Bioleaching to reprocess sulfidic polymetallic primary mining residues: Determination of metal leaching mechanisms

This is the final version. Available on open access from Elsevier via the DOI in this recordThe mining of non-ferrous metals produces the largest volume of metal-containing, extractive waste in Europe, and about 29% of all the waste produced in the EU-28. In the framework of the European project NEMO (Near-zero-waste recycling of low-grade sulfidic mining waste for critical-metal, mineral and construction raw-material production in a circular economy), new ways to valorize sulfidic tailings are being developed through the recovery of valuable metals and critical raw materials and the transformation of the residual in clean mineral fraction to be used for the mass production of cement, concrete and construction products. The first step of the NEMO concept consists of removing the sulfides remaining from primary bioleaching and extracting the metals in the residual material (known as ‘secondary ore’) using either enhanced bioleaching or an alkaline autoclave conversion processes. This paper focuses on one of the project case studies, the secondary ore, obtained from an operating heap leaching plant (Terrafame, Finland). This material still contains several sulfide minerals (pyrrhotite, pyrite, sphalerite, pentlandite, violarite, chalcopyrite) and significant amounts of metals (Zn, Ni, Cu, Co, rare earth elements). The study aimed to characterize the mineralogy of the secondary ore and perform bioleaching in 2 L-stirred tank reactors, with three microbial cultures growing at 42, 48 and 55 °C. These results were compared to abiotic experiments, performed under the same conditions. Nickel was released very quickly, suggesting that part of Ni dissolved in the primary heap was re-precipitated and remained in the secondary ore. By contrast, Cu dissolution was much slower but the kinetics were substantially improved when the temperature was increased to 55 °C. Cobalt dissolution kinetics were highly improved by the bacterial activity, whatever the consortium. This is consistent with the presence of Co in the pyrite in the secondary ore.European Union Horizon 202

Variability in energy cost of running at the end of a triathlon and a marathon

International audienceThe aim of this study was to investigate the increase in energy cost of running occurring at the end of a triathlon and a marathon event and to link them to the metabolic and hormonal changes, as well as to variations in stride length. Seven subjects took part in 3 experimental situations: a 2 h 15 min triathlon (30 min swimming, 60 min cycling and 45 min running), a 2 h 15 min marathon (MR) were the fast 45 min were run at the same speed as the triathlon run (TR), and a 45 min isolated run (IR) done at triathlon speed. The results show that energy cost during MR was higher than during TR (p < 0.01) (+ 8.9 %). Similar observations were made for pulmonary ventilation (+ 7.9 %) and heart rate (+ 6.3 %). Moreover, the values were significantly greater than the values obtained during the IR. TR and MR lead to greater weight loss (p < 0.01) (2.4±0.3 kg) than IR (1 ± 0.2 kg). The triathlon and the marathon produced a large decrease in plasma volume (respectively 19.6 ± 1.4 % and 12.9 ± 1.1 %) compared to IR (2 ± 0.4 %). Plasma renin activity was higher for the triathlon and the marathon than for the IR (p < 0.01). MR produces a significantly greater increase in plasma free fatty acids (F.F.A.) than TR (p < 0.05) and IR (p < 0.01). In addition, the F.F.A. at the end of TR were significantly higher than IR (p < 0.05). At the end of the trial the mean stride lengths for TR and IR were greater (+ 15 %) (p <0.01) than for MR. This study, carried out with subjects running overground, confirms the decrease in running efficiency previously shown at the end of a laboratory triathlon, and demonstrates that this decrease is lower than that occurring during a marathon

Mutants in the Mouse NuRD/Mi2 Component P66α Are Embryonic Lethal

The NuRD/Mi2 chromatin complex is involved in histone modifications and contains a large number of subunits, including the p66 protein. There are two mouse and human p66 paralogs, p66alpha and p66beta. The functions of these genes are not clear, in part because there are no mutants available, except in invertebrate model systems.We made loss of function mutants in the mouse p66alpha gene (mp66alpha, official name Gatad2a, MGI:2384585). We found that mp66alpha is essential for development, as mutant embryos die around day 10 of embryogenesis. The gene is not required for normal blastocyst development or for implantation. The phenotype of mutant embryos and the pattern of gene expression in mutants are consistent with a role of mp66alpha in gene silencing.mp66alpha is an essential gene, required for early mouse development. The lethal phenotype supports a role in execution of methylated DNA silencing

