Monitoring and assessment of environmental resources in the changing landscape of Ethiopia: a focus on forests and water.

Monitoring and Assessment (M&A) of environmental resources aims to support the formulation of policies and follow up on outcomes of their implementation. In this study, the state of M&A is explored for Ethiopia with a focus on forests and water resources. The study is intended to serve as recommendations for future M&A applications in Ethiopia, as well as fulfillment of SDGs and other national and international commitments. Expert meetings, key informant interviews, and selected document analysis served as sources of information. The findings were summarized using qualitative grading and institutional mapping. Basic results of the study are that monitoring data on climate and streamflow are standardized in forms that can be communicated to policymakers. Scantier and less standardized are environmental data on soils, sediment transport, forests, biodiversity, and air quality. Water quality, soil moisture, groundwater level, forest biomass, and soil carbon are rarely monitored and can only be found in reports or studies for the fulfillment of academic degree requirements. Resources like nutrient fluxes have rarely been documented, not at all in some cases. There is considerable scope for tapping both technological advances and experiences of citizen science and local participation in environmental governance to rapidly expand and improve monitoring from local to regional and national scales. The study showed that there is a need for establishing a coordinated national system for monitoring and assessing the status of the environment, including the use of natural resources. Communicating such data to the scientific and wider public will support evidence-based planning and policy-making towards national development.

The activity and stability of a cold-active acylaminoacyl peptidase rely on its dimerization by domain swapping.

The study of enzymes from extremophiles arouses interest in Protein Science because of the amazing solutions these proteins adopt to cope with extreme conditions. Recently solved, the structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) pinpoints a mechanism of dimerization unusual for this class of enzymes. The quaternary structure of SpAAP relies on a domain-swapping mechanism involving the N-terminal A1 helix. The A1 helix is conserved among homologous mesophilic and psychrophilic proteins and its deletion causes the formation of a monomeric enzyme, which is inactive and prone to aggregate. Here, we investigate the dimerization mechanism of SpAAP through the analysis of chimeric heterodimers where a protomer lacking the A1 helix combines with a protomer carrying the inactivated catalytic site. Our results indicate that the two active sites are independent, and that a single A1 helix is sufficient to partially recover the quaternary structure and the activity of chimeric heterodimers. Since catalytically competent protomers are unstable and inactive unless they dimerize, SpAAP reveals as an "obligomer" for both structural and functional reasons.

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.

Life in cold environments requires an overall increase in the flexibility of macromolecular and supramolecular structures to allow biological processes to take place at low temperature. Conformational flexibility supports high catalytic rates of enzymes in the cold but in several cases is also a cause of instability. The three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) reported in this paper highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. In its functional form SpAAP is a dimer, and an increase in flexibility is achieved through loosening of intersubunit hydrophobic interactions. The release of subunits from the quaternary structure is hindered by an 'arm exchange' mechanism, in which a tiny structural element at the N terminus of one subunit inserts into the other subunit. Mutants lacking the 'arm' are monomeric, inactive and highly prone to aggregation. Another feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. DATABASE: Structural data are available in the Protein Data Bank under the accession number 5L8S.