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The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation.

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE76629 | GEO | 2016/01/08

SECONDARY ACCESSION(S): PRJNA308194

REPOSITORIES: GEO

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The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation.

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2016-01-08 | E-GEOD-76629 | biostudies-arrayexpress

The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation. [PAR-CLIP]

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. CNBP PAR-CLIP

2016-01-08 | E-GEOD-76193 | biostudies-arrayexpress

The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation. [RNA-Seq]

2016-01-08 | E-GEOD-76627 | biostudies-arrayexpress

The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation. [RNA-Seq]

2016-01-08 | GSE76627 | GEO

The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation. [PAR-CLIP]

2016-01-08 | GSE76193 | GEO

The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation.

Project description:The human cellular nucleic acid binding protien binds G-rich elements close to translation initiation sires and promotes translation.

| PRJNA308194 | ENA

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

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

2020-01-02 | GSE93053 | GEO

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

2020-01-02 | GSE93052 | GEO

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

2020-01-02 | GSE93051 | GEO

The Human CCHC-type Zinc Finger Nucleic Acid-Binding Protein Binds G-Rich Elements in Target mRNA Coding Sequences and Promotes Translation.

Project description:The CCHC-type zinc finger nucleic acid-binding protein (CNBP/ZNF9) is conserved in eukaryotes and is essential for embryonic development in mammals. It has been implicated in transcriptional, as well as post-transcriptional, gene regulation; however, its nucleic acid ligands and molecular function remain elusive. Here, we use multiple systems-wide approaches to identify CNBP targets and function. We used photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation (PAR-CLIP) to identify 8,420 CNBP binding sites on 4,178 mRNAs. CNBP preferentially bound G-rich elements in the target mRNA coding sequences, most of which were previously found to form G-quadruplex and other stable structures in vitro. Functional analyses, including RNA sequencing, ribosome profiling, and quantitative mass spectrometry, revealed that CNBP binding did not influence target mRNA abundance but rather increased their translational efficiency. Considering that CNBP binding prevented G-quadruplex structure formation in vitro, we hypothesize that CNBP is supporting translation by resolving stable structures on mRNAs.

| S-EPMC5393907 | biostudies-literature

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