Sustainability through a gender lens: The extent to which research on UN Sustainable Development Goals includes sex and gender consideration.

Through efforts of the Gender Summits and UN Women, it is evident that all United Nations (UN) Sustainable Development Goals (SDGs) targets must be viewed from a gender perspective to ensure that the outcomes benefit women and men equally. Our research focuses on the extent to which sex and gender topics are explicitly covered in research related to the SDGs. Expanding on previous studies, we have developed an approach to detect and visualize the volume and proportion of research publications that include explicit mention of sex and gender terms. The approach visualizes the topical coverage of the publications in the corpus of each SDG as a term map, and overlays that view with the proportion of the publications associated with sex and gender topics. We show that attention to sex and gender topics is uneven across the SDGs, and that even where overlap between an SDG and consideration of sex and gender is high, significant topical areas of relevance to the SDG have little explicit connection with sex and gender. This study lays the groundwork for the evidence-based development of a roadmap toward greater integration of sex and gender across all SDGs as well as monitoring integration progress over time.

Phylogenomic and functional analysis of pterin-4a-carbinolamine dehydratase family (COG2154) proteins in plants and microorganisms.

Pterin-4a-carbinolamine dehydratases (PCDs) recycle oxidized pterin cofactors generated by aromatic amino acid hydroxylases (AAHs). PCDs are known biochemically only from animals and one bacterium, but PCD-like proteins (COG2154 in the Clusters of Orthologous Groups [COGs] database) are encoded by many plant and microbial genomes. Because these genomes often encode no AAH homologs, the annotation of their COG2154 proteins as PCDs is questionable. Moreover, some COG2154 proteins lack canonical residues that are catalytically important in mammalian PCDs. Diverse COG2154 proteins of plant, fungal, protistan, and prokaryotic origin were therefore tested for PCD activity by functional complementation in Escherichia coli, and the plant proteins were localized using green fluorescent protein fusions. Higher and lower plants proved to have two COG2154 proteins, a mitochondrial one with PCD activity and a noncanonical, plastidial one without. Phylogenetic analysis indicated that the latter is unique to plants and arose from the former early in the plant lineage. All 10 microbial COG2154 proteins tested had PCD activity; six of these came from genomes with no AAH, and six were noncanonical. The results suggested the motif [EDKH]-x(3)-H-[HN]-[PCS]-x(5,6)-[YWF]-x(9)-[HW]-x(8,15)-D as a signature for PCD activity. Organisms having a functional PCD but no AAH partner include angiosperms, yeast, and various prokaryotes. In these cases, PCD presumably has another function. An ancillary role in molybdopterin cofactor metabolism, hypothesized from phylogenomic evidence, was supported by demonstrating significantly lowered activities of two molybdoenzymes in Arabidopsis thaliana PCD knockout mutants. Besides this role, we propose that partnerless PCDs support the function of as yet unrecognized pterin-dependent enzymes.