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HDL particles transport cholesterol and contain apolipoprotein A-I as their major protein. The solution structure of discoidal HDL particles reconstituted with a shortened apoA-I is now solved via a combination of NMR and EPR analyses.
The crystal structure of MurJ, a bacterial lipid II flippase involved in peptidoglycan biosynthesis and a member of the MOP transporter superfamily, reveals an inward-facing conformation and points to an alternating-access mechanism.
Genome-wide analyses of S. cerevisiae replisome mobility reveal overlapping roles of Pif1 and Rrm3 helicases in alleviating replication-fork arrest at tRNA genes.
Crystal structures of human APOBEC3A and a chimera of APOBEC3B and APOBEC3A bound to ssDNA reveal an unanticipated ‘U-shaped’ binding mode and provide insight into target selectivity.
The structure of GlyRα3 in complex with a selective potentiator that decreases neuropathic pain in an animal model identifies a novel allosteric regulatory mechanism.
The cryo-EM structure of human polycystin-2 (PC2) in a closed conformation reveals a domain located above the pore filter, forming an upper vestibule and making contacts with the pore and voltage-sensor-like domains.
Cryo-EM analysis captures three states of the human Rad51 recombinase and visualizes structures of presynaptic and postsynaptic filaments as well as a synaptic complex in the process of DNA-strand exchange.
The binding sites for the anticoagulant drug warfarin and for vitamin K on the human VKOR are determined through biochemistry and computational approaches. The results indicate a competitive mechanism of inhibition of VKOR by warfarin.
A newly developed assay in yeast reveals that large-scale expansions of trinucleotide repeats can occur in a single step, rather than through several small-scale events.
Mass spectrometry and biochemical analyses reveal that the major form of VKOR found in cells features a disulfide bond between Cys51 and Cys132, and this intermediate is the target of the anticoagulant drug warfarin.
New data reveal that telomere length is maintained in human pluripotent stem cells through the opposing activities of telomerase-meditated elongation and telomere trimming mechanisms promoted by HR factors.
The enzyme FICD was previously known to AMPylate the ER-resident chaperone BiP, inactivating the chaperone. Mammalian FICD is now shown to catalyze the removal of the AMP group from BiP.
Genetic and biochemical assays reveal that carbon monoxide produced by heme catabolism influences circadian rhythm in mammals by altering the activity of transcription factor CLOCK–BMAL1 at clock-gene targets.
Large-scale sequencing approaches reveal that the genetic code of Euplotes ciliates supports widespread ribosomal frameshifting at stop codons, and that additional mechanisms are required for efficient translation termination.
Barcoded HIV ensembles (B-HIVE) provides a new approach to map HIV integration sites and to determine how genomic context influences proviral transcription activity and response to latency-reversing agents.
spFRET microscopy analysis reveals how FACT reversibly uncoils DNA from nucleosomes during remodeling, thus modulating DNA accessibility in vitro and in vivo.
Opposing effects of 8-oxodGTP on telomerase activity – promoting elongation by destabilizing G4 structures or inhibiting elongation by acting as a chain terminator – explain the differential sensitivity of cells with short telomeres to oxidative stress.
The ribosome-assembly factor Mrt4 prevents untimely recruitment of the RNA-export receptor Mex67–Mtr2 to the nascent 60S ribosomal subunit, thereby ensuring appropriately timed nuclear export.
Cryo-EM analyses of yeast TRiC (CCT) reveal conformational changes induced by ATP binding and a staggered mode of nucleotide binding to the different subunits.
The RNA-binding protein CPEB1 drives post-transcriptional changes in the host transcriptome and poly(A)-tail lengthening of viral RNAs, processes essential for productive HCMV infection.