TY - JOUR
T1 - The Interaction of NF-κB Transcription Factor with Centromeric Chromatin
AU - Filliaux, Shaun
AU - Bertelsen, Chloe
AU - Baughman, Hannah
AU - Komives, Elizabeth
AU - Lyubchenko, Yuri
N1 - Publisher Copyright:
© 2024 American Chemical Society.
PY - 2024/6/20
Y1 - 2024/6/20
N2 - Centromeric chromatin is a subset of chromatin structure and governs chromosome segregation. The centromere is composed of both CENP-A nucleosomes (CENP-Anuc) and H3 nucleosomes (H3nuc) and is enriched with alpha-satellite (α-sat) DNA repeats. These CENP-Anuc have a different structure than H3nuc, decreasing the base pairs (bp) of wrapped DNA from 147 bp for H3nuc to 121 bp for CENP-Anuc. All these factors can contribute to centromere function. We investigated the interaction of H3nuc and CENP-Anuc with NF-κB, a crucial transcription factor in regulating immune response and inflammation. We utilized atomic force microscopy (AFM) to characterize complexes of both types of nucleosomes with NF-κB. We found that NF-κB unravels H3nuc, removing more than 20 bp of DNA, and that NF-κB binds to the nucleosomal core. Similar results were obtained for the truncated variant of NF-κB comprised only of the Rel homology domain and missing the transcription activation domain (TAD), suggesting that RelATAD is not critical in unraveling H3nuc. By contrast, NF-κB did not bind to or unravel CENP-Anuc. These findings with different affinities for two types of nucleosomes to NF-κB may have implications for understanding the mechanisms of gene expression in bulk and centromere chromatin.
AB - Centromeric chromatin is a subset of chromatin structure and governs chromosome segregation. The centromere is composed of both CENP-A nucleosomes (CENP-Anuc) and H3 nucleosomes (H3nuc) and is enriched with alpha-satellite (α-sat) DNA repeats. These CENP-Anuc have a different structure than H3nuc, decreasing the base pairs (bp) of wrapped DNA from 147 bp for H3nuc to 121 bp for CENP-Anuc. All these factors can contribute to centromere function. We investigated the interaction of H3nuc and CENP-Anuc with NF-κB, a crucial transcription factor in regulating immune response and inflammation. We utilized atomic force microscopy (AFM) to characterize complexes of both types of nucleosomes with NF-κB. We found that NF-κB unravels H3nuc, removing more than 20 bp of DNA, and that NF-κB binds to the nucleosomal core. Similar results were obtained for the truncated variant of NF-κB comprised only of the Rel homology domain and missing the transcription activation domain (TAD), suggesting that RelATAD is not critical in unraveling H3nuc. By contrast, NF-κB did not bind to or unravel CENP-Anuc. These findings with different affinities for two types of nucleosomes to NF-κB may have implications for understanding the mechanisms of gene expression in bulk and centromere chromatin.
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U2 - 10.1021/acs.jpcb.3c08388
DO - 10.1021/acs.jpcb.3c08388
M3 - Article
C2 - 38860885
AN - SCOPUS:85196024829
SN - 1520-6106
VL - 128
SP - 5803
EP - 5813
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 24
ER -