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Structural basis for pre-miRNA-31 biogenesis

ABSTRACT: Structural basis for pre-miRNA-31 biogenesis

PROVIDER: PRJNA957777 | ENA |

REPOSITORIES: ENA

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Structural basis for pre-miRNA-31 biogenesis

Project description:MicroRNAs (miRNAs) are a class of small non-coding RNAs that regulate protein gene expression post-transcriptionally. By base pairing with target mRNAs, miRNAs triggers mRNA degradation or translational suppression[1-4]. Abnormal miRNAs levels are associated with cancers, diabetes, neurological and other diseases[5-8]. RNA polymerase II transcribes primary miRNA (pri-miR) in the nucleus and pri-miRs are subsequently processed by Microprocessor, which is composed of Drosha and DiGeorge syndrome critical region 8 (DGCR8) proteins, to generate precursor miRNAs (pre-miRs). Pre-miRs are exported from the nucleus to the cytoplasm in a GTP-dependent manner by Exportin-5. In the cytoplasm, a pre-miRs are further processed by Dicer to generate 21-22 nt mature miRNA[4, 9]. Argonaute (Ago) protein loads one of mature miRNAs into protein and forms miRNA-induced silencing complex, which is responsible for mRNA degradation or translational suppression[2, 4].

2023-04-24 | GSE230167 | GEO

Structural basis of MALAT1 RNA maturation and mascRNA biogenesis

Project description:Structural basis of MALAT1 RNA maturation and mascRNA biogenesis

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Structural basis for 5’-ETS recognition by Utp4 at the early stages of ribosome biogenesis

Project description:Structural basis for 5’-ETS recognition by Utp4 at the early stages of ribosome biogenesis

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Structural Basis for Target-Directed MicroRNA Degradation

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Structural basis of virulence activation in Francisella tularensis

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The structural basis for cohesin/CTCF anchored loops

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Structural basis of MALAT1 RNA maturation and mascRNA biogenesis

Project description:MALAT1 lncRNA plays key roles in regulating transcription, splicing, and tumorigenesis. Its maturation and stabilization require precise processing by RNase P, which simultaneously initiates the biogenesis of a 3′ cytoplasmic mascRNA. mascRNA was proposed to fold into a tRNA-like secondary structure, but lacks eight conserved linking residues required by the canonical tRNA fold. Here, we report crystal structures of human mascRNA before and after processing, which reveal an ultracompact, quasi-tRNA-like structure. Despite lacking all linker residues, mascRNA faithfully recreates the characteristic “elbow” feature of tRNAs to recruit RNase P and ELAC2 for processing, which exhibit distinct substrate specificities. Rotation and repositioning of the D-stem and anticodon regions preclude mascRNA from aminoacylation, avoiding interference with translation. Therefore, a class of metazoan lncRNAs employ a previously unrecognized, unusually streamlined quasi-tRNA architecture to recruit select tRNA-processing enzymes while excluding others, to drive bespoke RNA biogenesis, processing, and maturation.

2024-03-18 | GSE248290 | GEO

Structural basis for 5’-ETS recognition by Utp4 at the early stages of ribosome biogenesis

Project description:Eukaryotic ribosome biogenesis begins with the co-transcriptional assembly of the 90S pre-ribosome. The ‘U three protein’ (UTP) complexes and snoRNA particles arrange around the nascent pre-ribosomal RNA chaperoning its folding and further maturation. The earliest event in this hierarchical process is the binding of the UTP-A complex to the 5’-end of the pre-ribosomal RNA (5’-ETS). This oligomeric complex predominantly consists of β-propeller and α-solenoidal proteins. Here we present the structure of the Utp4 subunit from the thermophilic fungus Chaetomium thermophilum at 2.15 Å resolution and analyze its function by UV RNA-crosslinking (CRAC) and in context of a recent cryo-EM structure of the 90S pre-ribosome. Utp4 consists of two orthogonal and highly basic β-propellers that perfectly fit the EM-data. The Utp4 structure highlights an unusual Velcro-closure of its C-terminal β-propeller as relevant for protein integrity and Utp8 recognition in the context of the pre-ribosome. We provide a first model of the 5’-ETS RNA from an internally hidden 5’-end up to the region that hybridizes to the 3’-hinge sequence of U3 snoRNA and validate a specific Utp4/5’-ETS interaction by CRAC analysis. Altogether Utp4 is central to the UTP-A complex and organizes the 5’-ETS for further maturation.

2017-06-06 | GSE98331 | GEO

Snapshots of native pre-50S ribosomes reveal a biogenesis factor network and evolutionary specialization

Project description:Ribosome biogenesis is a fundamental multi-step cellular process that culminates in the formation of the ribosomal subunits, whose production and modifications are steered and regulated by numerous biogenesis factors. In this study, we analyze unperturbed native prokaryotic ribosome biogenesis by isolating bona fide pre-50S subunits by using an E. coli strain, producing the affinity tagged biogenesis factor ObgE from its native gene locus. Our integrative structural approach reveals a network of interacting biogenesis factors consisting of YjgA, RluD, RsfS and ObgE on the immature pre-50S subunit. In addition, our study provides mechanistic insight into how the GTPase ObgE, in concert with other biogenesis factors, facilitates the maturation of the 50S functional core and reveals both conserved and divergent evolutionary features of ribosome biogenesis between prokaryotes and eukaryotes.

2020-12-23 | PXD021374 | Pride

Structural basis for DNMT3A-mediated de novo DNA methylation

Project description:Structural basis for DNMT3A-mediated de novo DNA methylation

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