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High-resolution fleezers reveal duplex opening and stepwise assembly by an oligomer of the DEAD-box helicase Ded1p.
Nat Commun
January 2025
Department of Physics and Astronomy, Michigan State University, East Lansing, MI, USA.
DEAD-box RNA-dependent ATPases are ubiquitous in all domains of life where they bind and remodel RNA and RNA-protein complexes. DEAD-box ATPases with helicase activity unwind RNA duplexes by local opening of helical regions without directional movement through the duplexes and some of these enzymes, including Ded1p from Saccharomyces cerevisiae, oligomerize to effectively unwind RNA duplexes. Whether and how DEAD-box helicases coordinate oligomerization and unwinding is not known and it is unclear how many base pairs are actively opened.
View Article and Find Full Text PDFPeri-centrosomal localization of small interfering RNAs in C. elegans.
Sci China Life Sci
January 2025
Department of Obstetrics and Gynecology, The First Affiliated Hospital of USTC, The USTC RNA Institute, Ministry of Education Key Laboratory for Membraneless Organelles & Cellular Dynamics, Hefei National Research Center for Physical Sciences at the Microscale, Center for Advanced Interdisciplinary Science and Biomedicine of IHM, School of Life Sciences, Division of Life Sciences and Medicine, Biomedical Sciences and Health Laboratory of Anhui Province, University of Science and Technology of China, Hefei, 230027, China.
The centrosome is the microtubule-organizing center and a crucial part of cell division. Centrosomal RNAs (cnRNAs) have been reported to enable precise spatiotemporal control of gene expression during cell division in many species. Whether and how cnRNAs exist in C.
View Article and Find Full Text PDFThe RNA-dependent association of phosphatidylinositol 4,5-bisphosphate with intrinsically disordered proteins contribute to nuclear compartmentalization.
PLoS Genet
December 2024
Department of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.
Article Synopsis
- RNA is essential for forming nuclear compartments, with phosphatidylinositol 4,5-bisphosphate (PIP2) playing a key role in RNA transcription and localization in these compartments.
- The study identified the RNA-dependent PIP2-associated (RDPA) nuclear proteome, revealing that proteins in this group often have intrinsically disordered regions that can bind to PIP2 and possess modification sites.
- Highlighting the relationship between PIP2 and RNA, the research found that the protein BRD4 interacts with PIP2 in an RNA-dependent manner, suggesting that PIP2 is crucial for organizing nuclear processes necessary for gene expression.
Coxsackievirus B3-Induced mA Modification of RNA Enhances Viral Replication via Suppression of YTHDF-Mediated Stress Granule Formation.
Microorganisms
October 2024
Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.
N6-methyladenosine (mA) is the most prevalent internal RNA modification. Here, we demonstrate that coxsackievirus B3 (CVB3), a common causative agent of viral myocarditis, induces mA modification primarily at the stop codon and 3' untranslated regions of its genome. As a positive-sense single-stranded RNA virus, CVB3 replicates exclusively in the cytoplasm through a cap-independent translation initiation mechanism.
View Article and Find Full Text PDFDecoding the interplay between mA modification and stress granule stability by live-cell imaging.
Sci Adv
November 2024
Shenzhen Bay Laboratory, Shenzhen 518132, China.
-methyladenosine (mA)-modified mRNAs and their cytoplasmic reader YTHDFs are colocalized with stress granules (SGs) under stress conditions, but the interplay between mA modification and SG stability remains unclear. Here, we presented a spatiotemporal mA imaging system (SMIS) that can monitor the mA modification and the translation of mRNAs with high specificity and sensitivity in a single live cell. SMIS showed that mA-modified reporter mRNAs dynamically enriched into SGs under arsenite stress and gradually partitioned into the cytosol as SG disassembled.
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