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Binding factors of RNAPII isolated from the HeLa cell nuclei

ABSTRACT: RNA polymerase II (RNAPII) is a major transcription protein that transcribes the genomic DNA packaged into chromatin. To reveal the RNAPII structures during transcription in the human genome, we extracted the RNAPII molecules inside the HeLa cell nuclei and determined the structures of transcribing RNAPII molecules associated with/without the transcription elongation factors and nucleosome. Our LC-MS/MS analysis revealed that the preinitiation complex components, such as Mediator, TFIIH, and TFIID, the elongation complex subunits, such as SPT4/5, SPT6, and ELOF1, and histones exist in the immunopurified fraction of RNAPII from HeLa cell nuclei.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hitoshi Kurumizaka

PROVIDER: PXD052434 | JPOST Repository | Thu Apr 24 00:00:00 BST 2025

REPOSITORIES: jPOST

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			Action	DRS
	220520kujiA01_0603F60_1ul.raw	Raw
	220520kujiA01_0603F60_1ul_kHSukb24pSTY_Perc.msf	Msf
	220520kujiA02_0603F60_1ul.raw	Raw
	220520kujiA03_0603F60_1ul.raw	Raw
	220520kujiA04_0603F60_1ul.raw	Raw

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Project description:Nucleosome assembly in vivo requires assembly factors, such as histone chaperones, to bind to histones and mediate their deposition onto DNA. In yeast, the essential histone chaperone FACT (FAcilitates Chromatin Transcription) functions in nucleosome assembly and H2A-H2B deposition during transcription elongation and DNA replication. Recent studies have identified candidate histone residues that mediate FACT binding to histones, but it is not known which histone residues are important for FACT to deposit histones onto DNA during nucleosome assembly. In this study, we report that the histone H2B repression (HBR) domain within the H2B N-terminal tail is important for histone deposition by FACT. Deletion of the HBR domain causes significant defects in histone occupancy in the yeast genome, particularly at HBR-repressed genes, and a pronounced increase in H2A-H2B dimers that remain bound to FACT in vivo. Moreover, the HBR domain is required for purified FACT to efficiently assemble recombinant nucleosomes in vitro. We propose that the interaction between the highly basic HBR domain and DNA plays an important role in stabilizing the nascent nucleosome during the process of histone H2A-H2B deposition by FACT. 6 samples, 2 inputs and 4 ChIP samples for histone H2B (2 for wild-type and 2 for an H2B â30-37 mutant)

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