A combination of cryo-electron microscopy, structure prediction, and evolutionary analyses reveal several functional states of the dynamic protein translocation machinery at the mammalian endoplasmic reticulum.

The analysis of the first 1000 revertible protein trap alleles in zebrafish resulted in new functional genomic annotations and produced a panel of potential new models of human disease.

An atomic model of the 3744-residue Tra1 protein reveals multiple transcription activator binding sites, its integration within the SAGA chromatin coactivator complex, and a striking similarity to DNA-repair factor DNA-PKcs.

Cytosolic and organellar Hsp90s from higher eukaryotes have evolved a variable, and environmentally responsive N-terminal extension to regulate their activity.

A viral protein hijacks the key effector of transcriptional gene silencing, Su(var)3-9, to evade host plant surveillance.

The crystal structures of the intracellular part of the plexin receptor in the active dimer form, and its complex with a key downstream signalling protein Rap, provide insights into how plexin initiates a signalling cascade involved in axon guidance.

Structure of the dimeric Haemophilus influenzae TRAP transporter (SiaQM) reveals two Na⁺ sites, the substrate-binding site and lipid-binding sites, and weak but promiscuous binding of SiaP to SiaQM.

While the transcription factor c-Myc explores the space in the nucleus in an unrestricted manner, the elongation factor P-TEFb's sampling of the nucleus is constrained to a complex domain with fractal characteristics.

The core of histone acetyltransferase complex, NuA4, flexibly tethers various histone recognition modules, including the HAT module which is capable of binding nucleosomes marked by H3K4me3 and H3 acetylation.

Cryo-electron microscopy structures, combined with biochemical experiments, show how the E. coli F element-encoded TraR protein regulates transcription initiation by altering RNA polymerase conformation and conformational heterogeneity.