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Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (iCLIP results)

ABSTRACT: Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (iCLIP results)

PROVIDER: PRJNA587446 | ENA |

REPOSITORIES: ENA

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Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (iCLIP results)

Project description:RNA granules are cellular condensates that contain RNAs and proteins. The mechanism that drive the recruitment of many mRNAs to RNA granules are not fully understood. Here we characterize the assembly and transcriptome of the germ (P) granules of C. elegans. We find that mRNAs are recruited into P granules by condensation with the intrinsically-disordered protein MEG-3. MEG-3 binds ~500 mRNAs in C. elegans embryos in a sequence-independent manner that favors mRNAs with low ribosome coverage. Translational stress causes additional mRNAs to localize to P granules and translational activation correlates with P granule exit for two mRNAs coding for germ cell fate regulators. MEG-3/RNA condensates assembled in vitro are gel-like and trap mRNAs in a non-dynamic state. Our observations reveal similarities between P granules and stress granules and identify gelation with intrinsically-disordered proteins as a sequence-independent mechanism to enrich low-translation mRNAs in RNA granules

2019-12-01 | GSE139878 | GEO

Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq datasets)

2019-12-01 | GSE139879 | GEO

Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq and ribosome profiling)

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Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins

Project description:Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins

| PRJNA587431 | ENA

Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq datasets)

Project description:Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq datasets)

| PRJNA587445 | ENA

Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq and ribosome profiling)

Project description:Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq and ribosome profiling)

| PRJNA587444 | ENA

BRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation

Project description:BRCA1/BARD1 is a tumor suppressor E3 ubiquitin (Ub) ligase with roles in DNA damage repair and in transcriptional regulation. BRCA1/BARD1 RING domains interact with nucleosomes to facilitate mono-ubiquitylation of distinct residues on the C-terminal tail of histone H2A. These enzymatic domains constitute a small fraction of the heterodimer, raising the possibility of functional chromatin interactions involving other regions such as the BARD1 C-terminal domains that bind nucleosomes containing the DNA damage signal H2A K15-Ub and H4 K20me0, or portions of the expansive intrinsically disordered regions found in both subunits. Herein, we reveal novel interactions that support robust H2A ubiquitylation activity mediated through a high-affinity, intrinsically disordered DNA-binding region of BARD1. These interactions support BRCA1/BARD1 recruitment to chromatin and sites of DNA damage in cells and contribute to their survival. We also reveal distinct BRCA1/BARD1 complexes that depend on the presence of H2A K15-Ub, including a complex where a single BARD1 subunit spans adjacent nucleosome units. Our findings identify an extensive network of multivalent BARD1-nucleosome interactions that serve as a platform for BRCA1/BARD1-associated functions on chromatin.

2023-06-21 | PXD035345 | Pride

Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins

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

2019-12-01 | GSE139881 | GEO

Proteomic and bioinformatic analysis of the nuclear intrinsically disordered proteome

Project description:Intrinsically disordered proteins (IDPs) are biologically active molecules which are involved in many cellular functions although they do not possess a defined three-dimensional structure. They are mostly signalling and regulatory proteins. This study is the first large-scale proteomic analysis of the nuclear IDPs. We experimentally showed that IDPs are overrepresented in the nucleus in comparison to the whole cell. The analysis in terms of molecular function indicated that nuclear intrinsically disordered proteome (IDP-ome) is enriched in proteins involved in transcription regulation and especially in transcription factors.

2015-09-21 | PXD002676 | Pride