Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Rea1 is an ATPase related to dynein motor proteins that has been implicated in the biogenesis of the 60S ribosomal subunit. A new cryo-EM study vividly demonstrates the power of structural methods, deciphering the role of Rea1 in monitoring key pre-60S maturation steps before the acquisition of export competence in budding yeast.
Release of neurotransmitters occurs by opening of a fusion pore in a manner thought to be mediated by SNARE proteins, but whether the fusion pore is a lipidic or a proteinaceous structure is controversial. A new study using very small nanodiscs shows that it is both.
A comprehensive review of the discovery and molecular dissection of the eukaryotic ribosome-associated quality-control pathway for degradation of nascent proteins arising from interrupted translation.
A new crystal structure of mouse Unkempt, a translational regulator of neuronal cell morphology, reveals how its two zinc-finger-triplet clusters recognize distinct cognate RNA sites.
The identification of N6-methyldeoxyadenosine in the DNA of Xenopus laevis, mice and humans extends the presence of this mark to vertebrates, thus fostering the potential importance of this mark as a carrier of epigenetic information.
Single-molecule FRET provides insight into the structural dynamics of the KirBac1.1 potassium channel and reveals that channel gating is controlled by the tightness of the slide-helix ‘belt’.
The cryo-EM structure of a nucleoplasmic pre-60S particle with the Rix1–Rea1 checkpoint machinery reveals insights into pre-60S maturation before nuclear export.
Structural and biochemistry analyses reveal that the monomeric RING domains of E3 ligases Arkadia and Ark2C bind free ubiquitin with high affinity, and the RING–Ub complex stabilizes donor ubiquitin conjugated to E2, thus promoting transfer.
Spy is an ATP-independent chaperone that resides in the Escherichia coli periplasm and promotes the folding of its client Im7. Kinetic analyses now reveal that Im7 folds into its native state while it is bound to Spy.
Biochemical analyses, auxin-induced degradation experiments and EM imaging provide a map of the subunit connectivity of the yeast exocyst and show that the exocyst exists predominantly as a stable octameric complex.
A nanodisc-based approach reveals that the fusion pores formed during neurotransmitter exocytosis are hybrid structures composed of both membrane lipids and SNARE proteins.
New cryo electron microscopy structures of bluetongue virus (BTV) under low- and high-pH conditions reveal pH sensors that mediate host-membrane fusion and penetration by a nonenveloped virus.
Crystal structures of HIV-1 Env V1V2 in complex with human broadly neutralizing antibodies and ontogeny analyses allow the engineering of Env trimers that are recognized by ancestor and intermediate antibody forms.