Towards an\u2028 EU research and innovation policy agenda for nature-based solutions & re-naturing cities. Final report of the Horizon 2020 expert group on nature-based solutions and re-naturing cities.

1. Nature-based solutions harness the power and sophistication of nature to turn environmental, social and economic challenges into innovation opportunities. They can address a variety of societal challenges in sustainable ways, with the potential to contribute to green growth, 'future-proofing' society, fostering citizen well-being, providing business opportunities and positioning Europe as a leader in world markets. \u2028 2. Nature-based solutions are actions which are inspired by, supported by or copied from nature. They have tremendous potential to be energy and resource-efficient and resilient to change, but to be successful they must be adapted to local conditions. \u2028 3. Many nature-based solutions result in multiple co-benefits for health, the economy, society and the environment, and thus they can represent more efficient and cost-effective solutions than more traditional approaches. \u2028 4. An EU Research & Innovation (R&I) agenda on nature-based solutions will enable Europe to become a world leader both in R&I and in the growing market for nature-based solutions. For this, the evidence base for the effectiveness of nature-based solutions needs to be developed and then used to implement solutions. Both need to be done in conjunction with stakeholders. The potential for transferability and upscaling of solutions also requires further investigation. There is also a need to develop a systemic approach that combines technical, business, finance, governance, regulatory and social innovation. \u2028 5. Four principal goals have been identified that can be addressed by nature-based solutions: �� Enhancing sustainable urbanisation through nature-based solutions can stimulate economic growth as well as improving the environment, making cities more attractive, and enhancing human well-being. \u2028 �� Restoring degraded ecosystems using nature-based solutions can improve the resilience of ecosystems, enabling them to deliver vital ecosystem services and also to meet other societal challenges. \u2028 �� Developing climate change adaptation and mitigation using nature-based solutions can provide more resilient responses and enhance the storage of carbon. \u2028 �� Improving risk management and resilience using nature-based solutions can lead to greater benefits than conventional methods and offer synergies in reducing multiple risks. \u2028 6. Based on the four goals, seven nature-based solutions for R&I actions are recommended to be taken forward by the European Commission and Member States: �� Urban regeneration through nature-based solutions \u2028 �� Nature-based solutions for improving well-being in urban areas \u2028 �� Establishing nature-based solutions for coastal resilience \u2028 �� Multi-functional nature-based watershed management and ecosystem restoration \u2028 �� Nature-based solutions for increasing the sustainability of the use of matter and energy \u2028 �� Nature-based solutions for enhancing the insurance value of ecosystems \u2028 �� Increasing carbon sequestration through nature-based solutions \u2028This report was produced by the Horizon 2020 Expert Group on 'Nature-Based Solutions and Re- Naturing Cities', informed by the findings of an e-consultation and a stakeholder workshop. \u202

Structural Insights into the Nucleotide-Binding Domains of the P1B-type ATPases HMA6 and HMA8 from Arabidopsis thaliana

International audienceCopper is a crucial ion in cells, but needs to be closely controlled due to its toxic potential and ability to catalyse the formation of radicals. In chloroplasts, an important step for the proper functioning of the photosynthetic electron transfer chain is the delivery of copper to plastocyanin in the thylakoid lumen. The main route for copper transport to the thylakoid lumen is driven by two PIB-type ATPases, Heavy Metal ATPase 6 (HMA6) and HMA8, located in the inner membrane of the chloroplast envelope and in the thylakoid membrane, respectively. Here, the crystal structures of the nucleotide binding domain of HMA6 and HMA8 from Arabidopsis thaliana are reported at 1.5Å and 1.75Å resolution, respectively, providing the first structural information on plants Cu+-ATPases. The structures reveal a compact domain, with two short helices on both sides of a twisted beta-sheet. A double mutant, aiding in the crystallization, provides a new crystal contact, but also avoids an internal clash highlighting the benefits of construct modifications. Finally, the histidine in the HP motif of the isolated domains, unable to bind ATP, shows a side chain conformation distinct from nucleotide bound structures

HMA6 and HMA8 are two chloroplast Cu+-ATPases with different enzymatic properties.

The final version of record is available at http://www.bioscirep.org/content/35/3/e00201International audienceCopper (Cu) plays a key role in the photosynthetic process as cofactor of the plastocyanin (PC), an essential component of the chloroplast photosynthetic electron transfer chain. Encoded by the nuclear genome, PC is translocated in its apo-form into the chloroplast and the lumen of thylakoids where it is processed to its mature form and acquires Cu. In Arabidopsis, Cu delivery into the thylakoids involves two transporters of the PIB-1 ATPases family, heavy metal associated protein 6 (HMA6) located at the chloroplast envelope and HMA8 at the thylakoid membrane. To gain further insight into the way Cu is delivered to PC, we analysed the enzymatic properties of HMA8 and compared them with HMA6 ones using in vitro phosphorylation assays and phenotypic tests in yeast. These experiments reveal that HMA6 and HMA8 display different enzymatic properties: HMA8 has a higher apparent affinity for Cu+ but a slower dephosphorylation kinetics than HMA6. Modelling experiments suggest that these differences could be explained by the electrostatic properties of the Cu+ releasing cavities of the two transporters and/or by the different nature of their cognate Cu+ acceptors (metallochaperone/PC)