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In situ cryo-electron microscopy structures of five intermediate states of the RNA-dependent RNA polymerase of cytoplasmic polyhedrosis virus reveals how repeated cycles of double-stranded RNA genome transcription are regulated within viral particles.
Reconstitution experiments show that ER Hsp70 BiP can switch its activity from chaperone to ER stress sensor via interaction with UPR proteins IRE1 and PERK.
Paired-seq allows parallel analysis of transcriptome and accessible chromatin in millions of single cells and can be used to study dynamic and cell-type-specific gene regulatory programs in complex tissues, as demonstrated here for mouse adult cerebral cortex and fetal forebrain.
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.
Cryo-EM structures of mouse TRPV3 in open, closed and intermediate states, obtained by incubation of the protein samples at different temperatures immediately prior to freezing, offer insight into conformational changes induced by heat in TRPV3.
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.