Fig. 3: The intrinsically disordered regions (IDRs) in the N-terminal part of CHD4 are important for remodelling. | Nature Communications

Fig. 3: The intrinsically disordered regions (IDRs) in the N-terminal part of CHD4 are important for remodelling.

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

Fig. 3

A RTFA data for the IDR1 charge mutants, along with a mutant in which residues 1–144 were deleted. B Numbers of positively or negatively charged residues, as well as polar residues, in the del+ and del– mutants. C RTFA data for IDR2 mutants in which the sequence of residues 227–362 was either scrambled (scram) or depleted of either positively charged residues (del + ) or negatively charged residues (del–). We note that the del– curve (which is a mean of three replicates) displays an apparent biphasic shape, but this has not been investigated further at this point. It is only one of the three replicates that has this shape. D Microscale thermophoresis (MST) data showing the binding of a 46w60 nucleosome to WT CHD4 and the indicated variants. Three technical replicates and fits to a 1:1 binding isotherm are shown for each mutant and KD values are indicated (see also Supplementary Fig. S1). We estimate the uncertainty for KD’s to be ~25%. All raw data are provided as a Source Data file.

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