Transcriptional activation domains achieve rapid, dynamic, specific interaction with Mediator through binding of an unstructured peptide to multiple hydrophobic surfaces without particular amino acid side chain interactions.

Biochemical and structural analyses of a universal mRNP remodeling pathway suggest an ATPase-powered targeted deposition of export factors onto mRNP.

The N-terminal domain of the chromatin remodeler ISWI contains previously uncharacterized conserved motifs that maintain structure, prevent ATP hydrolysis unless nucleosomes are bound, and confer H4-tail sensitivity without directly competing with the H4 tail.

Analysis of conformational heterogeneity in cryo-EM data by a recently developed deep learning method reveals the structure and dynamics of the oncogenic chromatin remodeler ALC1 bound to a poly-ADP-ribosylated nucleosome.

A mechanistic basis is provided for the regulative ability of the mammalian embryo offering a long-sought explanation for coordinating cell behaviors at the population level ensuring robustness in developmental outcome.

A technology to produce homogenously poly-ADP-ribosylated proteins reveals key molecular mechanisms that govern ATP-dependent chromatin remodeling activity at DNA damage sites.

Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

Editors' Summary: This Replication Study has reproduced some parts of the original paper but other parts could not be interpreted.