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Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing [fCLIP-seq]

ABSTRACT: Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing [fCLIP-seq]

PROVIDER: PRJNA611047 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11263282_1.fastq.gz	Fastqsanger.gz
	SRR11263282_2.fastq.gz	Fastqsanger.gz
	SRR11263283_1.fastq.gz	Fastqsanger.gz
	SRR11263283_2.fastq.gz	Fastqsanger.gz
	SRR11263284_1.fastq.gz	Fastqsanger.gz

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Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing

Project description:Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing

| PRJNA611053 | ENA

Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing

Project description:TENT4 enzymes generate “mixed tails” on mRNAs by adding adenosines with intermittent non-adenosine residues, which protect mRNAs from deadenylation. Here we discover the extensive mixed tailing in the transcripts of two distinct DNA viruses, hepatitis B virus (HBV) and human cytomegalovirus (HCMV), and their striking similarity in the mechanism to exploit the TENT4-ZCCHC14 complex. TAIL-seq analyses of HBV and HCMV RNAs revealed that TENT4A and TENT4B are responsible for the mixed tailing and protection of viral poly(A) tails. By fCLIP-seq on HBV-producing cells, we found that the HBV posttranscriptional regulatory element (PRE) is the primary site of the TENT4 interactome. A hairpin with a CNGGN-type pentaloop in the PRE is critical for TENT4-dependent regulation. Unexpectedly, HCMV also utilizes a similar pentaloop hairpin, an interesting example of convergent evolution. We further found that the CNGGN pentaloop is recognized by the SAM domain-containing ZCCHC14 protein which in turn recruits TENT4 to stabilize viral transcripts. Altogether, our study reveals the action mechanism of PRE that has been widely used to enhance gene expression, and introduces the TENT4-ZCCHC14 complex as the key host factor and a potential target for antiviral therapeutics.

2020-04-27 | PXD018061 | Pride

Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing [TAIL-seq]

Project description:Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing [TAIL-seq]

| PRJNA611056 | ENA

Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing [TAIL-seq]

2020-03-09 | GSE146600 | GEO

Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing [fCLIP-seq]

2020-03-09 | GSE146597 | GEO

Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing

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

2020-03-09 | GSE146602 | GEO

Mixed tailing by TUT3 and TUT5 shields mRNA from rapid deadenylation [TAIL-Seq]

Project description:RNA tails play integral roles in the control of mRNA translation and decay. Guanylation of poly(A) tail was discovered recently, yet the enzymology and function remain obscure. Here we identify TUT3 (PAPD5) and TUT5 (PAPD7) (TUT3/5) as the enzymes responsible for mRNA guanylation. Purified TUT3/5 predominantly incorporate GTPs to generate a mixed poly(A) tail with intermittent non-adenosine residues. A single guanosine is sufficient to impede the deadenylation complex (CCR4-NOT) which trims the tail and exposes guanosine at the 3′ end. Consistently, the depletion of TUT3/5 leads to a decrease in mRNA half-life and abundance in cells. Thus, TUT3/5 produce a mixed tail which shields the mRNA from rapid deadenylation. Our study unveils the role of mixed tailing, and expands the complexity of post-transcriptional gene regulation.

2019-06-09 | GSE116349 | GEO

Mixed tailing by TUT3 and TUT5 shields mRNA from rapid deadenylation [RNA-Seq]

2019-06-09 | GSE115529 | GEO

Mixed tailing by TUT3 and TUT5 shields mRNA from rapid deadenylation

Project description:Mixed tailing by TUT3 and TUT5 shields mRNA from rapid deadenylation

| PRJNA478241 | ENA

Tailing Biocrusts

Project description:Tailing Biocrusts Metagenome

| PRJNA1046590 | ENA