{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nStructure‐specific recognition protein 1 (SSRP1) is a core subunit of the FACT complex that plays a pivotal role in dynamically reorganizing chromatin. In multiple studies, FACT has been shown to facilitate both disassembly and reassembly of nucleosomes during transcription, DNA replication, and repair. High‐resolution structural and biophysical analyses have demonstrated that SSRP1 contributes extensive DNA‐binding capacity and can adopt alternate conformations depending on the local histone composition, thereby ensuring efficient nucleosome remodeling and the preservation of epigenetic integrity. In addition, FACT’s rapid binding to chromatin—and its subsequent release and re‐binding during replication licensing—underscores the central role of SSRP1 in regulating nucleosome dynamics."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its structural role, SSRP1 functions in regulating gene expression and maintaining genome stability through diverse DNA repair pathways. Investigations have revealed that SSRP1 can act as a transcriptional co‐activator, for example by potentiating p63‐dependent transcription, while its recruitment to active chromatin regions is required for proper nucleosome recovery during transcription elongation. FACT also promotes the deposition of histone variants important for DNA damage signaling and facilitates transcription‐coupled nucleotide excision repair by recruiting key repair factors. Moreover, SSRP1 interacts with proteins such as LEDGF/p75 and modulates the activity of recombination factors to limit aberrant homologous recombination, thereby preserving genomic integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant expression and regulation of SSRP1 are associated with altered cell fate decisions and oncogenesis. Upregulation of SSRP1 has been linked to aggressive phenotypes in several cancers, with elevated levels correlating with enhanced proliferation, resistance to chemotherapy, and disrupted cell cycle control. SSRP1 contributes to centromere assembly, modulates key signaling cascades (including AKT and MAPK), and promotes re‐entry of quiescent cells into the cell cycle by, for instance, facilitating the degradation of cell cycle inhibitors. Post‐translational modifications (such as CK2‐mediated phosphorylation) further fine‐tune its DNA‐binding activity, while roles in microtubule stabilization and in the repair of drug‐induced DNA lesions expand its functional repertoire. Additional studies indicate that SSRP1 acts as a coregulator for nuclear hormone receptors and supports replication stress tolerance, implicating it as both a biomarker and an attractive therapeutic target in diverse pathological contexts."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Duane D Winkler, Karolin Luger "}, {"type": "b", "children": [{"type": "t", "text": "The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.R110.180778"}], "href": "https://doi.org/10.1074/jbc.R110.180778"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21454601"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21454601"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Fu-Kai Hsieh, Olga I Kulaeva, Smita S Patel, et al. 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