"Grüne Wirtschaft" in Russland - Probleme und Perspektiven

Auch in Russland ist man sich der Notwendigkeit für radikale Veränderungen im weltweiten und russischen Entwicklungsmodell bewusst. Der Begriff "grüne Wirtschaft" ist für Russland neu, und er wird praktisch nicht verwendet. Dennoch korrespondieren die für die nächsten zehn bis zwanzig Jahre gesteckten Ziele des Landes in vielem mit denen eines Wechsels zu "grüner" Wirtschaft. Für die Durchsetzung nachhaltiger Entwicklungsziele müssen allerdings beträchtliche Anstrengungen unternommen werden. Diese wären mit radikalen Veränderungen in den umweltintensiven Rohstofftrends der Wirtschaft verbunden. Es wird immer deutlicher, dass sich das auf Rohstoffexporte basierende Modell, wie es sich in Russland herausgebildet hat, erschöpft hat. Eine neue Wirtschaft sollte den Akzent auf eine qualitative und nicht auf eine quantitative Entwicklung setzen. Das Land sollte nicht danach streben, die Menge der gewonnenen und genutzten natürlichen Ressourcen zu steigern und dadurch zusätzlich die Umwelt zu beeinträchtigen. Russland sollte vielmehr die Nutzung der sich bereits im Wirtschaftskreislauf befindenden Rohstoffen und Materialien effizienter gestaltet und deren Verluste vermeiden

Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro

RAD51 is a central protein of homologous recombination and DNA repair processes that maintains genome stability and ensures the accurate repair of double-stranded breaks (DSBs). In this work, we assessed amyloid properties of RAD51 in vitro and in the bacterial curli-dependent amyloid generator (C-DAG) system. Resistance to ionic detergents, staining with amyloid-specific dyes, polarized microscopy, transmission electron microscopy (TEM), X-ray diffraction and other methods were used to evaluate the properties and structure of RAD51 aggregates. The purified human RAD51 protein formed detergent-resistant aggregates in vitro that had an unbranched cross-β fibrillar structure, which is typical for amyloids, and were stained with amyloid-specific dyes. Congo-red-stained RAD51 aggregates demonstrated birefringence under polarized light. RAD51 fibrils produced sharp circular X-ray reflections at 4.7 Å and 10 Å, demonstrating that they had a cross-β structure. Cytoplasmic aggregates of RAD51 were observed in cell cultures overexpressing RAD51. We demonstrated that a key protein that maintains genome stability, RAD51, has amyloid properties in vitro and in the C-DAG system and discussed the possible biological relevance of this observation

Different amyloid aggregation of smooth muscles titin <i>in vitro</i>

<p>A comparative study of amyloid properties of the aggregates of smooth muscle titin (SMT) from chicken gizzard was carried out. These aggregates were formed in two solutions: 0.15 M glycine-KOH, pH 7.2–7.4 (SMT(Gly)) and 0.2 M KCl, 10 mM imidazole, pH 7.0 (SMT(KCl)). Electron microscopy data showed that SMT aggregates has an amorphous structure in both cases. The results of atomic-force microscopy demonstrated slight differences in morphology in two types of aggregates. The SMT(Gly) aggregates were represented as branching chains, composed of spherical aggregates approximately 300–500 nm in diameter and up to 35 nm in height. The SMT(KCl) aggregates formed sponge-like structures with strands of 8–10 nm in height. Structural analysis of SMT aggregates by X-ray diffraction revealed the presence of cross-β-sheet structure in the samples under study. In the presence of SMT(Gly) aggregates, thioflavine T fluorescence intensity was higher (~3-fold times) compared with that in the presence of SMT(KCl) aggregates. Congo red-stained SMT(Gly) aggregates had yellow to apple-green birefringence under polarized light, which was not observed for SMT(KCl) aggregates. Dynamic light scattering data showed the similar rate of aggregation for both types of aggregates, though SMT(KCl) aggregates were able to partially disaggregate under increased ionic strength of the solution. The ability of SMT to aggregation followed by disaggregation may be functionally significant in the cell.</p