Proceedings of the National Academy of Sciences (PNAS), a peer reviewed journal of the National Academy of Sciences (NAS) - an authoritative source of high-impact, original research that broadly spans...

LA JOLLA—The Salk Institute will welcome plant biologist Lucia Strader as a new professor and holder of the Howard H. and Maryam R. Newman Chair in Plant Biology in October 2025. Strader is an interna...

Designed protein pockets recognize intrinsically disordered protein regions

Nature Communications - Chromatin heterogeneity in the cell nucleus modulates the size, mobility, and formation of biomolecular condensates; decreasing chromatin heterogeneity correlates with...

More than 2,700 human mRNA 3′UTRs have hundreds of highly conserved (HC) nucleotides, but their biological roles are unclear. Here, we show that mRNAs with HC 3′UTRs mostly encode proteins with long intrinsically disordered regions (IDRs), including MYC, UTX, and JMJD3. These proteins are only fully active when translated from mRNA templates that include their 3′UTRs, raising the possibility of functional interactions between 3′UTRs and IDRs. Rather than affecting protein abundance or localization, we find that HC 3′UTRs control transcriptional or histone demethylase activity through co-translationally determined protein oligomerization states that are kinetically stable. 3′UTR-dependent changes in protein folding require mRNA-IDR interactions, suggesting that mRNAs act as IDR chaperones. These mRNAs are multivalent, a biophysical RNA feature that enables their translation in network-like condensates, which provide favorable folding environments for proteins with long IDRs. These data indicate that the coding sequence is insufficient for the biogenesis of biologically active conformations of IDR-containing proteins and that RNA can catalyze protein folding. ### Competing Interest Statement The authors have declared no competing interest. Pershing Square Foundation, https://ror.org/04tce9s05 G. Harold & Leila Y. Mathers Foundation National Institutes of Health, DP1GM123454, R35GM144046 Memorial Sloan Kettering Cancer Center, https://ror.org/02yrq0923, P30 CA008748

The REX element is associated with long-range enhancer–promoter interactions.

Scientists track how these membraneless biomolecular foci self-organize for their cellular tasks.

Nature Methods - CondenSeq is an imaging-based, high-throughput platform for characterizing condensate formation within the nuclear environment, uncovering the protein sequence features that...

A genetic mutation that fuses two genes drives several different cancer types by forming networks of protein interactions that alter gene expression in cells, a study by UT Southwestern Medical Center...

Condensates regulate transcription by selectively compartmentalizing biomolecules, yet the rules of specificity and their relationship to function rem…

Located in the Department of Ophthalmology, the Wert laboratory studies the post-mitotic neuronal cells of the retina, particularly the photoreceptor cells. Our goal is to discover and understand the ...

Lysosomal phospholipase PLA2G15 was identified as a physiological BMP hydrolase whose activity depends on unique esterification and stereochemistry of BMP and offers a potential therapeutic targe...