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Platinoid drugs augment immunotherapy via histone acetylation of MHCI machinery genes [TRAMP]

ABSTRACT: Platinoid drugs augment immunotherapy via histone acetylation of MHCI machinery genes [TRAMP]

PROVIDER: PRJNA521468 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8550250.fastq.gz	Fastqsanger.gz
	SRR8550260.fastq.gz	Fastqsanger.gz
	SRR8550251.fastq.gz	Fastqsanger.gz
	SRR8550261.fastq.gz	Fastqsanger.gz
	SRR8550252.fastq.gz	Fastqsanger.gz

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Platinoid drugs augment immunotherapy via histone acetylation of MHCI machinery genes

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

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Substrate Specificity of the TRAMP Nuclear Surveillance Complexes

Project description:During nuclear surveillance in yeast, the RNA exosome functions together with the TRAMP complexes. These include the DEAH-box RNA helicase Mtr4 together with an RNA-binding protein (Air1 or Air2) and a poly(A) polymerase (Trf4 or Trf5). To better determine how RNA substrates are targeted, we analyzed protein and RNA interactions for TRAMP components. Mass spectrometry identified three distinct TRAMP complexes formed in vivo. These complexes preferentially assemble on different classes of transcripts. Unexpectedly, on many substrates, including pre-rRNAs and pre-mRNAs, binding specificity was apparently conferred by Trf4 and Trf5. Clustering of mRNAs by TRAMP association showed coenrichment for mRNAs with functionally related products, supporting the significance of surveillance in regulating gene expression. We compared binding sites of TRAMP components with multiple nuclear RNA binding proteins, revealing preferential colocalization of subsets of factors. TRF5 deletion reduced Mtr4 recruitment and increased RNA abundance for mRNAs specifically showing high Trf5 binding.

2020-07-02 | PXD017114 | Pride

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