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. 2016 Jul 4;214(1):13–24. doi: 10.1083/jcb.201605005

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© 2016 Chen and Mellone

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Figure 4. — Chromatin reorganization during CENP-A assembly in humans. (A) Newly synthesized CENP-A-H4 dimers in complex with an as-yet-unidentified chaperone are handed off to the assembly factor HJURP, which is recruited to the centromere by the Mis18 complex–CENP-C pathway (not depicted). (B) After the recruitment of CHD1, FACT, and RNA polymerase II, the placeholder (H3.1/H3.3-H4)₂ tetramers (or entire nucleosomes) are disassembled and (CENP-A-H4)₂ tetramers are deposited onto DNA. Mis18 transiently recruits the lysine acetyltransferase KAT7 to centromeres, which acetylates H3-containing nucleosomes and facilitates RSF binding. (C) After their formation, new CENP-A nucleosomesare spaced by the RSF complex, which promotes CENP-B binding.