Volume 27 Issue 12, December 2020

Analysis of co-occurring chromatin interactions using multi-contact 3C and polymer simulations shows that, during interphase, entanglements between chromosomes and chromosomal domains are rare.

Primary cilia are isolated from monolayers of mammalian cells in culture for cryo-ET analyses, revealing new features as well as how they differ from motile cilia.

The effects of four antibodies on the aggregation pathway of Aβ are examined via an in-depth kinetics approach, revealing the specific molecular steps affected by each antibody.

Atomic force microscopy imaging of yeast condensin indicates that condensin may extrude DNA by switching conformation between open O and collapsed B shapes, indicative of a type of scrunching model.

A new X-ray crystal structure and supporting biochemical analyses of the human cardiac calsequestrin polymer reveal the basis of filament assembly and map disease-associated mutations to the multimerization interface.

Proteomic definition of the telomeric PARylome combined with genetic and histone H3.3 deposition assays at telomeres reveals that PAR-regulated HIRA activity compensates for loss of ATRX in ALT cells.

A directed genetic screen of chromatin regulators reveals that histone H3K4me2 deposition facilitates recovery of protein biosynthesis following UV-induced DNA damage repair and extends lifespan in C. elegans.

The solid-state NMR structure of an amyloid fiber formed by human hormone β-endorphin reveals a protonated Glu8 in the fibrillar core. Under neutral conditions, deprotonation of Glu8 would contribute to fibril disassembly and hormone peptide release.

Cryo-EM and liposome assays reveal that Atg9 functions as a lipid scramblase, transporting phospholipids between inner and outer liposome leaflets. Analyses of mutants in yeast support a role for this activity in autophagy.

Cryo-EM analyses together with liposome and cellular assays reveal that human ATG9A forms a trimer that mediates phospholipid flipping and promotes autophagosome membrane expansion.

A solid-state NMR structure of the transmembrane domain from SARS-CoV-2 envelope protein in the phospholipid environment reveals determinants of cation selectivity, a dehydrated pore and an N-terminal drug-binding site.