RESUMEN
From the beginning of March 2020 and for the following two and half months, many European countries comprising Italy have been forced into an unprecedented lockdown, allowing only the opening of essential economic activities needed to address the problems created by the pandemic (e.g. sanitary, food provision). Like many sectors of the Italian economy, aquaculture has also slowed down due to the ongoing emergency and the consequent closure of business. In our study we provided a 'snapshot' of the socio-economic effects of the lockdown on the aquaculture sector in Italy, immediately following the adoption of the COVID-19 restrictions as they were perceived by the workers. Although it was surveyed for a short-time period, differences in perception have been detected both in relation to the type of aquaculture as well as to the geographic locations where farms were placed, partially reflecting the economic gaps already existing within the northern and the southern part of the country before the lockdown.
RESUMEN
AIM: The aim of this study was to evaluate the moderating effect of peroxisome proliferator activated receptor-γ (PPAR-γ) gene variants on the association of serum C-reactive protein level (CRP) and ischemic stroke (IS). MATERIAL AND METHODS: A total of 114 patients with IS and 135 healthy controls were included. RESULTS: After adjustment for age, sex, total cholesterol, LDL and HDL cholesterol, triglycerides, hypertension, smoking, body mass index and previous therapy with antihypertensive and/or statins, PPAR-γ had statistically significant moderating effect on association of serum CRP level and IS in patients younger than 60. In participants with PPAR CG or GG genotype level of CRP and IS were not statistically significantly associated (ORâ¯=â¯1.00; 95% CI 0.90-1.10; pâ¯=â¯0.933), but in participants with PPAR CC genotype, the association of serum CRP level and IS was significant (ORâ¯=â¯1.67; 95% CI 1.21-2.31; pâ¯=â¯0.002). CONCLUSION: In patients with PPAR CC genotype the association of serum CRP level and IS was significant.
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Proteína C-Reactiva/análisis , Accidente Cerebrovascular Isquémico/genética , PPAR gamma/genética , Estudios de Casos y Controles , Femenino , Genotipo , Humanos , Accidente Cerebrovascular Isquémico/sangre , Masculino , Persona de Mediana EdadRESUMEN
The COVID-19 global pandemic has had severe, unpredictable and synchronous impacts on all levels of perishable food supply chains (PFSC), across multiple sectors and spatial scales. Aquaculture plays a vital and rapidly expanding role in food security, in some cases overtaking wild caught fisheries in the production of high-quality animal protein in this PFSC. We performed a rapid global assessment to evaluate the effects of the COVID-19 pandemic and related emerging control measures on the aquaculture supply chain. Socio-economic effects of the pandemic were analysed by surveying the perceptions of stakeholders, who were asked to describe potential supply-side disruption, vulnerabilities and resilience patterns along the production pipeline with four main supply chain components: a) hatchery, b) production/processing, c) distribution/logistics and d) market. We also assessed different farming strategies, comparing land- vs. sea-based systems; extensive vs. intensive methods; and with and without integrated multi-trophic aquaculture, IMTA. In addition to evaluating levels and sources of economic distress, interviewees were asked to identify mitigation solutions adopted at local / internal (i.e., farm-site) scales, and to express their preference on national / external scale mitigation measures among a set of a priori options. Survey responses identified the potential causes of disruption, ripple effects, sources of food insecurity, and socio-economic conflicts. They also pointed to various levels of mitigation strategies. The collated evidence represents a first baseline useful to address future disaster-driven responses, to reinforce the resilience of the sector and to facilitate the design reconstruction plans and mitigation measures, such as financial aid strategies.
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Acetyl-coenzyme A (CoA) synthetase (Acs) is an enzyme central to metabolism in prokaryotes and eukaryotes. Acs synthesizes acetyl CoA from acetate, adenosine triphosphate, and CoA through an acetyl-adenosine monophosphate (AMP) intermediate. Immunoblotting and mass spectrometry analysis showed that Salmonella enterica Acs enzyme activity is posttranslationally regulated by acetylation of lysine-609. Acetylation blocks synthesis of the adenylate intermediate but does not affect the thioester-forming activity of the enzyme. Activation of the acetylated enzyme requires the nicotinamide adenine dinucleotide-dependent protein deacetylase activity of the CobB Sir2 protein from S. enterica. We propose that acetylation modulates the activity of all the AMP-forming family of enzymes, including nonribosomal peptide synthetases, luciferase, and aryl- and acyl-CoA synthetases. These findings extend our knowledge of the roles of Sir2 proteins in gene silencing, chromosome stability, and cell aging and imply that lysine acetylation is a common regulatory mechanism in eukaryotes and prokaryotes.
