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Cell-based and in vitro analyses reveal that BRD4 functionally associates with eRNAs and that BRD4 bromodomains, through eRNA interactions, promote BRD4 binding at mutant p53-targeted enhancers to augment enhancer activation and tumor promoting gene expression.
A new system to analyze the instability of fragile X (CGG)n repeats in mammalian cells suggests that long repeats cause replication fork stalling, resulting in repeat length changes and mutation at a distance via break-induced replication.
The cryo-EM structure of human αvβ8 integrin in the extended-closed conformation shows the headpiece rotating about a flexible αv-knee, suggesting a ligand surveillance mechanism for integrins.
The mitochondrial fission dynamin (Dnm1) from an algae is captured in a closed conformation, with the GTPase domain compacted against the stalk. This work indicates that formation of the closed conformation may contribute to membrane fission.
Characterization of mRNA structure during the zebrafish maternal-to-zygotic transition identifies the ribosome as a major RNA structure remodeler in vivo and reveals that structural dynamics can affect gene expression, partly by modulating miRNA activity.
Cryo-EM structures of the RAG endonuclease in complex with intact DNA substrates reveal that DNA melting is the first step in V(D)J recombination, a mechanism potentially conserved in retroviral integration and DNA transposition.
A pair of SHIP box motifs identified within the Exo1 nuclease mediate interactions with Msh2 during DNA mismatch repair and define potential new Msh2-binding partners in yeast and human cells.
Cryo-EM analyses of human IP3 receptor in different ligand states (apo, with Ca2+ and/or IP3) reveal conformational changes in the cytoplasmic domain and how Ca2+ can regulate channel function.
Structural and functional dissection of the TIRR–53BP1 complex shows that TIRR acts as a regulatory switch that blocks 53BP1 binding to chromatin to direct DNA repair, and it releases 53BP1 in response to DNA damage by binding RNA.
Cryo-EM analyses of microtubules in different nucleotide-bound states reveal differences in lateral and longitudinal contacts within the lattice, indicating the structural basis for microtubule catastrophe.
Crystal structures of activated, phosphorylated fly parkin in complex with phosphorylated ubiquitin and human UbcH7 reveal large domain movements enabled by the parkin’s internal linkers. Results also explain some Parkinson’s disease mutations.
The crystal structure of human AT2R binding an angiotensin II analog reveals ‘core’ and ‘extended’ domains within the binding pocket. A signature positively charged motif orients the C terminus of the peptide ligand at the bottom of the binding pocket.
Neural network analyses of ribosome profiling data reveal sequence features that affect translation elongation, which can be manipulated to control protein expression levels in yeast.
Cryo-EM structure of the Salmonella Typhimurium FliP–FliQ–FliR complex identifies this export gate as a core component of the periplasmic portion of the type III secretion system.
Structures of Cdc48 with heterodimeric cofactor Ufd1–Npl4 reveal the location of Npl4's MPN domain above Cdc48’s central pore, thus suggesting how Npl4 engages with polyubiquitinated substrates and promotes their translocation into the ATPase.
Crystal structures of the CLCF proton-coupled fluoride antiporter Eca in two conformations capture two rotamers of the gating glutamate and reveal simultaneous accessibility of F– and H+ ions via separate pathways on opposite sides of the membrane.
The structural basis for self-assembly of human SYCP1, the core architectural element of the meiotic synaptonemal complex, reveals an obligate tetrameric structure that assembles into a zipper-like supramolecular lattice.
Cryo-EM analyses of mitochondrial complex I (NADH:ubiquinone oxidoreductase) isolated from mouse heart allow comparisons between the active and deactive states and provide new mechanistic insights into this important complex.
A cryo-EM structure of the human SLC1 transporter ASCT2 in the inward-facing conformation reveals the retrovirus-docking site and helps to elucidate the transport cycle. The transport domain is more solvent exposed than in most of the homolog structures.
The crystal structure of SLC38A9 from Danio rerio in complex with arginine in the cytosol-open conformation reveals the mechanism of substrate binding.