Solution structure and dynamic analysis of chicken MBD2 methyl binding domain bound to a target-methylated DNA sequence

The epigenetic code of DNA methylation is interpreted chiefly by methyl cytosine binding domain (MBD) proteins which in turn recruit multiprotein co-repressor complexes. We previously isolated one such complex, MBD2-NuRD, from primary erythroid cells and have shown it contributes to embryonic/fetal β-type globin gene silencing during development. This complex has been implicated in silencing tumor suppressor genes in a variety of human tumor cell types. Here we present structural details of chicken MBD2 bound to a methylated DNA sequence from the ρ-globin promoter to which it binds in vivo and mediates developmental transcriptional silencing in normal erythroid cells. While previous studies have failed to show sequence specificity for MBD2 outside of the symmetric mCpG, we find that this domain binds in a single orientation on the ρ-globin target DNA sequence. Further, we show that the orientation and affinity depends on guanine immediately following the mCpG dinucleotide. Dynamic analyses show that DNA binding stabilizes the central β-sheet, while the N- and C-terminal regions of the protein maintain mobility. Taken together, these data lead to a model in which DNA binding stabilizes the MBD2 structure and that binding orientation and affinity is influenced by the DNA sequence surrounding the central mCpG

Stress-Induced PARP Activation Mediates Recruitment of Drosophila Mi-2 to Promote Heat Shock Gene Expression

Eukaryotic cells respond to genomic and environmental stresses, such as DNA damage and heat shock (HS), with the synthesis of poly-[ADP-ribose] (PAR) at specific chromatin regions, such as DNA breaks or HS genes, by PAR polymerases (PARP). Little is known about the role of this modification during cellular stress responses. We show here that the nucleosome remodeler dMi-2 is recruited to active HS genes in a PARP–dependent manner. dMi-2 binds PAR suggesting that this physical interaction is important for recruitment. Indeed, a dMi-2 mutant unable to bind PAR does not localise to active HS loci in vivo. We have identified several dMi-2 regions which bind PAR independently in vitro, including the chromodomains and regions near the N-terminus containing motifs rich in K and R residues. Moreover, upon HS gene activation, dMi-2 associates with nascent HS gene transcripts, and its catalytic activity is required for efficient transcription and co-transcriptional RNA processing. RNA and PAR compete for dMi-2 binding in vitro, suggesting a two step process for dMi-2 association with active HS genes: initial recruitment to the locus via PAR interaction, followed by binding to nascent RNA transcripts. We suggest that stress-induced chromatin PARylation serves to rapidly attract factors that are required for an efficient and timely transcriptional response

SS18 Together with Animal-Specific Factors Defines Human BAF-Type SWI/SNF Complexes

Contains fulltext : 94049.pdf (publisher's version ) (Open Access

DNA methylation and methyl-CpG binding proteins: developmental requirements and function

DNA methylation is a major epigenetic modification in the genomes of higher eukaryotes. In vertebrates, DNA methylation occurs predominantly on the CpG dinucleotide, and approximately 60% to 90% of these dinucleotides are modified. Distinct DNA methylation patterns, which can vary between different tissues and developmental stages, exist on specific loci. Sites of DNA methylation are occupied by various proteins, including methyl-CpG binding domain (MBD) proteins which recruit the enzymatic machinery to establish silent chromatin. Mutations in the MBD family member MeCP2 are the cause of Rett syndrome, a severe neurodevelopmental disorder, whereas other MBDs are known to bind sites of hypermethylation in human cancer cell lines. Here, we review the advances in our understanding of the function of DNA methylation, DNA methyltransferases, and methyl-CpG binding proteins in vertebrate embryonic development. MBDs function in transcriptional repression and long-range interactions in chromatin and also appear to play a role in genomic stability, neural signaling, and transcriptional activation. DNA methylation makes an essential and versatile epigenetic contribution to genome integrity and function