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Examining how TNRC6 binding to its targets changes with the T6B peptide using RIPseq

ABSTRACT: Examining how TNRC6 binding to its targets changes with the T6B peptide using RIPseq

PROVIDER: PRJNA1224206 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR32358428_1.fastq.gz	Fastqsanger.gz
	SRR32358428_2.fastq.gz	Fastqsanger.gz
	SRR32358429_1.fastq.gz	Fastqsanger.gz
	SRR32358429_2.fastq.gz	Fastqsanger.gz
	SRR32358430_1.fastq.gz	Fastqsanger.gz

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Examining how TNRC6 binding to its targets changes with the T6B peptide using RIPseq

Project description:Prior studies have demonstrated that the T6B peptide can selectively de-repress miRNA targets in non-neuronal cells. However, since neurons may have a different expression profile of miRNA pathway genes as well as other binding partners of TNRC6, we sought to validate the intended function of T6B in neurons. We performed RNA immunoprecipitation of TNRC6 followed by sequencing (TNRC6 RIPseq) in cultured cortical pyramidal neurons transduced with mutant T6B (control) or T6B. We reasoned that TNRC6 would indirectly pull down miRNA targets through its high-affinity binding with AGO in control neurons, but not in the presence of T6B, which outcompetes TNRC6 binding to AGO.

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ripseq experiment for rfl8 targets - Functional characterization of the pentatricopeptide repeat protein PPR RFL8

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Project description:Through the RNA interference (RNAi) pathway, small RNAs can influence translation, splicing, transcriptional activation, and transcriptional repression. RNAi is carried out by the targeting Argonaute (Ago) effector protein and the facilitating TNRC6 (also known as GW182) scaffolding protein. Here, we use a suite of gene knockout cell lines and high-throughput sequencing to gather definitive answers about the TNRC6 paralogs, their roles in the cell, and their relation to Ago knockout cell lines. Each subsequent TNRC6 paralog knockout caused more gene changes and few genes overlapped between the single TNRC6 paralog knockouts. In addition, TNRC6 knockout and Ago knockout cell lines’ gene expression profiles are highly correlated with one another, indicating the important regulatory functions these proteins share. Overall we found that in spite of less than 40% sequence identity, TNRC6 paralogs are functionally redundant and can replace one another for core RNAi functions.

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Ago-APP: a GW peptide-based Argonaute affinity capture strategy

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ripseq experiment for rfl8 targets - Functional characterization of the pentatricopeptide repeat protein PPR RFL8

Project description:ripseq experiment for rfl8 targets - Functional characterization of the pentatricopeptide repeat protein PPR RFL8

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miR-122-dependent binding of TNRC6 to HCV RNA

Project description:The liver-specific microRNA, miR-122, is an essential host factor for replication of hepatitis C virus (HCV), an important infectious cause of chronic liver disease and hepatocellular carcinoma. miR-122 stabilizes the positive-strand HCV RNA genome and promotes viral RNA synthesis by binding two closely spaced sites (S1 and S2) near the 5’ end of the genome in association with Ago2. Ago2 is essential for both host factor activities, but whether other host proteins are involved is unknown. Using a quantitative proteomics approach, we identified TNRC6A (GW182) and its paralogs (TNRC6B and TNRC6C), as functionally important components of the miR-122/Ago2 host factor complex binding HCV RNA. Depletion of any two TNRC6 proteins reduced HCV replication in Huh-7.5 cells,but did not reduce viral RNA stability or translational activity, but rather dampened miR-122 stimulation of viral RNA synthesis. However, TNRC6 depletion had no effect on replication of HCV in which S2 was mutated so that miR-122 binds only S1, whereas it significantly enhanced replication when S1 was mutated and only S2 bound by miR-122. Consistent with this, we found that TNRC6 proteins preferentially associate with the S1 site, and that the association of Ago2 with S2 is increased in TNRC6-depleted cells. Collectively, these data suggest a model in which TNRC6 proteins, which are known to interact with Ago2, preferentially direct the miR-122/Ago2 complex to S1 while restricting its association with S2, thereby fine tuning the spatial organization of miR-122/Ago2 complexes bound to the viral RNA.

2019-04-24 | PXD013054 | Pride

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