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The crystal structure of the full five-subunit BAM complex from Escherichia coli reveals the interactions between individual components and domains and provides insights into the biogenesis of β-barrel outer-membrane proteins.
Mapping the spatial distribution of interaction sites between FG nucleoporins and nuclear transport receptors within the native NPC through SPEED microscopy reveals the 3D configuration of the FG-nucleoporin barrier and competition among transport receptors.
In addition to controlling Pol II pausing at promoters, the small nuclear RNA 7SK inhibits transcription at enhancers and super enhancers by recruiting the chromatin-remodeling complex BAF
Single-molecule FRET data reveal that CENP-A alters nucleosome structure by facilitating lateral passing of the two DNA gyres; this change is reversed by the nonhistone centromere protein CENP-C.
A 3.7- to 4.8-Å cryo-EM structure of the yeast CMG complex resolves two Mcm2–7 helicase conformations that may drive complex translocation and reveals an Mcm5-subunit domain inserted into the central channel, thus supporting a steric-exclusion model of DNA unwinding.
A combination of evolutionary covariance, biochemistry and SAXS analyses reveal that Escherichia coli FliG exists as a monomer in solution but forms domain-swapped polymers in assembled flagellar motors, thus leading to a thermodynamic model for self-assembly.
Complementary biochemical and genetic analyses reveal that SUMOylation of the six subunits of the MCM2–7 DNA helicase inhibits CMG formation, thereby negatively regulating DNA replication initiation in budding yeast.
Unraveling the molecular arms race between virus and host has been taken to a new level. A cryo-EM study reveals in unprecedented detail how the herpesvirus immune-evasion protein ICP47 inhibits the peptide transporter TAP.
This Perspective highlights recent progress on the location, functions and mechanisms of N6-methyladenosine (m6A), the most abundant internal modification in eukaryotic mRNA. In particular, the authors discuss how m6A modification affects the mammalian RNA life cycle at multiple stages.
In this Review, the authors discuss emerging mechanisms of how the replication machinery of mammalian cells overcomes replication-fork obstacles, thus ensuring faithful genome duplication.
‘Repeat swap’ modeling of the outward-facing conformation and biochemical analyses show that the bacterial VcINDY symporter uses an elevator-type mechanism for substrate transport across the cell membrane.
The higher abundance of U1 among snRNPs is explained by the identification of an additional mode of assembly: RBP U1-70K bridges pre-U1 to SMN–Gemin2–Sm, thus establishing a Gemin5-independent assembly pathway.
New crystal structures of the NapA antiporter in both outward- and inward-facing conformations provide evidence for an elevator-like ion-translocation mechanism in sodium/proton exchangers.
Cryo-EM structures of EF4 with the 70S ribosome, in conjunction with functional assays, reveal insights into the mechanism of EF4-mediated tRNA back-translocation.
Interaction of the RNase XRN2 with PAXT-1 and related XTB domain–containing proteins is important for XRN2 function in vivo and probably serves to increase XRN2 stability in the absence of substrate.
An evolutionarily conserved YxxΦ motif present in a subset of integrin α-chains directs selective endocytosis of integrin heterodimers via interaction with the clathrin adaptor AP2, which is important for cell motility.
During oxidative DNA demethylation, Neil DNA glycosylases stimulate processing of abasic sites generated by Tdg, which excises 5-methylcytosine oxidation products generated by Tet dioxygenases, promoting restoration of unmodified cytosines via base excision repair.