Transcription is regulated and mediated by multiprotein complexes in a chromatin context. Transcription causes changes in DNA topology which is modulated by DNA topoisomerases, enzymes that catalyse changes in DNA topology via transient breaking and re-joining of one or both strands of the phosphodiester backbone. Mammals have six DNA topoisomerases, this review focuses on one, DNA topoisomerase II beta (TOP2B). In the absence of TOP2B transcription of many developmentally regulated genes is altered. Long genes seem particularly susceptible to the lack of TOP2B. Biochemical studies of the role of TOP2B in transcription regulated by ligands such as nuclear hormones, growth factors and insulin has revealed PARP1 associated with TOP2B and also PRKDC, XRCC5 and XRCC6. Analysis of publicly available databases of protein interactions confirms these interactions and illustrates interactions with other key transcriptional regulators including TRIM28. TOP2B has been shown to interact with proteins involved in chromosome organisation including CTCF and RAD21. Comparison of publicly available Chip-seq datasets reveals the location at which these proteins interact with genes. The availability of resources such as large datasets of protein–protein interactions, e.g. BioGrid and IntAct and protein–DNA interactions such as Chip-seq in GEO enables scientists to extend models and propose new hypotheses.
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December 2021
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Fuelled by the ‘resolution revolution’, cryo-EM has transformed our molecular understanding of transcriptional regulation in bacteria. As an example, Wood and colleagues (pp. 2695–2710) present the sialic acid gene repressor NanR (PDB-6WFG), where cryo-EM revealed the DNA-binding mode. “E. coli Bacteria” by NIAID is licensed under CC BY 2.0. Cover artwork courtesy of Christopher Horne.
Review Article|
November 08 2021
TOP2B's contributions to transcription
Caroline A. Austin
;
Biosciences Institute, The Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, U.K.
Correspondence: Caroline Austin (caroline.austin@ncl.ac.uk) or Ian Cowell (ian.cowell@ncl.ac.uk)
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Ian G. Cowell
;
Biosciences Institute, The Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, U.K.
Correspondence: Caroline Austin (caroline.austin@ncl.ac.uk) or Ian Cowell (ian.cowell@ncl.ac.uk)
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Mushtaq M. Khazeem
;
Mushtaq M. Khazeem
Biosciences Institute, The Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, U.K.
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Dawn Lok
;
Dawn Lok
Biosciences Institute, The Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, U.K.
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Huei Teng Ng
Huei Teng Ng
Biosciences Institute, The Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, U.K.
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Publisher: Portland Press Ltd
Received:
August 24 2021
Revision Received:
October 07 2021
Accepted:
October 11 2021
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2021
Biochem Soc Trans (2021) 49 (6): 2483–2493.
Article history
Received:
August 24 2021
Revision Received:
October 07 2021
Accepted:
October 11 2021
Citation
Caroline A. Austin, Ian G. Cowell, Mushtaq M. Khazeem, Dawn Lok, Huei Teng Ng; TOP2B's contributions to transcription. Biochem Soc Trans 17 December 2021; 49 (6): 2483–2493. doi: https://doi.org/10.1042/BST20200454
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