Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The arginine methyltransferase PRMT5 modifies the splicing regulator SRSF1, which results in alternative splicing of multiple genes essential for the survival of acute myeloid leukemia cells.
The first structure of this unusual recombinase in complex with substrate DNAs reveals surprisingly unpaired and refolded transposon end DNAs that are positioned in part by direct interactions with a GTP cofactor.
Segmented, double-stranded RNA viruses of the Reoviridae family tightly regulate the activity of encapsidated polymerases to mediate the transition between genome replication and iterative rounds of multipartite transcription within a particle. By resolving multiple in situ structures of the transcribing complex, a new study reveals enzyme conformational changes and RNA trajectories during specific transcriptional states that support an ‘ouroboros’ model of conservative transcription for a member of the Reoviridae family.
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 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.
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.
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 analyses of α-synuclein fibrils formed with hereditary Parkinson’s disease mutant H50Q reveal features that help explain the mutant’s properties in vitro and in cells.
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.
CRISPR–Cas9-based method to introduce site-specific S-GlcNAcylation enables dissection of the roles of protein O-GlcNAcylation. S-GlcNAc, a hydrolytically stable structural mimic of O-GlcNAc, is recognized by a range of O-GlcNAc-binding proteins.