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Here the authors show that, when phosphorylated at Tyr34, THEMIS behaves as an allosteric activator to phosphatase SHP1, ensuring appropriate negative regulation of T cell antigen receptor signaling and thus assisting in T cell maturation and expansion.
Here, the authors use a massively parallel reporter assay RNA polymerase II massively systematic transcript end readout, to quantify factors that influence transcriptional start site selection in the genome of Saccharomyces cerevisiae to reveal patterns of dependence on DNA sequence, RNA polymerase II activity and nucleoside triphosphate abundance.
The NLRC4 inflammasome, vital for immune defense, responds to infections and inflammation. Here the authors reveal the role of Bacillusthailandensis type III secretion system needle protein in activating NLRC4 complex through structural insights.
By probing the epigenome in differentiating DNA methylation-free murine ESCs, the authors uncover a subset of germline and neural enhancers sensitive to DNA methylation. Failure to decommission these elements leads to biased adoption of these fates over other lineages.
How do intrinsically disordered proteins behave inside the cell? Moses et al. show that these flexible proteins contain structural preferences inside cells, and that these preferences can change with the composition of the intracellular environment.
Here, the authors demonstrate that CAND1 increases the dissociation rate of CRL2s, thus exerting an inhibitory effect, which in turn endows CRL2s with a selectivity for different targets based on their affinity for CRL2, thereby pacing protein degradation.
Here, using cryo-EM, in vitro and cellular assays, the authors elucidate how SS18–SSX1, via an unorthodox manner of selectively recognizing ubiquitylated nucleosomes, hijacks the BAF1 complex to Polycomb-repressed regions in synovial carcinoma.
Here, using cryo-EM, the authors delineate how the chromatin remodeling complex of ISWIa binds dinucleosomes. Their findings showcase synergistic interactions between ISWIa subumnits and neighboring nucleosomes, thus exemplifying the nucleosome spacing activity of ISWIa.
Using structural, biochemical, and functional assays, the authors demonstrate that the E3 ligase KLHDC2, via newly developed small-molecule ligands, can be co-opted to target critical targets for degradation.
Here the authors show that TET dioxygenases, the erasers of DNA methylation, use a self-limiting mechanism via their LCD domain to ensure adaptable methylome status and protect the genome from excessive oxidative methylation.
Here, using cryo-electron microscopy and functional assays in mouse oocytes and embryos, the authors delineate the composition of the subcortical maternal complex, showing that clinical variants associated with female reproductive diseases disrupt complex formation.
Here, using deep mutagenesis and cryo-EM, the authors unveil an autoinhibited conformation of a clamp loader from T4 bacteriophage, which is characterized by disassembled catalytic sites and blocked DNA binding.
Here, the authors show how Aurora kinase A (AURKA) employs Rab1a to direct ER remodeling. Activated Rab1A is retained on the ER and directly interacts with the RTN/REEP ER-shaping machinery to promote its oligomerization, eventually triggering an increase of ER complexity during mitosis.
Using cryo-electron microscopy the authors show that PtuA, an ATPase, and PtuB, a nuclease, assemble into a supramolecular complex with a stoichiometry of 6:2 for anti-phage defense in bacteria. Nucleoside triphosphates inhibit PtuAB activity while phage infection activates PtuAB to cleave phage genome for immune defense.
Here, the authors solve sequential structures of binding by the transcription activators NtcA and NtcB, showing that they cooperatively induce looping back of the promoter DNA towards RNA polymerase allowing transcription activation through a DNA looping mechanism.
Here the authors characterize the sequence-specific effect of an anticancer compound on mRNA cleavage, providing insights into the mechanism of mRNA 3′ processing.
Here, the authors show how binding of talin and kindlin to the β-integrin cytoplasmic tail increases talin and decreases kindlin affinity toward it, providing insights into mechanisms of integrin activation.
Using cryo-EM, Schmidt, Schulz, et al. solve the structure of the iron nitrogenase complex, which shows a unique architecture of alternative nitrogenases and suggests the G subunit to be involved in substrate channeling, stabilization of the cofactor and determining specificty among nitrogenase components.
The study presents a high-resolution structure of the retriever complex and a model of the retriever–CCC assembly, providing a mechanistic framework for studying how retriever facilitates endosomal recycling of diverse membrane proteins.