Abstract 1845 Biochemical characterization of HSF2BP as a meiotic homologous recombination factor
Year: 2024
Type: conference-abstract
Abstract: Meiosis is a type of cell division that leads to the formation of cells with haploid number of chromosomes. Meiotic recombination is initiated by the deliberate introduction of double-strand breaks (DSB) into DNA. HSF2BP (or MEILB2) is a meiotic homologous recombination (HR) factor known to localize at programmed DNA DSB sites and facilitate the recruitment of BRCA2. In the absence of HSF2BP, the recombinases RAD51 and DMC1 fail to localize at meiotic DSBs. Although it is established that the meiotic DSB repair via HR involves HSF2BP, the precise molecular mechanism underlying this activity is still unknown. However, misregulation of this protein is implicated in male infertility and primary ovarian insufficiency in females. Our biochemical study aims to elucidate the activities of HSF2BP in meiotic HR. We expressed the human HSF2BP in Escherichia coli and then purified the protein through nickel affinity and ion exchange chromatographic methods. We demonstrated that HSF2BP interacts with single- and double-stranded DNA through electromobility shift assays. Also, HSF2BP protected RAD51 nucleoprotein filament by inhibiting the nucleolytic activity of deoxyribonuclease I. Further biochemical analyses provided evidence that HSF2BP binds to and hydrolyzes ATP. Thus, our results suggest that HSF2BP plays a crucial role in meiotic homologous recombination.
Source: Journal of Biological Chemistry
Authors: Amara Onoh, Emily Peak, Michael Sehorn
Institution: Clemson University
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,800
OpenAlex ID: W4393166671