Place de la securisation dans les dispositifs juridique et institutionnel fonciers Beninois

La performance des instruments juridiques de gouvernance foncière demeure toujours problématique particulièrement dans les pays ouest-africains. Dans ce contexte, le présent article a analysé la place de la sécurisation foncière dans l’arsenal juridique béninois. L’analyse part du postulat que la définition de la sécurisation foncière doit prendre en compte simultanément quatre piliers dont : la propriété/transfert, l’usage ou l’utilisation, l’accessibilité et la conservation des terres. Ainsi, une analyse de contenu des différents instruments juridiques, institutions et acteurs de la gestion foncière au Bénin à travers leurs objectifs et missions a été effectuée. Il ressort que les réformes entreprises dans la gestion foncière ont faiblement pris en compte des aspects de conservation de la terre et de biodiversité. Le cadre juridique et institutionnel mis en oeuvre dans la gestion foncière ne garantit pas la conservation des terres et la biodiversité au Bénin. Cette recherche suggère la prise en compte du pilier conservation dans l’arsenal juridique qui régit le foncier pour une gouvernance responsable des régimes fonciers au Bénin. English title: the place of security in Benin’s legal and institutional arsenal on land tenure systems Abstract The performance of legal instruments for land governance remains problematic, particularly in West African countries. In this context, this article analyzes the place of land tenure security in the Benin legal arsenal. The analysis is based on the assumption that the definition of land tenure security must simultaneously take into account four main elements: ownership/transfer, use or utilization, accessibility and conservation of land. Thus, a content analysis of the different legal instruments (Livre Blanc, laws), institutions and land management agents in Benin was carried out through its objectives and missions. It emerged that the reforms undertaken in land management have shown gaps in terms of taking into account aspects of land conservation and biodiversity in the different laws developed, the missions and objectives of institutions and development projects oriented towards land management in Benin. Thus, the legal and institutional framework implemented in land management does not guarantee the conservation of land and biodiversity in Benin. This research suggests that the conservation aspect should be taken into account in the legal arsenal governing land tenure for responsible governance of land in Benin. Keywords: Land security, land conservation, legal reform, Benin

Submerged benthic macrophytes in Mediterranean lagoons: distribution patterns in relation to water chemistry and depth

International audienc

Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons

The reactive species of oxygen and chlorine damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to methionine sulfoxide, which can cause a loss of biological activity. To rescue proteins with methionine sulfoxide residues, living cells express methionine sulfoxide reductases (Msrs) in most subcellular compartments, including the cytosol, mitochondria and chloroplasts. Here we report the identification of an enzymatic system, MsrPQ, repairing proteins containing methionine sulfoxide in the bacterial cell envelope, a compartment particularly exposed to the reactive species of oxygen and chlorine generated by the host defence mechanisms. MsrP, a molybdo-enzyme, and MsrQ, a haem-binding membrane protein, are widely conserved throughout Gram-negative bacteria, including major human pathogens. MsrPQ synthesis is induced by hypochlorous acid, a powerful antimicrobial released by neutrophils. Consistently, MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA. For this activity, MsrPQ uses electrons from the respiratory chain, which represents a novel mechanism to import reducing equivalents into the bacterial cell envelope. A remarkable feature of MsrPQ is its capacity to reduce both rectus (R-) and sinister (S-) diastereoisomers of methionine sulfoxide, making this oxidoreductase complex functionally different from previously identified Msrs. The discovery that a large class of bacteria contain a single, non-stereospecific enzymatic complex fully protecting methionine residues from oxidation should prompt a search for similar systems in eukaryotic subcellular oxidizing compartments, including the endoplasmic reticulum