Figure 4: Proposed ‘corralling’ mechanism of hDot1L activation by H2B-Ub. | Nature Communications

Figure 4: Proposed ‘corralling’ mechanism of hDot1L activation by H2B-Ub.

From: Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation

Figure 4

Core histones, hDot1L and ubiquitin are coloured in blue, yellow and purple, respectively. The DNA-binding region of hDot1L is illustrated in orange, and the N-terminal tail of H2A is shown in green. Top, binding model of hDot1L and an unmodified nucleosome. In this case, a non-productive 1:1 enzyme-substrate complex is favored. Bottom, binding model of hDot1L with a ubiquitylated nucleosome. The presence of H2B-Ub in the nucleosome physically obstructs the formation of non-productive enzyme-substrate complexes and corrals hDot1L on the nucleosomal surface to its catalytically productive position.

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