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HSP70 binds RNA and regulates transcription by RNA Polymerase III [FLASH-seq]

ABSTRACT: HSP70 binds RNA and regulates transcription by RNA Polymerase III [FLASH-seq]

PROVIDER: PRJNA790738 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	SRR17276161_1.fastq.gz	Fastqsanger.gz
	SRR17276161_2.fastq.gz	Fastqsanger.gz
	SRR17276162_1.fastq.gz	Fastqsanger.gz
	SRR17276162_2.fastq.gz	Fastqsanger.gz
	SRR17276163_1.fastq.gz	Fastqsanger.gz

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HSP70 binds RNA and regulates transcription by RNA Polymerase III [FLASH-seq]

Project description:We examined the RNA binding ability of the 70-kDa heat shock protein (HSP70) family member HSPA1A and HSP8 and identified the RNA species bound to HSP70 or HSP8 in vivo. We used a UV-crosslinkiung and immunoprecipitation based approach named FLASH-seq (Akta? et al., 2017) using 3xFLAG-Histidine-Biotin tagged ectopically expressed protein in HEK293T cells.

2024-01-17 | GSE191242 | GEO

HSP70 binds RNA and regulates transcription by RNA Polymerase III [RNA-seq]

Project description:We examined the RNA binding ability of the 70-kDa heat shock protein (HSP70) family member HSPA1A and identified the RNA species bound to HSP70 in vivo. We used a UV-crosslinkiung and immunoprecipitation based approach named FLASH-seq (Aktaş et al., 2017) using 3xFLAG-Histidine-Biotin tagged ectopically expressed protein in HEK293T cells.

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HSP70 binds RNA and regulates transcription by RNA Polymerase III [RNA-seq]

Project description:HSP70 binds RNA and regulates transcription by RNA Polymerase III [RNA-seq]

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HSP70 binds RNA and regulates transcription by RNA Polymerase III [ChIP-seq]

Project description:HSP70 binds RNA and regulates transcription by RNA Polymerase III [ChIP-seq]

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HSP70 binds to specific non-coding RNA and regulates human RNA polymerase III

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HSP70 binds to specific non-coding RNA and regulates human RNA polymerase III

Project description:This SuperSeries is composed of the SubSeries listed below.

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RNA polymerase III interactome

Project description:Many regulatory proteins and complexes have been identified which influence transcription by RNA polymerase (pol) II with a fine precision. In comparison, only a few regulatory proteins are known for pol III, which transcribes mostly house-keeping and non-coding RNAs. Yet, pol III transcription is precisely regulated under various stress conditions like starvation. We used proteomic approaches and pol III transcription complex components TFIIIC (Tfc6), pol III (Rpc128) and TFIIIB (Brf1) as baits to find identify the potential interactors through mass spectrometry-based proteomics. A large number of proteins were found in the interactome, which includes known chromatin modifiers, factors and regulators of transcription by pol I and pol II.

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Project description:RNA Pol III plays a vital role in transcription and as a viral-DNA sensor, but how it is assembled and distributed within cells remain poorly understood. Here, we show that Pol III is assembled with chaperones in the cytoplasm and forms transcription-dependent protein clusters upon transport into the nucleus. The largest subunit (RPC1) depletion through an auxin-inducible degron leads to rapid degradation and disassembly of Pol III complex in the nucleus and cytoplasm, respectively. This generates a pool of partially assembled Pol III intermediates, which can be rapidly mobilized into the nucleus upon the restoration of RPC1. Our study highlights the critical role of subcellular localization in determining Pol III's fate and provide insight into the dynamic regulation of nuclear Pol III levels and the origin of cytoplasmic Pol III complexes involved in mediating viral immunity.

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