Acronicta psi
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA871019 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| ERR10038430_1.fastq.gz | Fastqsanger.gz | |||
| ERR10038430_2.fastq.gz | Fastqsanger.gz | |||
| ERR10033482.fastq.gz | Fastqsanger.gz | |||
| ERR10890701_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 6 |
Similar Datasets
Project description:Acronicta rumicis Mitochondrial Genome sequencing and assembly
| PRJNA932563 | ENA
Project description:Pseudouridine (Ψ) is known for decades, but its flexibility in base-pairing remains unclear. This study engineers artificial box H/ACA guide RNAs to direct pseudouridylation at the uridine of a premature termination codon (PTC; UAA, UAG, or UGA) within an intron-less mRNA and U36 of the anticodon of a matching tRNA in yeast and human cells. Targeted pseudouridylation leads to the formation of a Ψ-Ψ codon-anticodon pair, which, together with the other two Watson-Crick base pairs in the codon-anticodon duplex, significantly improves codon-anticodon recognition, robustly promoting PTC read-through. The intron-less mRNA level remains unchanged with or without guide RNAs. Additionally, pseudouridylation does not impact tRNA stability or charging. Our results show that nonsense suppression is promoted by the high affinity of the Ψ-Ψ pair, which is verified by melting curve analysis. This work has identified an unusual Ψ-Ψ base pair, which contributes significantly to codon-anticodon recognition and translational recoding.
2025-06-20 | GSE299290 | GEO
Project description:Prions are infectious proteins that can adopt a structural conformation different from that of the normal protein. This change of conformation is then propagated among other molecules of the same protein. Prions are associated with neurodegenerative diseases in mammals, but are also found in fungi (in the yeast Saccharomyces cerevisiae and the filamentous fungus Podospora anserina), in which they control heritable traits. They are widespread in wild yeast strains, suggesting a biologically important role. [PSI+] is one of the most widely studied yeast prions. It corresponds to an aggregated conformation of the translational release factor, eRF3, which suppresses nonsense codons. [PSI+] modifies cellular fitness, inducing various phenotypes, depending on the genetic background. However, the genes displaying [PSI+]-controlled expression remain largely unknown. We used the recently described ribosome profiling approach to identify genes displaying changes in expression in the presence of [PSI+]. This made it possible to determine the positions of all active ribosomes within the genome, in both [PSI+] and [PSI-] isogenic strains. Comparisons of the translatomes and transcriptomes of the two strains revealed that the primary effect of [PSI+] was to repress genes involved in the stress response. Thus, we provide the first description of the global translational effect of [PSI+] and a new genetic explanation of the phenotypic differences between [PSI-] and [PSI+] strains under stress conditions.
2014-07-18 | GSE41590 | GEO
Project description:Chlamydomonas reinhardtii PSI-Cyt b6f complexes from sucrose density gradient fractions were identified by western blot and SMF spectroscopy, but showed high heterogeneity, as evident from the multiple bands present in the Coomassie stained SDS gel and original EM micrographs. Therefore potential PSI-Cyt b6f supercomplexes were enriched by a subsequent PsaA HisTag purification step. Only this additional enrichment enabled the identification of novel PSI supercomplexes, although the sample remained far from being homogeneous. This dataset describes the quantitative mass spectrometric analysis of the enriched PSI supercomplex fraction in comparison to unpurified samples using metabolic 15N labeling.
2018-10-03 | PXD008857 | Pride