NuRD deacetylates nucleosomes

Stable Identifier
R-HSA-9944092
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
3/5
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This reaction shows a generic representation of the histone deacetylation activity of the NuRD complex on a non-specific acetylated chromatin template. The NuRD complex is recruited to specific regions in the genome by virtue of the DNA- and histone-binding properties of its components, as well as through protein-protein interactions with sequence-specific transcription factors, some of which are illustrated in this pathway (reviewed in Asmamaw et al, 2024; Alendar and Berns, 2021). NuRD binds to a di-nucleosome substrate and interacts with adjacent acetylated nucleosomes (Millard et al, 2013). Histone deacetylase activity is provided by the HDAC1 and/or HDAC2 components of the complex. (Xue et al, 1998; reviewed in Torchy et al, 2015).
Literature References
PubMed ID Title Journal Year
23791785 Class I HDACs share a common mechanism of regulation by inositol phosphates

Millard, CJ, Watson, PJ, Celardo, I, Gordiyenko, Y, Cowley, SM, Robinson, CV, Fairall, L, Schwabe, JW

Mol Cell 2013
34725129 Sentinels of chromatin: chromodomain helicase DNA-binding proteins in development and disease

Alendar, A, Berns, A

Genes Dev 2021
38971208 Histone deacetylase complexes: Structure, regulation and function

Asmamaw, MD, He, A, Zhang, LR, Liu, HM, Gao, Y

Biochim Biophys Acta Rev Cancer 2024
9885572 NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities

Xue, Y, Wong, J, Moreno, GT, Young, MK, Côté, J, Wang, W

Mol. Cell 1998
25796366 Structure and function insights into the NuRD chromatin remodeling complex

Torchy, MP, Hamiche, A, Klaholz, BP

Cell Mol Life Sci 2015
Participants
Participates
Catalyst Activity

histone deacetylase activity of NuRD [nucleoplasm]

Cross References
RHEA
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