Volume 26 Issue 2, February 2019

Structural information on the respiratory supercomplex III₂IV₂ from budding yeast and from Mycobacterium smegmatis has become available, with cryo-EM work from four different groups.

A growing body of evidence suggests that cotranslational folding occurs from bacteria to mammalian cells, in particular for multi-domain proteins. In the assembly of yeast proteasomes, the initial interaction of Rpt1 and Rpt2 subunits has been found to take place on the translating ribosomes, coordinated by elongation pausing and involving the formation of Not1-containing compartments.

The Ninth International Conference on the Hsp90 Chaperone Machine concluded in October 2018, in Leysin, Switzerland. The program highlighted findings in various areas, including integrated insights into the molecular mechanism of Hsp90, cochaperones, and clients’ structure and function.

The noncoding RNA Xist regulates the accessibility of select chromatin regions on the inactive X chromosome (Xi) by directly inhibiting the chromosome remodeler BRG1 and by expelling it from the Xi.

Assembly of proteasome subunits Rpt1 and Rpt2 is shown to occur co-translationally. Ribosomal pausing facilitates the incorporation of nascent Rpt1 and Rpt2 into Not-containing particles and their subsequent association with each other.

Structures of human 5-HT_2AR in complex with several drugs reveal a side-extended cavity that is unique for this receptor, while molecular docking suggests that a highly 5-HT_2AR-selective antagonist binds residues within this cavity.

A combination of bulk and single-molecule fluorescence analysis reveals the choreography of binding and rearrangement of individual DNA-binding domains of RPA during homologous recombination.

Transcriptional attenuation in response to heat shock is regulated by enhanced recruitment of N-TEFs to gene promoters, which depends on stress-activated kinase p38α and nascent-protein ubiquitination.