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Investigating the Interaction Between RAD54 Terminal Domains to RAD54B Motor Protein in Homologous Recombination DNA Repair
DNA damage is a complex phenomenon arising from both endogenous and exogenous sources,
posing threats to genomic stability and necessitating an effective DNA damage response (DDR). A
dysfunctional DDR can cause genomic instability, which is defined by a higher frequency of DNA
mutations. Genomic instability is a common feature of many cancers, and it can result in
oncogenic mutations and tumor suppressor gene inactivation that drive tumor progression and
may impact cancer treatments, influencing tumor cell sensitivity or resistance to chemotherapy.
Homologous recombination is a vital DNA repair mechanism essential for maintaining genomic
stability, and a deficiency in its repair is known to increase cancer risk. RAD54 plays a crucial role
in HR, as it stabilizes the ssDNA-RAD51 nucleofilaments and removes RAD51 after the invasion
occurs. However, the role of its paralog RAD54B, postulated to have a similar or complementary
function to RAD54, has not yet been ascertained. Understanding the interaction between RAD54
and RAD54B could provide insights into how these proteins work together to promote DNA repair
by Homologous Recombination. Fundamental studies in Homologous Recombination hold great
translational potential to help improve traditional genotoxin-based and personalized anti-cancer
therapy. Here we aim to study the interactions between RAD54 and RAD54B through in vitro
pulldown assays using purified proteins.
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