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FACT complex subunit SSRP1 (structure-specific recognition protein 1) is a multi-domain protein encoded by the human SSRP1 gene and forms a heterodimer with SUPT16H as a core component of the facilitates chromatin transcription (FACT) complex[1][2][6]. SSRP1 plays a pivotal role in nucleosome disassembly and reassembly during gene transcription, DNA replication, and DNA repair, partly by binding histones H2A-H2B and H3-H4 and interacting with a range of transcriptional and chromatin remodeling factors[1][2][4][7]. Structurally, SSRP1 comprises multiple pleckstrin homology (PH) domains and a high-mobility group (HMG) box, the latter conferring its ability to recognize structurally distorted DNA such as that formed by cisplatin, which connects directly to its therapeutic relevance in oncology[2][4][7]. SSRP1 also serves as a co-activator for certain transcription factors, including p63, and is essential for proper cell proliferation and survival[1][3]. Dysregulation of SSRP1 is implicated in cancer and has emerged as a candidate for targeted therapies and as a biomarker in autoimmune diseases such as systemic lupus erythematosus[5][6].
DNA-binding and nucleosome disassembly in conjunction with anticancer agents (e.g., enhances the effects of cisplatin by recognizing cisplatin-modified DNA)[1][6][10]
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