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Structural, biophysical and modeling approaches, combined with cell-based assays, reveal how the oncogenic transcription factor MYC interacts with subunits of the general transcription factor TFIID to modulate gene expression.
Cryo-EM resolution of the Drosophila P element transposase strand transfer complex visualizes a unique configuration of the transposon ends and the location of an essential GTP required for transposition of this historically important mobile element.
The arginine methyltransferase PRMT5 modifies the splicing regulator SRSF1 and affects acute myeloid leukemia cell survival by modulating SRSF1 function.
Cryo-EM maps of different clathrin cage architectures and accompanying analyses lead to a consensus model of the clathrin triskelion hub, suggesting a universal assembly mode that still allows adaptation to various vesicle sizes and shapes.
A unique arrangement of catalytic and regulatory subunits revealed by cryo-EM analysis of DNA polymerase δ holoenzyme in a template–primer complex suggests how interactions between the functional modules promote DNA synthesis and proofreading activities.
Analysis of X-chromosome upregulation using single-cell transcriptional kinetics data reveals increased burst frequency of X-linked genes that appear on the active X chromosome when X inactivation takes place.
The architecture of the Listeria monocytogenes ClpXP machine is revealed by cryo-EM analyses explaining how the symmetry mismatch between hexameric ClpX and heptameric ClpP rings is resolved for functional coordination.
The histone chaperone FACT interacts directly with cohesin and contributes to the functions of cohesin in nuclear organization during interphase and during mitotic chromosome folding in S. cerevisiae.
Mapping spliceosome engagement with pre-mRNAs using iCLIP reveals how the position and strength of branchpoints affect the crosslinking patterns of spliceosomal factors.
Time-resolved crystallography captures Escherichia coli rhomboid protease GlpG in different steps of catalysis, revealing how substrate reaches the active site and reaction intermediates.
Cryo-EM analyses of supercoiled polyhooks from Salmonella sp. reveal 11 protofilaments, each containing protomers in a different conformation, in which the domains behave as rigid bodies connected by two hinge regions.
Cryo-EM and biochemistry analyses show how E. coli SecA recognizes nascent polypeptides for cotranslational targeting, revealing the role of the ribosome in the process.
An antibody that recognizes the F glycoproteins from Nipah and Hendra viruses can neutralize both viruses and recognizes a quaternary epitope in the prefusion F trimer, preventing conformational changes required for fusion.
PRC2 preferentially binds G tracts within nascent pre-mRNAs, causing transfer of PRC2 from chromatin to RNA upon gene activation, thus providing a mechanism to selectively remove PRC2 from specific genes.
The dynamics of conformational changes of an RCK domain of the MthK channel, combined with existing atomic structures of those states, allows the development of a mechanistic model for the channel.
Cryo-EM structures of the multienzyme complex between the endoribonuclease Las1 and the polynucleotide kinase Grc3 reveal two molecular switches that coordinate nuclease and kinase function.
Lewis and Lu present an approach using a rhodamine tag and a polarization microscope to follow 10°–16° rotation of an ɑ-helix, corresponding to 3.4- to 8.1-Å translation, from the MthK RCK domain in real time.
The energetics of Ca2+-dependent conformational changes in an RCK domain from MthK are now determined from real-time monitoring, leading to a model that predicts the channel’s open probability behavior.
Cryo-EM structure of the dynein-2 complex (involved in intraflagellar transport, IFT) reveals distinct conformations of the two DHC2 tails within the same assembly, suggesting the mechanisms of autoinhibition and of transport on anterograde IFT trains.
Comprehensive genome-wide analyses of nucleosome occupancy and promoter activity after rapid depletion of chromatin remodelers in Saccharomyces cerevisiae provides insight into remodeler function in transcription initiation via nucleosome positioning.