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Here the authors find that Polycomb repressive complex PRC1 functions independently of PRC2 to counteract Pol II binding, regulating transcription initiation and burst frequency.
CTCF is a conserved DNA- and RNA-binding protein with roles in genome folding and transcriptional regulation. Two recent studies investigated how CTCF knockout perturbs genome biology and derails embryogenesis in zebrafish and Drosophila melanogaster, revealing contrasting effects across species.
A series of cryo-EM structures examining transcription initiation by vaccinia poxvirus RNA polymerase reveal how viral transcription factors identify and melt a promoter and how a polymerase-associated helicase mediates promoter escape.
Outer-arm dyneins (OADs) assemble in large arrays on the ciliary axoneme to drive rhythmic beating. Cryo-EM structures of microtubule-bound Tetrahymena thermophila OAD arrays reveal details of this complex assembly and suggest a model for its mechanism of coordinated action.
High-resolution cryo-EM structures of human ATM bound to ATPγS and two distinct ATM inhibitors provide insights into the mechanism of inhibitor selectivity and offer a framework for structure-based drug design.
Emerging findings provide compelling evidence that the BRCA1-binding partner BARD1 contributes yet further to BRCA1 function. BARD1 is crucial for positioning the E2 ubiquitin-conjugating enzyme that confers specificity of its ligase to residues on histone H2A, and BARD1 also promotes DNA damage–induced chromatin recruitment through an interaction with ubiquitin-conjugated Lys13 or Lys15 of H2A on the nucleosome core particle.
Molnupiravir, a wide-spectrum antiviral that is currently in phase 2/3 clinical trials for the treatment of COVID-19, is proposed to inhibit viral replication by a mechanism known as ‘lethal mutagenesis’. Two recently published studies reveal the biochemical and structural bases of how molnupiravir disrupts the fidelity of SARS-CoV-2 genome replication and prevents viral propagation by fostering error accumulation in a process referred to as ‘error catastrophe’.
Two de novo designed protein classes that link phosphorylation by tyrosine and serine kinases to protein-protein association provide potential new avenues to regulating cell function.
Human islet amyloid polypeptide (hIAPP) is a protein commonly forming aggregates in islet cells of those afflicted by type II diabetes. New structures of fibrils seeded with patient-derived material reveal a diverse repertoire of structures, some of which may resemble those appearing in vivo.
Cryo-EM structures of human type 1 and type 2 bradykinin receptors (B1R and B2R) reveal the basis for discrimination between the endogenous peptides des-Arg10-kallidin and bradykinin and their activation mechanism.
The cryo-EM structure of human mitochondrial RNase P bound to precursor tRNA reveals the molecular basis for the first step of RNA processing in human mitochondria.
The frameshift stimulation element (FSE) of coronaviruses is an RNA structure that is required for balanced expression of viral proteins and is thus a promising drug target. A structure of the SARS-CoV-2 FSE serves as a guide for the development of antisense oligonucleotides that impair virus replication.
Cryo-EM structures and functional analyses of the SARS-CoV-2 B.1.1.7 variant spike protein reveal that the A570D mutation creates a molecular switch to regulate up-down conformations of the ACE2 receptor-binding domain through a pedal-bin-like mechanism.