SummaryMulti-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double helices. SMC subunits comprise an ABC ATPase “head” and a “hinge” dimerization domain connected by a 49 nm coiled-coil “arm.” The heads undergo ATP-dependent engagement and disengagement to drive SMC action on the chromosome. Here, we elucidate the architecture of prokaryotic Smc dimers by high-throughput cysteine cross-linking and crystallography. Co-alignment of the Smc arms tightly closes the interarm space and misaligns the Smc head domains at the end of the rod by close apposition of their ABC signature motifs. Sandwiching of ATP molecules between Smc heads requires them to substantially tilt and translate relative to each other, thereby opening up the Smc arms. We show that this mechanochemical gating reaction regulates chromosome targeting and propose a mechanism for DNA translocation based on the merging of DNA loops upon closure of Smc arms.

During embryogenesis, differentiation of skeletal muscle is regulated by transcription factors that include members of the Msx homeoprotein family. By investigating Msx1 function in repression of myogenic gene expression, we identified a physical interaction between Msx1 and H1b, a specific isoform of mouse histone H1. We found that Msx1 and H1b bind to a key regulatory element of MyoD, a central regulator of skeletal muscle differentiation, where they induce repressed chromatin. Moreover, Msx1 and H1b cooperate to inhibit muscle differentiation in cell culture and in Xenopus animal caps. Our findings define a previously unknown function for "linker" histones in gene-specific transcriptional regulation.

SummarySMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive “hinge” dimerization domain with an ATP-regulated “head” dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB’s association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc’s dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome.

Narrow bandgap n-type molecular semiconductors are relevant as key materials components for the fabrication near-infrared organic solar cells (OSCs) and organic photodetectors (OPDs). We thus designed nearly isostructural nonfullerene electron acceptors, except for the choice of solubilizing units, which absorb from 600 to 1100 nm. Specific molecules include CTIC-4F, CO1-4F, and COTIC-4F, whose optical bandgaps are 1.3, 1.2, and 1.1 eV, respectively. Modulation of intramolecular charge transfer characteristics was achieved by replacing alkoxy groups with alkyl groups on thiophene spacers that connect an electron-rich cyclopentadithiophene core to peripheral electron-poor fragments. OSCs incorporating CTIC-4F and CO1-4F with PTB7-Th achieve power conversion efficiencies of over 10% with short-circuit current densities as high as ∼25 mA·cm–2. The same blends achieve OPD responsivities of 0.52 A·W–1 at ∼920 nm. These findings highlight outstanding opportunities to tune further molecular design so that OPDs may ultimately compete with their silicon counterparts.