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Table 1 Functional domains of ISWI proteins

From: The emerging role of ISWI chromatin remodeling complexes in cancer

Domain

Functions

ATP binding domain

ATP binding domain, an autonomous nucleosome remodeling machine, interacts with the super helical location 2 (SHL2) of the nucleosomal DNA, with the N-terminal tail of H4 and with the α1 helix of H3

C-terminal NegC domain

The C-terminal NegC domain is involved in binding to the core2 domain and functions as an allosteric element for ISWI to respond to the extranucleosomal DNA length

SANT domain

SANT domain has a central role in chromatin remodeling by functioning as a unique histone-interaction module that couples histone binding to enzyme catalysis, and it is important for nucleosome sliding activity, such as the regulation of nucleosome spacing

WAC domain

WAC domain is involved in the interaction of ACF with chromatin and the binding of other ACF-related factors to DNA

DDT domain

DDT domain associates with the histone modifications H3K4me3 and H4K16ac and facilitates DNA binding

Bromodomain

Bromodomain is a conserved motif, which recognizes acetylated lysine residues of histones or interacting proteins

MBD domain

The MBD (methyl-CpG-binding) domain specifically recognizes and binds to methylated CpGs. This binding allows it to trigger methylation of H3K9 and results in transcriptional repression

PHD-type zinc finger domain

PHD-type zinc finger domain binds specific epigenetic marks on histone tails to recruit transcription factors and nucleosome-associated complexes to chromatin. For example, it resides in the BPTF subunit of NURF, interacts directly with H3K4me3, stabilizes association of BPTF/NURF with chromatin