The N-terminal region of chromodomain helicase DNA-binding protein 4 (CHD4) is essential for activity and contains a high mobility group (HMG) box-like-domain that can bind poly(ADP-ribose). Silva, A., Ryan, D., Galanty, Y., Low, J., Vandevenne, M., Jackson, S., & Mackay, J. Journal of Biological Chemistry, 291(2):924-938, 2016. doi abstract bibtex Chromodomain Helicase DNA-binding protein 4 (CHD4) is a chromatin-remodeling enzyme that has been reported to regulate DNA-damage responses through its N-terminal region in a poly(ADP-ribose) polymerase-dependent manner. We have identified and determined the structure of a stable domain (CHD4-N) in this N-terminal region. The-fold consists of a four-α-helix bundle with structural similarity to the high mobility group box, a domain that is well known as a DNA binding module. We show that the CHD4-N domain binds with higher affinity to poly(ADP-ribose) than to DNA. We also show that the N-terminal region of CHD4, although not CHD4-N alone, is essential for full nucleosome remodeling activity and is important for localizing CHD4 to sites of DNA damage. Overall, these data build on our understanding of how CHD4-NuRD acts to regulate gene expression and participates in the DNA-damage response.
@article{
title = {The N-terminal region of chromodomain helicase DNA-binding protein 4 (CHD4) is essential for activity and contains a high mobility group (HMG) box-like-domain that can bind poly(ADP-ribose)},
type = {article},
year = {2016},
pages = {924-938},
volume = {291},
id = {ecf7907f-b86b-3542-ab23-e2a9a7ff5cc9},
created = {2023-01-10T01:44:27.879Z},
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last_modified = {2023-01-10T01:44:27.879Z},
read = {false},
starred = {false},
authored = {false},
confirmed = {false},
hidden = {false},
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abstract = {Chromodomain Helicase DNA-binding protein 4 (CHD4) is a chromatin-remodeling enzyme that has been reported to regulate DNA-damage responses through its N-terminal region in a poly(ADP-ribose) polymerase-dependent manner. We have identified and determined the structure of a stable domain (CHD4-N) in this N-terminal region. The-fold consists of a four-α-helix bundle with structural similarity to the high mobility group box, a domain that is well known as a DNA binding module. We show that the CHD4-N domain binds with higher affinity to poly(ADP-ribose) than to DNA. We also show that the N-terminal region of CHD4, although not CHD4-N alone, is essential for full nucleosome remodeling activity and is important for localizing CHD4 to sites of DNA damage. Overall, these data build on our understanding of how CHD4-NuRD acts to regulate gene expression and participates in the DNA-damage response.},
bibtype = {article},
author = {Silva, A.P.G. and Ryan, D.P. and Galanty, Y. and Low, J.K.K. and Vandevenne, M. and Jackson, S.P. and Mackay, J.P.},
doi = {10.1074/jbc.M115.683227},
journal = {Journal of Biological Chemistry},
number = {2}
}
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