Facial width-to-height ratio predicts self-reported dominance and aggression in males and females,but a measure of masculinity does not

Recently, associations between facial structure and aggressive behaviour have been reported. Specifically, the facial width-to-height ratio (fWHR) is thought to link to aggression, although it is unclear whether this association is related to a specific dimension of aggression, or to a more generalized concept of dominance behaviour. Similarly, an association has been proposed between facial masculinity and dominant and aggressive behaviour, but, to date, this has not been formally tested. Because masculinity and fWHR are negatively correlated, it is unlikely that both signal similar behaviours. Here, we thus tested these associations and show that: (i) fWHR is related to both self-reported dominance and aggression; (ii) physical aggression, verbal aggression and anger, but not hostility are associated with fWHR; (iii) there is no evidence for a sex difference in associations between fWHR and aggression; and (iv) the facial masculinity index does not predict dominance or aggression. Taken together, these results indicate that fWHR, but not a measure of facial masculinity, cues dominance and specific types of aggression in both sexes.     

P. aeruginosa SGNH Hydrolase-Like Proteins AlgJ and AlgX Have Similar Topology but Separate and Distinct Roles in Alginate Acetylation

The O-acetylation of polysaccharides is a common modification used by pathogenic organisms to protect against external forces. Pseudomonas aeruginosa secretes the anionic, O-acetylated exopolysaccharide alginate during chronic infection in the lungs of cystic fibrosis patients to form the major constituent of a protective biofilm matrix. Four proteins have been implicated in the O-acetylation of alginate, AlgIJF and AlgX. To probe the biological function of AlgJ, we determined its structure to 1.83 Å resolution. AlgJ is a SGNH hydrolase-like protein, which while structurally similar to the N-terminal domain of AlgX exhibits a distinctly different electrostatic surface potential. Consistent with other SGNH hydrolases, we identified a conserved catalytic triad composed of D190, H192 and S288 and demonstrated that AlgJ exhibits acetylesterase activity in vitro. Residues in the AlgJ signature motifs were found to form an extensive network of interactions that are critical for O-acetylation of alginate in vivo. Using two different electrospray ionization mass spectrometry (ESI-MS) assays we compared the abilities of AlgJ and AlgX to bind and acetylate alginate. Binding studies using defined length polymannuronic acid revealed that AlgJ exhibits either weak or no detectable polymer binding while AlgX binds polymannuronic acid specifically in a length-dependent manner. Additionally, AlgX was capable of utilizing the surrogate acetyl-donor 4-nitrophenyl acetate to catalyze the O-acetylation of polymannuronic acid. Our results, combined with previously published in vivo data, suggest that the annotated O-acetyltransferases AlgJ and AlgX have separate and distinct roles in O-acetylation. Our refined model for alginate acetylation places AlgX as the terminal acetlytransferase and provides a rationale for the variability in the number of proteins required for polysaccharide O-acetylation.     

Localisation of the gene coding for the haemopoietic stem cell antigen CD34 to chromosome 1q32

Summary Using in situ hybridisation, we have localised the CD34 gene to chromosome 1 in the region q32.