Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.

During their final maturation in the cytoplasm, pre-60S ribosomal particles are converted to translation-competent large ribosomal subunits. Here, we present the mechanism of peptidyltransferase centre (PTC) completion that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3. Single-particle cryo-EM reveals that eL40 recruitment stabilises helix 89 to form the uL16 binding site. The loading of uL16 unhooks helix 38 from Nmd3 to adopt its mature conformation. In turn, partial retraction of the L1 stalk is coupled to a conformational switch in Nmd3 that allows the uL16 P-site loop to fully accommodate into the PTC where it competes with Nmd3 for an overlapping binding site (base A2971). Our data reveal how the central functional site of the ribosome is sculpted and suggest how the formation of translation-competent 60S subunits is disrupted in leukaemia-associated ribosomopathies.Bloodwise, MRC, Wellcome Trus

Child-display interaction: Exploring avatar-based touchless gestural interfaces

During the last decade, touchless gestural interfaces have been widely studied as one of the most promising interaction paradigms in the context of pervasive displays. In particular, avatars and silhouettes have been proved to be effective in communicating the touchless gestural interactivity supported by displays. In the paper, we take a child-display interaction perspective by exploring avatar-based touchless gestural interfaces. We believe that large displays offer an opportunity to stimulate child experience and engagement, for instance when learning about art, as well as bringing a number of challenges. The purpose of this study is twofold: 1) identifying the relevant aspects of children's interactions with a large display based on a touchless avatar-based interface, and 2) understanding the impact on recalling the content that arises from the interaction. We engaged 107 children over a period of five days during a public event at the university premises. Collected data were analyzed, and the outcomes transformed into three lessons learnt for informing the future design

Mechanism of completion of peptidyltransferase centre assembly in eukaryotes

During their final maturation in the cytoplasm, pre-60S ribosomal particles are converted to translation-competent large ribosomal subunits. Here, we present the mechanism of peptidyltransferase centre (PTC) completion that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3. Single-particle cryo-EM reveals that eL40 recruitment stabilises helix 89 to form the uL16 binding site. The loading of uL16 unhooks helix 38 from Nmd3 to adopt its mature conformation. In turn, partial retraction of the L1 stalk is coupled to a conformational switch in Nmd3 that allows the uL16 P-site loop to fully accommodate into the PTC where it competes with Nmd3 for an overlapping binding site (base A2971). Our data reveal how the central functional site of the ribosome is sculpted and suggest how the formation of translation-competent 60S subunits is disrupted in leukaemia-associated ribosomopathies