Fig. 1: Model for CHD4-driven nucleosome sliding activity. | Nature Communications

Fig. 1: Model for CHD4-driven nucleosome sliding activity.

From: The role of auxiliary domains in modulating CHD4 activity suggests mechanistic commonality between enzyme families

Fig. 1

A Model for CHD4-driven nucleosome sliding, based on previous work4,19,80. After initial binding of CHD4, multiple rounds of ATP hydrolysis are coupled to 1-bp translocations of DNA from the entry side, building up a bulge or twist defect that incorporates the additional base pairs. This defect is resolved by the expulsion of DNA from the exit side of the nucleosome. B Topology of human CHD4 (Uniprot: Q14839) and truncations used in this study. Regions that are known or predicted to be ordered are shown in colours. Regions predicted by mobiDB (https://mobidb.bio.unipd.it/) to be disordered are indicated as black rectangles. Sequence replacements for IDR1 mutants chrg1, chrg2 and chrg3 are indicated. The chrg4 mutant combines these three mutations together. Sequences for the IDR2 mutants are given in Supplementary Fig. 2B.

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