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. 2008 Sep;19(9):3616–3624. doi: 10.1091/mbc.E08-01-0050

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© 2008 by The American Society for Cell Biology

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Figure 1. — Histone H2B is polyubiquitylated. Yeast cells were engineered to express either His-tagged WT or mutant (K48R or K63R) nonremovable (G76A) ubiquitin, together with either myc-tagged (FGY1; lane 1) or HA-epitope–tagged H2B (FGY2; lanes 2–5). Cells were lysed, and HA-tagged proteins present in the total lysate (input) or His-purified (Ni-NTA) material were detected by WB. The position of free H2B is indicated, as is the position of the H2B–Ub conjugates. Note that the monoubiquitylated form of H2B–HA appears as a doublet in the input; we presume that this corresponds to H2B–HA that is monoubiquitylated with either endogenous Ub (bottom panel) or the slightly larger His-Ub.