A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.

<h4>Background</h4>Centromere identity is determined epigenetically by deposition of CenH3, a centromere-specific histone H3 variant that dictates kinetochore assembly. The molecular basis of the contribution of CenH3 to centromere/kinetochore functions is, however, incompletely understo...

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Autores principales:	Mònica Torras-Llort, Sònia Medina-Giró, Olga Moreno-Moreno, Fernando Azorín
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bed192c2386243048b1776e3ca1eacf3
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spelling	oai:doaj.org-article:bed192c2386243048b1776e3ca1eacf32021-11-18T07:02:39ZA conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.1932-620310.1371/journal.pone.0013747https://doaj.org/article/bed192c2386243048b1776e3ca1eacf32010-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21060784/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Centromere identity is determined epigenetically by deposition of CenH3, a centromere-specific histone H3 variant that dictates kinetochore assembly. The molecular basis of the contribution of CenH3 to centromere/kinetochore functions is, however, incompletely understood, as its interactions with the rest of centromere/kinetochore components remain largely uncharacterised at the molecular/structural level.<h4>Principal findings</h4>Here, we report on the contribution of Drosophila CenH3(CID) to recruitment of BubR1, a conserved kinetochore protein that is a core component of the spindle attachment checkpoint (SAC). This interaction is mediated by the N-terminal domain of CenH3(CID) (NCenH3(CID)), as tethering NCenH3(CID) to an ectopic reporter construct results in BubR1 recruitment and BubR1-dependent silencing of the reporter gene. Here, we also show that this interaction depends on a short arginine (R)-rich motif and that, most remarkably, it appears to be evolutionarily conserved, as tethering constructs carrying the highly divergent NCenH3 of budding yeast and human also induce silencing of the reporter. Interestingly, though NCenH3 shows an exceedingly low degree of conservation, the presence of R-rich motives is a common feature of NCenH3 from distant species. Finally, our results also indicate that two other conserved sequence motives within NCenH3(CID) might also be involved in interactions with kinetochore components.<h4>Conclusions</h4>These results unveil an unexpected contribution of the hypervariable N-domain of CenH3 to recruitment of kinetochore components, identifying simple R-rich motives within it as evolutionary conserved structural determinants involved in BubR1 recruitment.Mònica Torras-LlortSònia Medina-GiróOlga Moreno-MorenoFernando AzorínPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 10, p e13747 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mònica Torras-Llort Sònia Medina-Giró Olga Moreno-Moreno Fernando Azorín A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.
description	<h4>Background</h4>Centromere identity is determined epigenetically by deposition of CenH3, a centromere-specific histone H3 variant that dictates kinetochore assembly. The molecular basis of the contribution of CenH3 to centromere/kinetochore functions is, however, incompletely understood, as its interactions with the rest of centromere/kinetochore components remain largely uncharacterised at the molecular/structural level.<h4>Principal findings</h4>Here, we report on the contribution of Drosophila CenH3(CID) to recruitment of BubR1, a conserved kinetochore protein that is a core component of the spindle attachment checkpoint (SAC). This interaction is mediated by the N-terminal domain of CenH3(CID) (NCenH3(CID)), as tethering NCenH3(CID) to an ectopic reporter construct results in BubR1 recruitment and BubR1-dependent silencing of the reporter gene. Here, we also show that this interaction depends on a short arginine (R)-rich motif and that, most remarkably, it appears to be evolutionarily conserved, as tethering constructs carrying the highly divergent NCenH3 of budding yeast and human also induce silencing of the reporter. Interestingly, though NCenH3 shows an exceedingly low degree of conservation, the presence of R-rich motives is a common feature of NCenH3 from distant species. Finally, our results also indicate that two other conserved sequence motives within NCenH3(CID) might also be involved in interactions with kinetochore components.<h4>Conclusions</h4>These results unveil an unexpected contribution of the hypervariable N-domain of CenH3 to recruitment of kinetochore components, identifying simple R-rich motives within it as evolutionary conserved structural determinants involved in BubR1 recruitment.
format	article
author	Mònica Torras-Llort Sònia Medina-Giró Olga Moreno-Moreno Fernando Azorín
author_facet	Mònica Torras-Llort Sònia Medina-Giró Olga Moreno-Moreno Fernando Azorín
author_sort	Mònica Torras-Llort
title	A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.
title_short	A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.
title_full	A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.
title_fullStr	A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.
title_full_unstemmed	A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.
title_sort	conserved arginine-rich motif within the hypervariable n-domain of drosophila centromeric histone h3 (cenh3) mediates bubr1 recruitment.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/bed192c2386243048b1776e3ca1eacf3
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A conserved arginine-rich motif within the hypervariable N-domain of Drosophila centromeric histone H3 (CenH3) mediates BubR1 recruitment.

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