular Biology, Center for Integrated Protein Science Munich (CIPSM), Adolf-Butenandt-Institute, Ludwig-Maximilians-Universität Munich, Schillerstr. 44, D-80336 Munich, Germany
3
Department of Biology II, Center for Integrated Protein Science, Ludwig-Maximilians-Universität Munich, Planegg-Martinsried, D-82152 Munich, Germany
4
PicoQuant GmbH, Kekulestr. 7, D-12489 Berlin, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Herbert Schneckenburger
Received: 20 January 2015 / Revised: 18 February 2015 / Accepted: 18 February 2015 / Published: 12 March 2015
(This article belongs to the Special Issue Förster Resonance Energy Transfer (FRET) 2015)
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Abstract

The kinetochore proteins assemble onto centromeric chromatin and regulate DNA segregation during cell division. The inner kinetochore proteins bind centromeres while most outer kinetochore proteins assemble at centromeres during mitosis, connecting the complex to microtubules. The centromere–kinetochore complex contains specific nucleosomes and nucleosomal particles. CENP-A replaces canonical H3 in centromeric nucleosomes, defining centromeric chromatin. Next to CENP-A, the CCAN multi-protein complex settles which contains CENP-T/W/S/X. These four proteins are described to form a nucleosomal particle at centromeres. We had found the CENP-T C-terminus and the CENP-S termini next to histone H3.1 but not to CENP-A, suggesting that the Constitutive Centromere-Associated Network (CCAN) bridges a CENP-A- and a H3-containing nucleosome. Here, we show by in vivo FRET that this proximity between CENP-T and H3 is specific for H3.1 but neither for the H3.1 mutants H3.1C96A and H3.1C110A nor for H3.2 or H3.3. We also found CENP-M next to H3.1 but not to these H3.1 mutants. Consistently, we detected CENP-M next to CENP-S. These data elucidate the local molecular neighborhood of CCAN proteins next to a H3.1-containing centromeric nucleosome. They also indicate an exclusive position of H3.1 clearly distinct from H3.2, thus documenting a local, and potentially also functional, difference between H3.1 and H3.2. View Full-Text
Keywords: centromere; kinetochore; Constitutive Centromere-Associated Network (CCAN); mitosis; histone variants; chromatin; Förster Resonance Energy Transfer (FRET) centromere; kinetochore; Constitutive Centromere-Associated Network (CCAN); mitosis; histone variants; chromatin; Förster Resonance Energy Transfer (FRET)
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Abendroth, C.; Hofmeister, A.; Hake, S.B.; Kamweru, P.K.; Miess, E.; Dornblut, C.; Küffner, I.; Deng, W.; Leonhardt, H.; Orthaus, S.; Hoischen, C.; Diekmann, S. The CENP-T C-Terminus Is Exclusively Proximal to H3.1 and not to H3.2 or H3.3. Int. J. Mol. Sci. 2015, 16, 5839-5863.

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