RNA-binding proteins articles from across Nature Portfolio

Characterising interactions between proteins that are large and poorly soluble remains challenging. Here, the authors describe ReLo, a rapid and versatile eukaryotic cell culture-based method for detecting and studying direct interactions between structurally complex proteins.

Feng et al. developed a computational method PxR3D-map to jointly analyze crosslinked nucleotides and amino acids in protein-RNA complexes, which revealed key structural features underlying photocrosslinking of protein and RNA in cells.

The underlying mechanism for how heterotypic protein–RNA interactions modulate the liquid to amyloid transition of hnRNPA1A, a protein involved in amyotrophic lateral sclerosis, has so far remained elusive. Now characterization of hnRNPA1A condensate formation and aggregation in vitro reveals that the RNA/protein stoichiometry affects the molecular pathways leading to amyloid formation.

Inositol requiring enzyme 1 (IRE1) is a conserved protein kinase involved in the endoplasmic reticulum secretory pathway, however, IRE1 from S. cerevisiae and human show opposite responses to flavonoid quercetins. Here, the authors apply in silico and in vitro approaches to reveal the different binding modes of quercetins on IRE1, providing molecular insight into their opposite effects on S. cerevisiae and humans.

RoseTTAFoldNA extends the RoseTTAFold2 platform to predict the structures of protein–DNA and protein–RNA complexes.

Biomolecular condensates are recognized for their ability to compartmentalize the cytoplasm without bounding membranes, but the degree to which they organize the cytoplasm has not been clear. A new study reveals that condensates at a scale of 100 nm are responsible for the organization of at least 18% of the cytoplasmic proteome.

A new study in Science reports the mechanism through which TDP-43 enables correct processing of STMN2 mRNA, and proposes strategies to restore neuronal Stathmin-2 synthesis in TDP-43 proteinopathies.