{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T03:15:50Z","timestamp":1775790950769,"version":"3.50.1"},"reference-count":50,"publisher":"American Society for Cell Biology (ASCB)","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2013,4]]},"abstract":"<jats:p> Centromeres are the site of kinetochore formation during mitosis. Centromere protein A (CENP-A), the centromere-specific histone H3 variant, is essential for the epigenetic maintenance of centromere position. Previously we showed that newly synthesized CENP-A is targeted to centromeres exclusively during early G1 phase and is subsequently maintained across mitotic divisions. Using SNAP-based fluorescent pulse labeling, we now demonstrate that cell cycle\u2013restricted chromatin assembly at centromeres is unique to CENP-A nucleosomes and does not involve assembly of other H3 variants. Strikingly, stable retention is restricted to the CENP-A\/H4 core of the nucleosome, which we find to outlast general chromatin across several cell divisions. We further show that cell cycle timing of CENP-A assembly is independent of centromeric DNA sequences and instead is mediated by the CENP-A targeting domain. Unexpectedly, this domain also induces stable transmission of centromeric nucleosomes, independent of the CENP-A deposition factor HJURP. This demonstrates that intrinsic properties of the CENP-A protein direct its cell cycle\u2013restricted assembly and induces quantitative mitotic transmission of the CENP-A\/H4 nucleosome core, ensuring long-term stability and epigenetic maintenance of centromere position. <\/jats:p>","DOI":"10.1091\/mbc.e13-01-0034","type":"journal-article","created":{"date-parts":[[2013,1,31]],"date-time":"2013-01-31T03:02:57Z","timestamp":1359601377000},"page":"923-932","source":"Crossref","is-referenced-by-count":106,"title":["Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes"],"prefix":"10.1091","volume":"24","author":[{"given":"Dani L.","family":"Bodor","sequence":"first","affiliation":[{"name":"Instituto Gulbenkian de Ci\u00eancia, 2780-156 Oeiras, Portugal"}]},{"given":"Luis P.","family":"Valente","sequence":"additional","affiliation":[{"name":"Instituto Gulbenkian de Ci\u00eancia, 2780-156 Oeiras, Portugal"}]},{"given":"Jo\u00e3o F.","family":"Mata","sequence":"additional","affiliation":[{"name":"Instituto Gulbenkian de Ci\u00eancia, 2780-156 Oeiras, Portugal"}]},{"given":"Ben E.","family":"Black","sequence":"additional","affiliation":[{"name":"Perelman School of Medicine and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104-6059"}]},{"given":"Lars E. 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