The benefit of context for facial composite construction.

Purpose - The aim of this study was to investigate whether the presence of a whole-face context during facial composite production facilitates construction of facial composite images. Design/Methodology - In Experiment 1, constructors viewed a celebrity face and then developed a facial composite using PRO-fit in one of two conditions: either the full-face was visible while facial features were selected, or only the feature currently being selected was visible. The composites were named by different participants. We then replicated the study using a more forensically-valid procedure: In Experiment 2 non-football fans viewed an image of a premiership footballer and 24 hours later constructed a composite of the face with a trained software operator. The resulting composites were named by football fans. Findings - In both studies we found that presence of the facial context promoted more identifiable facial composite images. Research limitations/implications – Though this study uses current software in an unconventional way, this was necessary to avoid error arising from between-system differences. Practical implications - Results confirm that composite software should have the whole-face context visible to witnesses throughout construction. Though some software systems do this, there remain others that present features in isolation and these findings show that these systems are unlikely to be optimal. Originality/value - This is the first study to demonstrate the importance of a full-face context for the construction of facial composite images. Results are valuable to police forces and developers of composite software.

Phosphomimetic Mutation of the N-Terminal Lid of MDM2 Enhances the Polyubiquitination of p53 through Stimulation of E2-Ubiquitin Thioester Hydrolysis.

Mouse double minute 2 (MDM2) has a phosphorylation site within a lid motif at Ser17 whose phosphomimetic mutation to Asp17 stimulates MDM2-mediated polyubiquitination of p53. MDM2 lid deletion, but not Asp17 mutation, induced a blue shift in the λmax of intrinsic fluorescence derived from residues in the central domain including Trp235, Trp303, Trp323, and Trp329. This indicates that the Asp17 mutation does not alter the conformation of MDM2 surrounding the tryptophan residues. In addition, Phe235 mutation enhanced MDM2 binding to p53 but did not stimulate its ubiquitination function, thus uncoupling increases in p53 binding from its E3 ubiquitin ligase function. However, the Asp17mutation inMDM2 stimulated its discharge of the UBCH5a-ubiquitin thioester adduct (UBCH5a is a ubiquitin-conjugating enzyme E2D 1 UBC4/5 homolog yeast). This stimulation of ubiquitin discharge fromE2 was independent of the p53 substrate. There are now four known effects of the Asp17 mutation on MDM2: (i) it alters the conformation of the isolated N-terminus as defined by NMR; (ii) it induces increased thermostability of the isolated N-terminal domain; (iii) it stimulates the allosteric interaction ofMDM2 with the DNA-binding domain of p53; and (iv) it stimulates a novel protein–protein interaction with the E2-ubiquitin complex in the absence of substrate p53 that, in turn, increases hydrolysis of theE2-ubiquitin thioester bond. These data also suggest a new strategy to disrupt MDM2 function by targeting the E2-ubiquitin discharge reaction.