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

Breindl, Matthias and Spitzer, Dominika and Gerasimaite, Ruta and Kairys, Visvaldas and Schubert, Thomas and Henfling, Ramona and Schwartz, Uwe and Lukinavicius, Grazvydas and Manelyte, Laura (2024) Biochemical and cellular insights into the Baz2B protein, a non-catalytic subunit of the chromatin remodeling complex. NUCLEIC ACIDS RESEARCH, 52 (1). pp. 337-354. ISSN 0305-1048, 1362-4962

Full text not available from this repository. (Request a copy)

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. Graphical Abstract

Item Type: Article
Uncontrolled Keywords: DNA-BINDING DOMAIN; AT-HOOK MOTIFS; HETEROCHROMATIN FORMATION; MAMMALIAN ISWI; BROMODOMAIN; NORC; RNA; FAMILY; RECOGNITION; STABILITY
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III
Depositing User: Dr. Gernot Deinzer
Date Deposited: 12 Mar 2024 14:39
Last Modified: 04 Mar 2025 08:07
URI: https://pred.uni-regensburg.de/id/eprint/59404

Actions (login required)

View Item View Item