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The human CCHC-type Zinc Finger nucleic acid binding protein binds G-rich elements in target mRNA coding sequences initiation promotes translation.

ABSTRACT: The human CCHC-type Zinc Finger nucleic acid binding protein binds G-rich elements in target mRNA coding sequences initiation promotes translation.

PROVIDER: PRJNA359689 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5137670.fastq.gz	Fastqsanger.gz
	SRR5137680.fastq.gz	Fastqsanger.gz
	SRR5137671.fastq.gz	Fastqsanger.gz
	SRR5137681.fastq.gz	Fastqsanger.gz
	SRR5137672.fastq.gz	Fastqsanger.gz

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The human CCHC-type Zinc Finger nucleic acid binding protein binds G-rich elements in target mRNA coding sequences initiation promotes translation (Ribosome profiling).

Project description:CNBP is a eukaryote-conserved nucleic-acid binding protein required in mammals for embryonic development. It contains seven CCHC-type zinc-finger domains and was suggested to act as a nucleic acid chaperone, as well as a transcription factor. Here, we identify all CNBP isoforms as cytoplasmic messenger RNA (mRNA)-binding proteins. Using Photoactivatable Ribonucleoside Enhanced Cross-linking and Immunoprecipitation, we mapped its binding sites on RNA at nucleotide-level resolution on a genome-wide scale and find that CNBP interacted with 3961 mRNAs in human cell lines, preferentially at a G-rich motif close to the AUG start codon on mature mRNAs. Loss- and gain-of-function analyses coupled with system-wide RNA and protein quantification revealed that CNBP did not affect RNA abundance, but rather promoted translation of its targets. This is consistent with an RNA chaperone function of CNBP helping to resolve secondary structures, thus promoting translation.

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The human CCHC-type Zinc Finger nucleic acid binding protein binds G-rich elements in target mRNA coding sequences initiation promotes translation (RNA-Seq).

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Project description:Infection of animal cells by many viruses is detected and countered by a variety of means, including recognition of non-self nucleic acids. The zinc-finger antiviral protein (ZAP) depletes cytoplasmic RNA that is recognized as foreign in mammalian cells by virtue of its elevated CG dinucleotide content compared to endogenous mRNAs. Here, we determined a crystal structure of a protein-RNA complex containing the N-terminal, four-zinc finger human (h) ZAP RNA binding domain (RBD), and a CG dinucleotide-containing RNA target. The structure reveals in molecular detail how hZAP is able to bind selectively to CG-rich RNA. Specifically, the four zinc fingers create a basic patch on the hZAP RBD surface. The highly basic second zinc finger contains a pocket that selectively accommodates CG dinucleotide bases. Structure guided mutagenesis, crosslinking-immunoprecipitation-sequencing assays, and RNA affinity assays show that the structurally defined CG-binding pocket is not required for RNA binding per se in human cells. However, the pocket is a crucial determinant of high affinity specific binding to CG-dinucleotide-containing RNA. Moreover, variations in the RNA binding specificity a panel of CG-binding pocket mutants quantitatively predict their selective antiviral activity against a CG-enriched HIV-1 strain. Overall, the hZAP RBD:RNA structure provides an atomic-level explanation for how ZAP selectively targets foreign, CG-rich RNA.

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