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A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment

BACKGROUND: 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 interact...

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Autores principales: Torras-Llort, Mònica, Medina-Giró, Sònia, Moreno-Moreno, Olga, Azorín, Fernando
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2966416/
https://www.ncbi.nlm.nih.gov/pubmed/21060784
http://dx.doi.org/10.1371/journal.pone.0013747
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author Torras-Llort, Mònica
Medina-Giró, Sònia
Moreno-Moreno, Olga
Azorín, Fernando
author_facet Torras-Llort, Mònica
Medina-Giró, Sònia
Moreno-Moreno, Olga
Azorín, Fernando
author_sort Torras-Llort, Mònica
collection PubMed
description BACKGROUND: 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. PRINCIPAL FINDINGS: 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. CONCLUSIONS: 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.
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spelling pubmed-29664162010-11-08 A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment Torras-Llort, Mònica Medina-Giró, Sònia Moreno-Moreno, Olga Azorín, Fernando PLoS One Research Article BACKGROUND: 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. PRINCIPAL FINDINGS: 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. CONCLUSIONS: 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. Public Library of Science 2010-10-29 /pmc/articles/PMC2966416/ /pubmed/21060784 http://dx.doi.org/10.1371/journal.pone.0013747 Text en Torras-Llort et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Torras-Llort, Mònica
Medina-Giró, Sònia
Moreno-Moreno, Olga
Azorín, Fernando
A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment
title A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment
title_full A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment
title_fullStr A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment
title_full_unstemmed A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment
title_short A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3(CID)) Mediates BubR1 Recruitment
title_sort conserved arginine-rich motif within the hypervariable n-domain of drosophila centromeric histone h3 (cenh3(cid)) mediates bubr1 recruitment
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2966416/
https://www.ncbi.nlm.nih.gov/pubmed/21060784
http://dx.doi.org/10.1371/journal.pone.0013747
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