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A combination of structural and protein-chemistry approaches along with phylogenetic analyses provide insights into the specific activities of mouse tubulin tyrosine ligase-like enzymes as initiases or elongases of glutamylation.
A cryo-EM structure of mitochondrial complex I from Yarrowia lipolytica reveals structured waters involved in proton relays and energy transfer, with insights into the ‘deactive transition’ in mammalian systems.
A combination of cell-based and biochemical approaches reveals how oncogenic fusion protein SS18-SSX directs BAF complexes to H2AK119Ub-modified nucleosomes to remodel chromatin at cancer-specific gene targets.
Cryo-EM structures of HIV-1 capsid in tubular assemblies feature intrinsically curved and asymmetric hexamers and provide insight into cyclophilin A binding.
The SARS-CoV-2 spike glycoprotein is flexible, and its receptor-binding domain (RBD) fluctuates between open and closed conformations. Disulfide bonds are engineered into the spike ectodomain to lock the RBD in the closed state, leading to a construct with high thermostability.
EY6A, a neutralizing antibody isolated from a patient convalescing from COVID-19, binds the receptor binding domain of the SARS-CoV-2 spike glycoprotein with high affinity, at a location away from the binding site for the ACE2 receptor, similar to the one recognized by CR3022.
A crystal structure of bacterial multidrug transporter LmrP reveals the presence of a lipid inside the substrate binding cavity, with MD simulations and mutational analyses suggesting it could be involved in broad substrate specificity.
Massively parallel reporter assays from a synthetic mRNA library identify sequence features of 5′ UTRs that control mRNA translatability and reveal ribosome-dependent and ribosome-independent mRNA-surveillance pathways.
Crystallography and mutagenesis analyses examine how HIV-1 Nef interacts with AP2 to enable CD4 binding and downregulation and reveal the role of a Nef pocket that is also involved in downregulation of class I MHC.
The SARS-CoV-2 spike glycoprotein is flexible, and its receptor-binding domain (RBD) fluctuates between up or down conformations. Mutations engineered into the spike ectodomain either lock the RBD in the down state or make it adopt the up conformation more readily.
Live-cell single-molecule imaging reveals that the rate-limiting step in AGO2-mediated mRNA cleavage frequently involves unmasking of target sites by translating ribosomes.
Structural elucidation of the Kluyveromyces lactis telomeric Cdc13–Stn1–Ten1 complex unexpectedly reveals a distinct complex structure from that of RPA.
Two nanobodies that bind SARS-CoV-2 spike RBD are shown to block interaction with receptor ACE2 and thus neutralize the virus, and have an additive effect with antibody CR3022.
Disulfide-bond formation between a cysteine pair at the groove and C-terminal α-helix of the anti-apoptotic protein BFL-1 operates as a redox switch that controls the accessibility of the protein’s anti-apoptotic pocket, which is important for the regulation of pro-apoptotic BCL-2 family members.
Cryo-EM structures of the S. cerevisiae condensin holo complex reveal that ATP binding triggers exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains, potentially leading to an interconversion of DNA-binding sites in the catalytic core of condensin that might form the basis of its DNA translocation and loop-extrusion activities.
Cryo-EM and functional analyses of furin-cleaved spike from SARS-CoV-2 and the closely related spike from bat virus RaTG13 reveal differences in protein stability and binding to human receptor ACE2.
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.
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.