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. 2017 Jun 9;16(13):1259–1265. doi: 10.1080/15384101.2017.1325044

Figure 3.

Figure 3.

Role for the RbAp48-Hat1 complex-mediated acetylation of the H4 tail in CENP-Adeposition. The H4 tail in the CENP-A-H4 complex is acetylated at K5 and K12 by the RbAp48-Hat1 complex before H4-CENP-A centromere deposition. The CENP-A-H4 complex binds the N-terminus of HJURP, and the middle region of HJURP recognizes centromeres (via the Mis18 complex) to facilitate centromere deposition. Acetylation of the H4 tail normally facilitates this process; however, if acetylation does not occur correctly (as in RbAp48-deficient cells), the non-acetylated tail interferes with HJURP centromere recognition, preventing CENP-A from being incorporated into centromere domains. It is unclear how H4 acetylation facilitates CENP-A deposition. Given that HJURP is a highly phosphorylated protein, it may be that a combination of HJURP phosphorylation and H4 acetylation is critical for correct H4-CENP-A deposition.