The overexpression of RNA chaperones, including several DEAD box RNA helicases, enhances the fitness of mutationally compromised E. coli strains.

Modeling and biophysics show that the unstructured acidic tail of the Sm protein Hfq mimics nucleic acid to auto inhibit its chaperone activity, preventing Hfq from being sequestered by inauthentic substrates and providing insight into the evolution of Hfq's chaperone function among bacterial genera.

RNA chaperone Hfq dynamically binds various pools of cellular RNAs to execute different regulatory functions.

Alteration of the G-quadruplex structure formed by GGGGCC repeat RNA through the direct interaction with RNA-binding proteins can suppress pathogenic repeat-associated non-AUG translation, leading to therapeutic effects on neurodegeneration in C9orf72-linked amyotrophic lateral sclerosis and frontotemporal dementia.

A novel co-translational mechanism continuously adjusts the expression levels of ribosomal proteins Rpl3 and Rpl4 to their consumption during ribosome synthesis by regulating the abundance of their mRNAs.

Host protein homeostasis is a critical force shaping influenza evolution, impacting both the nature of selection on the influenza genome and the accessibility of specific mutational trajectories.

A transcriptional coactivator turns into a repressor at specific genes in colorectal cancer cells.

Quantitative time-resolved crosslinking mass spectrometry is developed to monitor protein interactions and dynamics inside molecular condensates and used to identify misfolding of the RNA-binding domain of FUS as a key driver of condensate-aging.

A major cytoplasmic chaperone, Ssa2p, acts as a nuclear import carrier for tRNAs upon nutrient starvation in Saccharomyces cerevisiae.

Quantitative dissection of the roles of chaperone binding and phosphorylation in regulating heat shock factor 1 leads to a predictive model of the dynamics of the yeast heat shock response.