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The development of a photocage-nanobody based technology enabled in-depth analysis of live cells from tissues while retaining their spatial information.
Graspetides are an important class of ribosomal natural products with potent bioactivities. New structural information provides insights into substrate recognition and catalysis, including a rare glimpse into the interactions between a tailoring enzyme and the core of the precursor peptide.
Structural and biochemical analysis of the plesiocin macrocyclase enzyme PsnB revealed that, unlike other ribosomal natural products, the core region of the precursor peptide enhances its interaction with the enzyme via conserved glutamate residues.
LYTACs induce selective degradation of extracellular proteins by recruiting them to cellular receptors that mediate delivery to the lysosome. Recent development of GalNAc-LYTACs and MoDE-As targeting the liver-specific ASGPR enables cell-type-restricted lysosomal protein degradation and reveals new LYTAC design principles.
Bifunctional ‘MoDE-A’ molecules, which contain ligands that bind to an extracellular protein and carbohydrate residues that recruit it to the asialoglycoprotein receptor, mediate cellular uptake and lysosomal turnover of target proteins.
Dan Tawfik suddenly left us on 4 May, 2021. His scientific intuition led him to articulate, and solve, many key questions related to protein chemistry and molecular evolution. Although science, particularly for his students, postdoctoral fellows and colleagues, is dimmer after his loss, his legacy will persist.
Structures of three cyanophycin synthetases reveal how the constituent glutathione synthetase and muramyl ligase-like domains cooperate to make cyanophycin, a poly-aspartate chain with arginine residues attached to the sidechains by isopeptide bonds.
Deploying two unrelated CRISPR nucleases in tandem, with multiplexed CRISPR RNAs and a chemically stabilized activator, creates a simple, one-step assay that can rapidly detect attomolar concentrations of RNA without needing target amplification.
The structure of a giant ubiquitin E3 ligase sheds light on its activation in a substrate-dependent manner and shows how a single E3 enzyme uses distinct recognition modules to confer substrate specificity.
Liquid–liquid phase separation, yielding membraneless organelles, allows for the sequestration and functional insulation of cellular proteins. A modularly built, synthetic membraneless organelle platform enables efficient control over endogenous cellular activities by knockdown of protein function or controlled protein release.
Controlled assembly of synthetic intracellular condensates from engineered disordered proteins enables control of cellular activities such as proliferation and division through recruitment, sequestration and insulation of endogenous client proteins.
The cystic fibrosis transmembrane conductance regulator anion channel can adopt an alternate conformation of its nucleotide-binding domain, which affects channel activity and, under certain conditions, leads to unfolding and protein degradation.
Approximately half of lipoproteins destined to the Escherichia coli outer membrane display intrinsically disordered linker peptides at their N termini, which are required for optimal trafficking by the Lol lipoprotein sorting system.
