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Using high-speed atomic force microscopy, the authors reveal the polymerization mechanism of VIPP1 into ESCRT-III-like filaments that adopt spiral and polygonal supramolecular structures.
Here, the authors show that cytoplasmic uridylyltransferases TUT7 and TUT4 bind let-7 pre-miRNA by alternative means in the absence and presence of Lin28A, which directly interacts with both RNA and enzyme to convert from a distributive to a processive mode of action.
Here the authors show that, upon embryo implantation, signaling triggers a large-scale rearrangement of protein–RNA interactions. Phosphorylated LIN28A reassembles onto the 3′ untranslated region termini of pluripotency-associated mRNAs, where it converges with the binding of poly(A)-binding protein and drives selective mRNA decay.
Here the authors establish that ploidy-to-cell size ratio is a highly conserved determinant of proteome composition. In both mammals and yeast, they find that growth in large cells is restricted by genome concentration as if it were a limiting nutrient.
Using cryo-electron microscopy, the authors obtained structures of Streptococcus pneumoniae nicotinamide adenine dinucleotide phosphate (NADPH) oxidase in different states. Combined with site-directed mutagenesis and biochemical assays, the structures shed light on the activity and regulation of NADPH oxidases.
Li et al. reveal the mechanism by which the ribosome termination complex catalyzes dissociation of GDP from release factor RF3 in Escherichia coli. The findings explain the guanine nucleotide exchange factor activity of the ribosome.
This study reveals the mechanisms of NEAT1 lncRNA maturation and menRNA biogenesis and uncovers an RNA-centric, riboswitch-like mechanism where menRNA drives its own conformational isomerization that directs repeat CCA addition and rapid degradation.
The idea of a scientific discovery is often linked to the eureka moment of a lone scientist, which then transforms our thinking. However, scientific discoveries are never made by individuals in isolation. They build on the work of countless researchers, and often require interdisciplinary and collaborative teams of researchers.
Lavdovskaia, Hanitsch, Linden et al. provide a comprehensive roadmap of mitoribosome biogenesis and establish that mitochondria use a unique pathway for the assembly of their translation machinery.
The authors follow the folding dynamics of a nascent protein trapped during its synthesis, showing how the ribosome and a molecular chaperone shape the pathway of protein folding.
Curiosity-driven and fundamental discovery science must be justified in its importance to human health and translational potential for practical applications and cures. However, many groundbreaking discoveries occur through the freedom to ask fundamental questions — the how and why — without knowing where they lead. Presented here is an example of a clinical target that emerged from a seemingly simple question in chromosome biology.
AlphaFold 3 represents a breakthrough in predicting the 3D structures of complexes directly from their sequences, offering insights into biomolecular interactions. Extending predictions to molecular behavior and function requires a shift from viewing biomolecules as static 3D structures to dynamic conformational ensembles.
Here the authors assemble a toolkit to probe K48–K63-branched ubiquitin chain function. By identifying specific binders and deubiquitinases and engineering a specific nanobody, they reveal the importance of these chains in p97-dependent processes.
Microtubules within cells often have 13 protofilaments but are nucleated by multi-protein y-TuRCs complexes that display 14 γ-tubulin molecules. High-resolution cryo-EM structures of γ-TuRCs after nucleation show that these γ-TuRCs ‘close’ during nucleation to display only 13 γ-tubulin molecules for protofilament assembly.
Here, the authors show that the canonical BRG/BRM-associated factor (SWI/SNF) chromatin remodeler generates subnucleosomes containing 50–80 bp of DNA associated with the four core histones. These hemisome-like particles interact with OCT4 to expand its binding domain at enhancers.
The authors uncover a Père David’s deer-like design for long noncoding RNAs such as metastasis-associated lung adenocarcinoma transcript 1 (MALAT1), which partially mimics the transfer RNA (tRNA) structure to recruit select tRNA processing enzymes for maturation and to create novel regulatory RNAs such as the MALAT1-associated small cytoplasmic RNA.
Cryo-EM structures of the human mitochondrial chaperone Hsp60 reveal alternating apical domain conformations that enable simultaneous client and co-chaperone interactions. These results provide a structural mechanism for efficient client capture and chaperone cycling.
This study uses single-base tiled screens, bioinformatics, comprehensive mutagenesis and proteomics to provide a high-resolution view of RNA silencing with PspCas13b. It reveals design principles for potent silencing without collateral effects.