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Spliceosome biogenesis and recycling remains a largely unexplored area. Two papers now reveal how protein chaperones remodel the 20S U5 snRNP, leading to formation of the U4/U6.U5 tri-snRNP.
Chromatin condensation does not impede nucleosome sliding by ISWI remodelers. Notably, ATP energy is used not only for remodeling but also for enzyme mobility and to prevent solidification of chromatin. A ‘monkey-bar’ model rationalizes the findings.
In C. elegans, systemic RNAi is initiated by SID-1-mediated dsRNA internalization. Here the authors present cryo-EM structures of SID-1 homologs and the SID-1–dsRNA complex, elucidating the structural basis for dsRNA recognition and uptake by SID-1.
This study provides structural and biochemical insight into how mammalian PIWI proteins use a limited supply of piRNAs to silence a vast array of ever-evolving transposons in the germline.
The heterogeneity of CARM1 for the first cell fate bias in mice arises from exon-skipping splicing of Carm1 pre-mRNAs, which is regulated by the competition between LincGET-paraspeckles and splicing speckles for binding to the Carm1 locus.
The authors investigate how the transcription machinery selects the correct direction to produce coding transcripts. Their results propose a universal mechanism by which Integrator licenses bidirectional transcription to determine the direction of eukaryotic pre-mRNA transcription.
Liu et al. reveal that human TOPORS is a SUMO1-selective SUMO-targeted ubiquitin ligase (STUbL). The parallel action of TOPORS and the STUbL RNF4 defines a general mechanistic principle governing pathways driven by direct SUMO–ubiquitin crosstalk.
The first membrane protein structure was reported almost 40 years ago. In this issue, we are publishing a set of papers that serve to underline the incredible advances in our understanding of the biology of these multifaceted molecular machines.
In this Perspective, the author describes the recent progress in understanding solute carrier (SLC) biology and discusses the roles of new families of atypical SLCs.
Using cryo-electron microscopy and integrative modeling, the authors defined the structure of vimentin intermediate filaments, revealing a helical tube built of five protofibrils that enclose a fiber of low-complexity N-terminal domains.
Here the authors show that the nucleus undergoes a transient ‘metamorphosis’ within a nuclear–cytoplasmic DNA damage response linked to health and disease. Through this process, the nuclear envelope projects tubules that capture damaged DNA, mediating its repair.
Combining high-speed atomic force microscopy (AFM) with localization AFM and principal component analysis, the authors present six structures of a glutamate transporter and associate the conformational states to the molecule’s activity timeline.
The Gabija system constitutes one of the most prevalent anti-phage defense systems and is composed of GajA and GajB. Here, using cryo-EM and biochemistry, the authors show that GajA and GajB form a supramolecular complex with a stoichiometry of 4:4 to promote anti-phage defense.
The authors report that the γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation, selectively nucleates microtubules with 13-protofilaments and characterize the structural transformations associated with this function.
Using cryo-electron tomography, Dendooven et al. determined the structure of the native budding yeast γ-tubulin ring complex (γTuRC) capping spindle microtubules and showed that γTuRC adopts an active closed conformation to function as a perfect geometric template for microtubule nucleation.
Here, using cryo-EM, biochemistry and cell biology, the authors reveal the unique assembly, catalytic mechanism, multimodal substrate recruitment and regulation of the atypical ubiquitin ligase complex CUL9–RBX1.
Precise protease positioning and gating of the proteasome core require the ordered assembly of 28 subunits. Cryo-EM structures of seven intermediates visualize five dedicated chaperones and three propeptides mediating step-by-step assembly of the human 20S proteasome.
To prevent promiscuous protein degradation, proteasomes are initially assembled as inactive complexes. Their activation is autocatalytic and coupled to assembly. Here the authors uncover key aspects of the autocatalytic activation mechanism.