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Wintermeyer and colleagues show that a nascent peptide within the E. coli ribosome can trigger alterations in SRP binding and membrane targeting in a purified system, which suggests that information about internal changes in the ribosomal exit tunnel can be conveyed externally via ribosomal protein L23. Cover image by Phil Early from istockphoto.com. pp 494-499
The splicing pathway is dominated by ATP-dependent RNA rearrangements promoted by DEAD-box helicases. Post-translational modifications have now been implicated in the regulation of two DEAD-box proteins that are required for catalytic activation of the spliceosome.
A heterotrimeric complex of minor pseudopilins from the type II secretion system has been identified and its crystal structure solved. Although each subunit shares the same overall α-β fold as other characterized (pseudo)pilins, GspK has a unique large α-helical domain inserted between two canonical β-strands. The structure constrains models for pseudopilus assembly.
Chromosomal breaks destabilize the genome and can cause developmental defects and diseases such as cancer. New work suggests that, shortly after DNA damage, dissociation of the histone binding protein HP1β from chromatin facilitates restoration of genome integrity.
Since the discovery that actin and actin-related proteins (ARPs) reside in the nucleus as integral subunits of chromatin-modifying and chromatin-remodeling complexes, efforts to uncover their roles in chromatin regulation have met with limited success. In a new study, the previously mysterious helicase-SANT–associated (HSA) domain found in many chromatin regulatory complexes is shown to act as a module that directs recruitment and contributes to the action of actin and ARPs in chromatin regulation.