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The authors use cryo-electron microscopy to reveal two structural states of Ca2+-activated gelsolin bound to the actin filament, illuminating the mechanisms of filament severing and barbed end capping.
This study presents the cryo-electron microscopy structure of Fanzor2, showcasing its unique structural elements and nucleic acid interaction sites. A comparison to TnpB-related RNA-guided endonucleases highlights divergent evolutionary paths.
Here, using cryo-electron microscopy to study the structure of LRPPRC (leucine-rich pentatricopeptide repeat-containing protein) in complex with SLIRP (SRA stem-loop-interacting RNA-binding protein), mRNA and the mitoribosome, the authors show that LRPPRC facilitates mRNA handoff to the mitoribosome and regulates the expression of several mitochondrial genes.
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.
Cryo-EM studies reveal that RYBP–PRC1 uses two distinct interfaces for binding unmodified and H2Aub1-modified nucleosomes. These binding modes enable the complex to generate H2Aub1 chromatin domains by a read–write mechanism.
The biogenesis and recycling of the ‘heart’ of the human spliceosome, the U5 small nuclear ribonucleoprotein (snRNP), requires CD2BP2 and TSSC4. Here the authors present cryo-electron microscopy structures that reveal how these protein chaperones orchestrate the ATP-independent (re)generation of the U5 snRNP.
Using deep mutational scanning, the authors uncover the functional consequence of missense mutations in ARID1B, a subunit of the SWI/SNF chromatin remodeling complex that is frequently mutated in human Coffin–Siris syndrome and in cancer.
Structures of complete extracellular receptor assemblies mediated by the pro-inflammatory cytokines IL-12 and IL-23 reveal key commonalities and diverse features, with only IL-12 juxtaposing receptor domains proximal to the cell membrane.
