ABSTRACT The scaffolding protein XRCC1 orchestrates base excision repair (BER) and DNA single strand break repair (SSBR) through extensive protein-protein interactions, and its disruption contributes to human neurological diseases such as SCAR26. Recruitment to DNA damage sites has been traditionally understood to depend exclusively on interaction with PARP1 and PARP1 mediated PARylation. Here, we report for the first time the discovery of GCN5 and TADA2B, components of histone acetyltransferase module of SAGA complex, as novel XRCC1 binding partners that provide critical fine-tuning control over repair site localization. We demonstrate that these SAGA complex components bind XRCC1 constitutively via distinct BRCT domain interactions — GCN5 mainly to BRCT I and TADA2B mainly to BRCT II — independent of DNA damage status or GCN5’s acetyltransferase activity. Depletion of either protein significantly impairs XRCC1 recruitment efficiency, while paradoxically rescuing focal retention defects in BRCT II deficient XRCC1 mutants. This dual regulatory behavior reveals a regulatory mechanism where constitutive protein interactions optimize normal XRCC1 function but become counterproductive when XRCC1 is structurally compromised, particularly in the BRCT II domain. Analysis of the SCAR26 associated variant, which disrupts TADA2B binding while maintaining LIG3 interaction, confirms this dual regulatory model and provides molecular insights into potential disease pathophysiology. Our findings establish a ‘ready-for-action’ model of DNA repair coordination where protein complexes pre-organize repair machinery for immediate deployment upon damage detection, expanding our understanding of BER regulation.