Volume 23 Issue 7, July 2016

Contrary to conventional wisdom that molecular chaperones rely on hydrophobic interactions to bind a wide variety of client proteins in danger of misfolding, three recent studies reveal that the ATP-independent chaperone Spy exploits electrostatic interactions to bind its clients quickly, yet loosely enough to enable folding of the client while it is chaperone bound.

This Perspective discusses how two complementary approaches, bottom-up in vitro and top-down in situ structural biology, have now converged to generate the first predictive structural models of the nuclear pore scaffold.

The lncRNA lnc-β-Catm associates with β-catenin and the methyltransferase Ezh2, thereby promoting β-catenin methylation and stabilization, which in turn lead to activation of Wnt–β-catenin signaling and promote liver CSCs self-renewal.

A new 'metal mimic' mutagenesis approach that captures a T5 flap endonuclease complex with an intact DNA substrate provides structural evidence that the single-stranded 5′ flap generated by Okazaki-fragment synthesis threads through the flap endonuclease enzyme.

The E3 ubiquitin ligase activity of the BRCA1–BARD1 complex is required to reposition 53BP1 on damaged chromatin and to promote DNA resection and repair via homologous recombination, in a mechanism involving the chromatin remodeler SMARCAD1.

BoNT/A1 invades motoneurons by binding to the neuronal receptor SV2. A combination of structural, biophysical and cellular analyses reveal that BoNT/A1 binding and uptake require glycosylation of SV2.

The canonical transcription factor ERG promotes degradation of a subset of mRNAs linked to mitotic progression by recruiting the CCR4–NOT deadenylation complex, thus revealing a new regulatory interplay between mRNA synthesis and degradation.

The histone methyltransferase DOT1L and the chromatin reader BRD4 together facilitate transcription of genes critical to the molecular pathogenesis of MLL leukemia.

Proteomic and genomic analysis of Polycomb group complexes in embryonic stem cells and neural progenitor cells identifies new PRC1 and PRC2 interaction partners and targets during neural lineage commitment.

READ is a new crystallographic approach to visualize conformational ensembles of heterogeneous and dynamic molecules. READ is applied here to structurally characterize the various folding states of client Im7 bound to chaperone Spy.