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. 2018 Apr 11;9:1394. doi: 10.1038/s41467-018-03895-5

Fig. 6.

Fig. 6

Model for the crosstalk between H2BK120ub and the H2A/H2A.Z N-terminal tail Top: key lysine residues within the H2A tail help position ubiquitin for optimal transfer from the charged ubiquitylation machinery to the H2BK120 (shown in gray) in the nucleosome. Bottom: lysine acetylation (or replacement in the case of H2A.Z—not shown) disrupts the interaction with the charged ubiquitin, lowering the efficiency of ubiquitylation