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  Biochemical and cellular insights into the Baz2B protein, a non-catalytic subunit of the chromatin remodeling complex

Breindl, M., Spitzer, D., Gerasimaitė, R., Kairys, V., Schubert, T., Henfling, R., et al. (2024). Biochemical and cellular insights into the Baz2B protein, a non-catalytic subunit of the chromatin remodeling complex. Nucleic Acids Research, 52(1), 337-354. doi:10.1093/nar/gkad1096.

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Breindl, Matthias, Author
Spitzer, Dominika, Author
Gerasimaitė, Rūta1, 2, Author           
Kairys, Visvaldas, Author
Schubert, Thomas, Author
Henfling, Ramona, Author
Schwartz, Uwe, Author
Lukinavičius, Gražvydas1, 2, Author           
Manelytė, Laura, Author
Affiliations:
1Department of NanoBiophotonics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350048              
2Research Group of Chromatin Labeling and Imaging, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350123              

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 Abstract: Baz2B is a regulatory subunit of the ATP-dependent chromatin remodeling complexes BRF1 and BRF5, which control access to DNA during DNA-templated processes. Baz2B has been implicated in several diseases and also in unhealthy ageing, however limited information is available on the domains and cellular roles of Baz2B. To gain more insight into the Baz2B function, we biochemically characterized the TAM (Tip5/ARBP/MBD) domain with the auxiliary AT-hook motifs and the bromodomain (BRD). We observed alterations in histone code recognition in bromodomains carrying cancer-associated point mutations, suggesting their potential involvement in disease. Furthermore, the depletion of Baz2B in the Hap1 cell line resulted in altered cell morphology, reduced colony formation and perturbed transcriptional profiles. Despite that, super-resolution microscopy images revealed no changes in the overall chromatin structure in the absence of Baz2B. These findings provide insights into the biological function of Baz2B.

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Language(s): eng - English
 Dates: 2023-11-242024-01-11
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1093/nar/gkad1096
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Project name : Deutsche Forschungsgemeinschaft [315563949]; Bavarian Ministry of Science and Art and the University of Regensburg [to L.M.]; G.L. and R.G. are supported by the Max Planck Society. Funding for open access charge: Library of University of Regensburg.
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Title: Nucleic Acids Research
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 52 (1) Sequence Number: - Start / End Page: 337 - 354 Identifier: ISSN: 0305-1048
CoNE: https://pure.mpg.de/cone/journals/resource/110992357379342