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An adenosine analog shows high antiviral potency against coronavirus and arenavirus mainly through an unusual base pairing mode.
Nat Commun
December 2024
Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China.
By targeting the essential viral RNA-dependent RNA polymerase (RdRP), nucleoside analogs (NAs) have exhibited great potential in antiviral therapy for RNA virus-related diseases. However, most ribose-modified NAs do not present broad-spectrum features, likely due to differences in ribose-RdRP interactions across virus families. Here, we show that HNC-1664, an adenosine analog with modifications both in ribose and base, has broad-spectrum antiviral activity against positive-strand coronaviruses and negative-strand arenaviruses.
View Article and Find Full Text PDFCross-regulation of RNA methylation modifications and R-loops: from molecular mechanisms to clinical implications.
Cell Mol Life Sci
December 2024
Department of Urology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
R-loops, RNA-DNA hybrid structures, are integral to key cellular processes such as transcriptional regulation, DNA replication, and repair. However, aberrant accumulation of R-loops can compromise genomic integrity, leading to the development of various diseases. Emerging evidence underscores the pivotal role of RNA methylation modifications, particularly N6-methyladenosine (mA) and 5-methylcytosine (mC), in orchestrating the formation, resolution, and stabilization of R-loops.
View Article and Find Full Text PDFFree amino acids accelerate the time-dependent inactivation of rat liver nucleotide pyrophosphatase/phosphodiesterase Enpp3 elicited by EDTA.
Amino Acids
December 2024
Departamento de Bioquímica y Biología Molecular y Genética, Facultad de Medicina y Ciencias de la Salud, Universidad de Extremadura, 06006, Badajoz, Spain.
Nucleotide-pyrophosphatases/phosphodiesterases (NPP/PDE) are membrane or secreted Zn-metallohydrolases of nucleoside-5´-monophosphate derivatives. They hydrolyze, for instance, ATP and 4-nitrophenyl-dTMP, and belong to the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family that contains seven members (ENPP1-ENPP7). Earlier we had shown that an NPP/PDE activity solubilized and partially purified from rat liver membranes is inactivated by EDTA in a time-dependent fashion, an effect enhanced by glycine and blocked by the 4-nitrophenyl-dTMP.
View Article and Find Full Text PDFTheoretical Insights on the Excited State Deactivation Mechanism in Protonated Adenosine.
J Phys Chem A
December 2024
Department of Chemistry, University of Isfahan, 81746-73441 Isfahan, Iran.
We present herein our computational exploration of the conformational landscape and photophysical properties of protonated adenosine (AdoH). Several different protonated isomers and conformers have been considered and their relevant photophysical properties have been addressed. From our quantum computational results, an S/S conical intersection (CI) has been located for all considered conformers, providing a significant route for the ultrafast deactivation mechanism of the S excited state of AdoH.
View Article and Find Full Text PDFStructures of KEOPS bound to tRNA reveal functional roles of the kinase Bud32.
Nat Commun
December 2024
Department of Molecular Genetics, University of Toronto, Toronto, ON, M5S 1A8, Canada.
Article Synopsis
- KEOPS is a crucial enzyme complex that modifies tRNAs, specifically adding a N-threonylcarbamoyl adenosine (tA) modification essential for protein synthesis in eukaryotes and archaea.
- Mutations in any of the KEOPS subunits can cause Galloway Mowat Syndrome (GAMOS) in humans, highlighting the complex's significance in cellular function.
- Recent cryogenic electron microscopy studies revealed how KEOPS interacts with tRNA, showing that its structure changes during modification and emphasizing the roles of all subunits, especially Bud32, in regulating tRNA modification.
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