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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.