Surprising epigenetic effect relies on snippets of RNA packaged within sperm

imageimageIn synucleinopathies such as Parkinson’s disease, the intrinsically disordered protein α-synuclein aggregates into amyloid fibrils. This study explores the effect of structural polymorphism ...

This structure of an archaeal tailed virus (arTV) provides detailed insights into arTV assembly and infection mechanisms.

The small heat shock proteins (sHsps) are a key class of molecular chaperones that can inhibit protein aggregation and enhance protein recovery from aggregates. However, the mechanisms sHsps employ to...

In two recent papers in Cell, Zhu et al. and Luo et al. use selective ribosome profiling to identify the substrates and timing of co-translational protein targeting to mitochondria. The results sugges...

The nuclear J-domain protein Apj1 controls the shut-off phase of the yeast heat shock response by displacing DNA-bound heat shock transcription factor Hsf1.

Nature Structural & Molecular Biology, Published online: 25 September 2025; doi:10.1038/s41594-025-01681-8This study reveals how human small ubiquitin-like modifier (SUMO) E1 recruits its E2 partner UBC9 and transfers SUMO1 through large structural changes, uncovering key mechanisms that ensure specificity and fidelity in SUMOylation, an essential protein modification pathway.

Ubiquitin is a conserved modifier regulating the stability and function of numerous target proteins. In all eukaryotes, polyubiquitin precursors are g…

imageimageIn Gram-positive bacteria the AAA+ protein ClpC and the peptidase ClpP form a central ATP-dependent protease crucial for stress resistance and virulence. Using structural biology and biochem...

Many important biological functions arise not from single genes, but from complex interactions encoded by entire genomes. Genome language models have emerged as a promising strategy for designing biol...

Synthetic trap-peptides facilitate the identification of complete holoenzymes that bind to the target sequence remarkably close to the phosphorylation site. PP4 bound to, but did not dephosphorylate,...

Yang et al. uncover the molecular details of how mitochondrial proteins cross the outer and inner mitochondrial membranes, with hydrophobicity guiding them into distinct pathways toward specific desti...

Mauthe et al. find that protein aggregate clearance requires fragmentation of the aggregate by a chaperone module and a proteasomal regulatory particle for recruitment and clustering of selective auto...

Author summary A delicate balance between peptidoglycan biosynthesis and hydrolysis is required to ensure proper cell division in the important pathogen Staphylococcus aureus. β-lactam antibiotics are...

Long-term study suggests that the more heatwaves people are exposed to, the more it accelerates body ageing.

Hypoxia, a condition characterized by insufficient oxygen supply, challenges cellular homeostasis and energy production, triggering adaptive respon...

Protein complexes are essential for cell function. Here, authors show that paired ribosomes can help each other’s nascent chains fold correctly, enabling proper dimer assembly and preventing misfoldin...

Targeted protein degradation is an emerging therapeutic strategy that leverages the cell’s natural protein clearance pathways to eliminate proteins of interest (POIs). One common approach involves bif...

Peroxisomes are single membrane-bound organelles containing numerous enzymes to perform metabolic functions. However, our view of peroxisomal protein import has remained incomplete. Two recent studies...

Chen et al. show that PEX39 cooperates with PEX7 in the peroxisomal import of proteins containing a PTS2 site and uncover an (R/K)PWE motif in PEX39 and PEX13 that binds to PEX7 and facilitates the im...

How multiple chaperones are organized to co-ordinate their activities has been unclear. We observed that the chaperone PDIA6 forms phase-separated condensates in the endoplasmic reticulum to which sev...

Leder et al. show that the chaperones PDIA6, Hsp70 BiP, ERdj3, PDIA1 and Hsp90 form co-condensates within the endoplasmic reticulum, enhancing folding and preventing misfolding of client proteins.