Please use this identifier to cite or link to this item: https://doi.org/10.1093/nar/gkx1180
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dc.titleProlyl isomerization of the CENP-A N-Terminus regulates centromeric integrity in fission yeast
dc.contributor.authorTan, H.L.
dc.contributor.authorLim, K.K.
dc.contributor.authorYang, Q.
dc.contributor.authorFan, J.-S.
dc.contributor.authorSayed, A.M.M.
dc.contributor.authorLow, L.S.
dc.contributor.authorRen, B.
dc.contributor.authorLim, T.K.
dc.contributor.authorLin, Q.
dc.contributor.authorMok, Y.-K.
dc.contributor.authorLiou, Y.-C.
dc.contributor.authorChen, E.S.
dc.date.accessioned2021-12-09T05:02:47Z
dc.date.available2021-12-09T05:02:47Z
dc.date.issued2018
dc.identifier.citationTan, H.L., Lim, K.K., Yang, Q., Fan, J.-S., Sayed, A.M.M., Low, L.S., Ren, B., Lim, T.K., Lin, Q., Mok, Y.-K., Liou, Y.-C., Chen, E.S. (2018). Prolyl isomerization of the CENP-A N-Terminus regulates centromeric integrity in fission yeast. Nucleic Acids Research 46 (3) : 1167-1179. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/gkx1180
dc.identifier.issn0305-1048
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/210115
dc.description.abstractCentromeric identity and chromosome segregation are determined by the precise centromeric targeting of CENP-A, the centromere-specific histone H3 variant. The significance of the amino-terminal domain (NTD) of CENP-A in this process remains unclear. Here, we assessed the functional significance of each residue within the NTD of CENP-A fromSchizosaccharomyces pombe(SpCENP-A) and identified a proline-rich 'GRANT' (Genomic stability-Regulating site within CENP-A N-Terminus) motif that is important for CENP-A function. Through sequential mutagenesis, we show that GRANT proline residues are essential for coordinating SpCENP-A centromeric targeting. GRANT proline-15(P15), in particular, undergoes cis-transisomerization to regulate chromosome segregation fidelity, which appears to be carried out by two FK506-binding protein (FKBP) family prolyl cis-trans isomerases. Using proteomics analysis, we further identified the SpCENP-A-localizing chaperone Sim3 as a SpCENP-A NTD interacting protein that is dependent on GRANT proline residues. Ectopic expression of sim3+ complemented the chromosome segregation defect arising from the loss of these proline residues. Overall, cis-trans proline isomerization is a posttranslational modification of the SpCENP-A NTD that confers precise propagation of centromeric integrity in fission yeast, presumably via targeting SpCENP-A to the centromere. © The Author(s) 2017.
dc.publisherOxford University Press
dc.rightsAttribution-NonCommercial 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/
dc.sourceScopus OA2018
dc.typeArticle
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.description.doi10.1093/nar/gkx1180
dc.description.sourcetitleNucleic Acids Research
dc.description.volume46
dc.description.issue3
dc.description.page1167-1179
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