Volume 24 Issue 8, August 2017

Meiotic progression is controlled by cytoplasmic polyadenylation and translational activation of masked, maternal mRNAs. RNA-binding-protein interactions with adjacent cis elements cause local conformational changes to the mRNAs that determine the extent and timing of their activation.

The ribosome-associated complex (RAC) is formed by the JD protein Zuo1 and the unconventional Hsp70 Ssz1. This Review presents recent developments that have increased our understanding of RAC's mechanisms and cellular functions.

New analyses reveal that TERRA transcripts arising from the subtelomeric pseudoautosomal (PAR) region of sex chromosomes nucleate pairing of X alleles in mouse ES cells.

Asparagine endopeptidase (AEP) cleaves human α-synuclein at Asn103, yielding a fragment with higher aggregation propensity than that of the full-length protein. Truncated α-synuclein is also more neurotoxic and leads to dopaminergic neuronal loss and motor impairments in mice.

The structure of C3b in complex with factor I and a shortened version of factor H, along with functional analyses, leads to a mechanistic model for how regulators determine sequential cleavage events on C3b.

Single-molecule spectroscopy analyses of titin fragments from modern animals and reconstructed from the last common ancestors to mammals, sauropsids and tetrapods shed light on the evolution of the mechanical properties of muscle titin from the Paleozoic to our days.

Structural analysis of the uridyl transferases TUT4 and TUT7 reveals the use of two functional modules in the switch from monouridylation of pre-let-7, which promotes let-7 expression, to oligouridylation of pre-let-7, which marks it for degradation.

The crystal structure of Thermotoga maritima lysophosphatidic acid acyltransferase reveals a two-helix motif that positions the active site for catalysis within the membrane bilayer.

New data reveal how Musashi binding to Xenopus oocyte mRNAs promotes changes in RNA secondary structure that modulate CPEB1 binding and influence polyadenylation and translational efficiency.