Publications by authors named "I S Abaeva"
Polypeptides arising from interrupted translation undergo proteasomal degradation by the ribosome-associated quality control (RQC) pathway. The ASC-1 complex splits stalled ribosomes into 40S subunits and nascent chain-tRNA-associated 60S subunits (60S RNCs). 60S RNCs associate with NEMF that promotes recruitment of the RING-type E3 ubiquitin (Ub) ligase Listerin (Ltn1 in yeast), which ubiquitinates nascent chains.
View Article and Find Full Text PDFArticle Synopsis
- Viral internal ribosomal entry sites (IRESs) are RNA elements that enable translation to start without the usual requirement for a cap structure, and they come in different classes based on their structural features.
- Research has uncovered new types of IRESs that vary in size and complexity, with some having tandem pseudoknots and others showing unique structural elements that enhance their function.
- The study also suggests that IRESs evolve through mechanisms such as the incremental addition of structural components and recombination of different RNA sequences, helping to explain their diversity across various viral genomes.
Article Synopsis
- - SARS CoV-2's nonstructural protein 1 (Nsp1) plays a crucial role in blocking host protein synthesis by hindering the start of translation and causing degradation of cellular mRNAs.
- - The study found that Nsp1's cleavage of various mRNAs (like β-globin, EMCV IRES, and CrPV IRES) requires only translational components and specific initiation factors, showing that a cellular endonuclease isn't involved.
- - Key findings include the identification of essential charged residues on Nsp1 and the eIF3g protein that are necessary for mRNA cleavage, which occurs at a specific site, emphasizing the general importance of these protein domains across different mRNAs. *
Internal ribosomal entry sites (IRESs) engage with the eukaryotic translation apparatus to promote end-independent initiation. We identified a conserved class of ∼150 nt long intergenic region (IGR) IRESs in dicistrovirus genomes derived from members of the phyla Arthropoda, Bryozoa, Cnidaria, Echinodermata, Entoprocta, Mollusca and Porifera. These IRESs, exemplified by Wenling picorna-like virus 2, resemble the canonical cricket paralysis virus (CrPV) IGR IRES in comprising two nested pseudoknots (PKII/PKIII) and a 3'-terminal pseudoknot (PKI) that mimics a tRNA anticodon stem-loop base-paired to mRNA.
View Article and Find Full Text PDFArticle Synopsis
- SARS CoV-2 nonstructural protein 1 (Nsp1) inhibits host translation by blocking initiation and causing cleavage of cellular mRNAs.
- The study found that cleavage requires Nsp1 and only standard translation components, with different initiation factors needed for different mRNAs.
- Key residues in Nsp1's N-terminal domain and eIF3g's RRM domain were identified as crucial for the cleavage process, indicating their role is consistent across various mRNA types.