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Novel RNA binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria

ABSTRACT: YebC enhances translation of prolin-rich motifs

PROVIDER: PRJEB78417 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	riboseq-comp_1.bam	Bam
	riboseq-comp_1.bam.bai	Bam
	riboseq-comp_2.bam	Bam
	riboseq-comp_2.bam.bai	Bam

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Respiratory syncytial virus (RSV) enhances translation of virus-resembling AU-rich host transcripts

Project description:Respiratory syncytial virus (RSV) enhances translation of virus-resembling AU-rich host transcripts

| PRJNA1118414 | ENA

Respiratory syncytial virus (RSV) enhances translation of virus-resembling AU-rich host transcripts

Project description:Viral infection often triggers eukaryotic initiator factor 2α (eIF2α) phosphorylation, leading to global 5’-cap-dependent translation inhibition. RSV encodes messenger RNAs (mRNAs) mimicking 5’-cap structures of host mRNAs and thus inhibition of cap-dependent translation initiation would likely also reduce viral translation. We confirmed that RSV limits widespread translation initiation inhibition and unexpectedly found that the fraction of ribosomes within polysomes increases during infection, indicating higher ribosome loading on mRNAs during infection. We found that AU-rich host transcripts that are less efficiently translated under normal conditions become more efficient at recruiting ribosomes, similar to RSV transcripts. Viral transcripts are transcribed in cytoplasmic inclusion bodies, where the viral AU-rich binding protein M2-1 has been shown to bind viral transcripts and shuttle them into the cytoplasm. We further demonstrated that M2-1 is found on polysomes, and that M2-1 might deliver host AU-rich transcripts for translation.

2024-09-03 | GSE268742 | GEO

mRNA circularization by METTL3-eIF3h enhances translation

Project description:mRNA circularization by METTL3-eIF3h enhances translation

| PRJNA481680 | ENA

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

MCT-1 enhances translation

Project description:MCT-1 is an oncogene initially identified in a human T-cell lymphoma. Subsequently, MCT-1 protein levels were found to be elevated in a subset of diffuse large B-cell lymphoma. Forced expression of MCT-1 has recently been shown to induce cell proliferation as well as activate survival-related pathways protecting lymphoid cells from apoptosis. We document here that MCT-1 interacts with the density-regulated protein (DENR/DRP), containing the SUI1 translation initiation domain, found in many translation initiation factors. MCT-1 contains the PUA domain, a recently described RNA binding domain that is found in several tRNA and rRNA modification enzymes. Our findings established that MCT-1 protein is interacting with the cap complex through its PUA domain and enhances translation. Furtheremore, our data support a putative role for the MCT-1 oncogene in translation and suggests a mechanism for its role in lymphomagenesis. Keywords: Gene upregulation by MCT-1

2006-09-15 | GSE4805 | 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 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. [RNA-Seq]

2016-01-08 | GSE76627 | GEO

mRNA circularization by METTL3-eIF3h enhances translation

Project description:N6-methyladenosine (m6A) modification of mRNA catalyzed by METTL3 is enriched at a subset of stop codons. METTL3 can promote translation but the mechanism and widespread relevance remain unknown. Here we show that METTL3 enhances translation only when tethered to reporter mRNA at sites close to the stop codon supporting a mRNA looping mechanism for ribosome recycling and translational control. Electron microscopy revealed the topology of individual polyribosomes with single METTL3 foci found in close proximity to 5’ cap-binding proteins. We identify a direct physical and functional interaction between METTL3 and the eukaryotic translation initiation factor 3 subunit h (eIF3h). METTL3 promotes translation of a large subset of oncogenic mRNAs, including BRD4 that are also m6A-modified in human primary lung tumors. The METTL3-eIF3h interaction is required for enhanced translation, formation of densely packed polyribosomes, and oncogenic transformation. METTL3 depletion inhibits tumorigenicity and sensitizes lung cancer cells to BRD4 inhibition. These findings uncover a mRNA looping mechanism of translation control and identify METTL3-eIF3h as a potential cancer therapeutic target.

2018-09-21 | GSE117299 | GEO

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