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Structural elucidation and functional analyses of the CIA targeting complex (CTC) bound to DNA2 and primase illuminate the mechanism of cytoplasmic Fe–S cluster transfer to client proteins.
Computational analysis of Ribo-seq data with ORFquant allows annotation and quantification of translation at the level of single open reading frames and reveals the extent of gene-specific differences in protein production in diverse human cell lines.
Bivalent chromatin domains contain opposing histone modifications that assist cell lineage specification. Two studies report a role for Dppa2 and Dppa4 in the establishment of bivalency and the prevention of de novo DNA methylation at development-related genes in mouse embryonic stem cells.
The epigenetic priming factors DPPA2 and DPPA4 are required for efficient ESC differentiation because they maintain bivalency at developmental promoters and protect them from DNA methylation, thereby poising them for future lineage-specific activation.
A cryo-EM structure of mouse TRPV3 in nanodiscs reveal lipids bound to the pore domain, stabilizing the selectivity filter in the narrow state and the S6 in a π-helical conformation.
Cryo-EM structures of TRPV3 in nanodiscs reveal lipids bound to the channel and unprecedented conformations of the selectivity filter and of the pore-lining helix S6, underscoring the importance of lipids for the channel structure.
Coupling of a single-cell ratiometric DNA methylation reporter with an unbiased CRISPR screen in ESCs identifies key genes and regulatory pathways that drive global DNA hypomethylation and establishes Dppa2 and Dppa4 as essential safeguards of focal epigenetic states.
Cryo-EM elucidation of a fully reconstituted Pol II–DSF–PAF1–SPT6 elongation complex defines the position of PAF1 subunit RTF1 and reveals contacts with the Pol II bridge helix that may allosterically stimulate transcription elongation.
A cryo-EM structure of in vitro−formed fibrils of the human islet amyloid polypeptide (hIAPP) suggests both why the mutation S20G promotes aggregation and a potential basis for cross-seeding with β-amyloid, and leads to the design of peptide inhibitors.
Cryo-EM analyses of amyloid fibrils formed by synthetic human IAPP show an S-fold for the main polymorph, with the backbone superimposable with those of amyloid-β fibrils in antiparallel arrangement.
Small molecules that hijack the cellular protein ubiquitination machinery to selectively degrade proteins of interest have emerged as therapeutic modalities and powerful research tools. This Review summarizes recent developments in this field, with a focus on the use of degraders as research tools.
RBS-ID, a method to identify RNA–protein interactions by crosslinking, uses hydrofluoride to cleave RNA to simple mono-nucleoside adducts, which improves coverage and resolution of RNA binding site identification.
Lauberth and Sartorelli consider and discuss recent insights into the biogenesis and function of enhancer RNAs and the key roles they play in the regulation of gene expression.
A cryo-EM structure of amyloid fibrils formed in vitro with recombinant human PrP provides insights into fibril architecture and the potential role of disease mutations.
Insights from structural biology lead to the development of mini-Ins—a human des-octapeptide insulin analog that is monomeric and has receptor binding affinity and in vitro and in vivo activities comparable to those of human insulin.
Cryo-EM structures of a C. elegans cGMP-activated channel TAX-4 in lipid nanodiscs reveal a hydrophobic gate in the central cavity and, together with electrophysiology, provide mechanistic insights into the gating and regulation of CNG channels.