Abstract
Human structure-specific recognition protein 1 (hSSRP1) is an essential component of the facilitates chromatin transcription complex, which participates in nucleosome disassembly and reassembly during gene transcription and DNA replication and repair. Many functions, including nuclear localization, histone chaperone activity, DNA binding, and interaction with cellular proteins, are attributed to hSSRP1, which contains multiple well-defined domains, including four pleckstrin homology (PH) domains and a high-mobility group domain with two flanking disordered regions. However, little is known about the mechanisms by which these domains cooperate to carry out hSSRP1’s functions. Here, we report the biochemical characterization and structure of each functional domain of hSSRP1, including the N-terminal PH1, PH2, PH3/4 tandem PH, and DNA-binding high-mobility group domains. Furthermore, two casein kinase II binding sites in hSSRP1 were identified in the PH3/4 domain and in a disordered region (Gly617–Glu709) located in the C-terminus of hSSRP1. In addition, a histone H2A–H2B binding motif and a nuclear localization signal (Lys677‒Asp687) of hSSRP1 are reported for the first time. Taken together, these studies provide novel insights into the structural basis for hSSRP1 functionality.
Highlights
Introduction playing critical roles in reversibleEukaryotic genomic DNA is organized nucleosome reorganization [16,17,18,19].into densely packed chromatin, a higher-SSRP1, an 87 kDa of basic repeating units, termed subunit of the FACT complex, is highly nucleosomes [1,2]
The outputs indicated that Human structure-specific recognition protein 1 (hSSRP1) contained four pleckstrin homology (PH) domains in the N-terminus (Met1– Arg428) followed by the high mobility group (HMG) domain within a long disordered region
We combined the isolated structural domains have been hydrophilicity of amino acids and the described for hSSRP1 and its homologs
Summary
Eukaryotic genomic DNA is organized nucleosome reorganization [16,17,18,19]. SSRP1 (human structure-specific order architecture dominated by arrays recognition protein-1), an 87 kDa of basic repeating units, termed subunit of the FACT complex, is highly nucleosomes [1,2]. The structure of the conserved across all eukaryotes, except nucleosome consists of 146 bp of DNA for its HMG domain, which is present in wrapped around an octamer of histone hSSRP1 but absent in the yeast homolog proteins, comprised of a heterotetramer. The FACT (facilitates chromatin transactions) complex, a heterodimer composed of the SSRP1 (hSSRP1) was initially characterized as an HMG-box protein binding to cisplatin-modified DNA with a classic DNA-binding domain at its C terminus, which enables it to bind DNA as it interacts with the nucleosome [23]. ATP-independent histone chaperone role of hSSRP1 was discovered in the complex that allows eukaryotic RNA regulation of the activity of transcription polymerase II to transcribe factors, including p63 and serum chromatinized DNA by destabilizing response factor (SRF) [29,30]. An overview of the topology of the fulllength hSSRP1 has been proposed
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