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Acetato CoA Ligasa/metabolismo , Proteínas Bacterianas/metabolismo , Lisina/metabolismo , Salmonella enterica/enzimología , Sirtuinas/metabolismo , Acetato CoA Ligasa/química , Acetato CoA Ligasa/genética , Acetilación , Acilcoenzima A/metabolismo , Adenosina Monofosfato/metabolismo , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Sitios de Unión , Coenzima A/metabolismo , Secuencia Conservada , Activación Enzimática , Regulación Bacteriana de la Expresión Génica , Immunoblotting , Espectrometría de Masas , NAD/metabolismo , Mapeo Peptídico , Salmonella enterica/genética , Espectrometría de Masa por Láser de Matriz Asistida de Ionización DesorciónRESUMEN
The Sir2 enzyme family is responsible for a newly classified chemical reaction, NAD(+)-dependent protein deacetylation. New peptide substrates, the reaction mechanism, and the products of the acetyl transfer to NAD(+) are described for SIR2. The final products of SIR2 reactions are the deacetylated peptide and the 2' and 3' regioisomers of O-acetyl ADP ribose (AADPR), formed through an alpha-1'-acetyl ADP ribose intermediate and intramolecular transesterification reactions (2' --> 3'). The regioisomers, their anomeric forms, the interconversion rates, and the reaction equilibria were characterized by NMR, HPLC, 18O exchange, and MS methods. The mechanism of acetyl transfer to NAD(+) includes (1) ADP ribosylation of the peptide acyl oxygen to form a high-energy O-alkyl amidate intermediate, (2) attack of the 2'-OH group on the amidate to form a 1',2'-acyloxonium species, (3) hydrolysis to 2'-AADPR by the attack of water on the carbonyl carbon, and (4) an SIR2-independent transesterification equilibrating the 2'- and 3'-AADPRs. This mechanism is unprecedented in ADP-ribosyl transferase enzymology. The 2'- and 3'-AADPR products are candidate molecules for SIR2-initiated signaling pathways.
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Adenosina Difosfato Ribosa/análogos & derivados , Adenosina Difosfato Ribosa/síntesis química , Silenciador del Gen , Histona Desacetilasas/química , NAD/química , Proteínas Reguladoras de Información Silente de Saccharomyces cerevisiae , Transactivadores/química , Adenosina Difosfato Ribosa/química , Adenosina Difosfato Ribosa/metabolismo , Secuencia de Aminoácidos , Arabinosa/química , Proteínas Arqueales/química , Proteínas Arqueales/genética , Proteínas Bacterianas/química , Proteínas Bacterianas/genética , Óxido de Deuterio/metabolismo , Inhibidores Enzimáticos/química , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Inhibidores de Histona Desacetilasas , Histona Desacetilasas/genética , Histona Desacetilasas/metabolismo , Humanos , Isomerismo , Cinética , Datos de Secuencia Molecular , NAD/metabolismo , Resonancia Magnética Nuclear Biomolecular , O-Acetil-ADP-Ribosa , Isótopos de Oxígeno/metabolismo , Sirtuina 1 , Sirtuina 2 , Sirtuinas , Especificidad por Sustrato , Transactivadores/antagonistas & inhibidores , Transactivadores/genética , Transactivadores/metabolismoRESUMEN
The yeast Sir2 protein, required for transcriptional silencing, has an NAD(+)-dependent histone deacetylase (HDA) activity. Yeast extracts contain a NAD(+)-dependent HDA activity that is eliminated in a yeast strain from which SIR2 and its four homologs have been deleted. This HDA activity is also displayed by purified yeast Sir2p and homologous Archaeal, eubacterial, and human proteins, and depends completely on NAD(+) in all species tested. The yeast NPT1 gene, encoding an important NAD(+) synthesis enzyme, is required for rDNA and telomeric silencing and contributes to silencing of the HM loci. Null mutants in this gene have significantly reduced intracellular NAD(+) concentrations and have phenotypes similar to sir2 null mutants. Surprisingly, yeast from which all five SIR2 homologs have been deleted have relatively normal bulk histone acetylation levels. The evolutionary conservation of this regulated activity suggests that the Sir2 protein family represents a set of effector proteins in an evolutionarily conserved signal transduction pathway that monitors cellular energy and redox states.
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Proteínas Fúngicas/fisiología , Histona Desacetilasas/fisiología , NAD/fisiología , Proteínas Reguladoras de Información Silente de Saccharomyces cerevisiae , Transactivadores/fisiología , ADN Ribosómico/genética , Histonas/metabolismo , Filogenia , Poli(ADP-Ribosa) Polimerasas/fisiología , Recombinación Genética , Saccharomyces cerevisiae/enzimología , Sirtuina 1 , Sirtuina 2 , SirtuinasRESUMEN
With the exception of the methanogenic archaea Methanococcus jannaschii and Methanobacterium thermoautotrophicum deltaH, all organisms surveyed contain orthologs of Escherichia coli cysteinyl-tRNA synthetase (CysRS). The characterization of CysRS-encoding (cysS) genes and the demonstration of their ability to complement an E. coli cysSts mutant reveal that Methanococcus maripaludis and Methanosarcina barkeri, two other methanogenic archaea, possess canonical CysRS proteins. A molecular phylogeny inferred from 40 CysRS sequences indicates that the CysRS of M. maripaludis and Methanosarcina spp. are specific relatives of the CysRS of Pyrococcus spp. and Chlamydia, respectively. This result suggests that the CysRS gene was acquired by lateral gene transfer in at least one euryarchaeotic lineage.
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Escherichia coli/genética , Aminoacil-ARN de Transferencia/fisiología , Secuencia de Aminoácidos , Animales , Clonación Molecular , Evolución Molecular , Genes Arqueales , Genes Bacterianos , Prueba de Complementación Genética , Methanococcus/genética , Methanosarcina barkeri/genética , Datos de Secuencia Molecular , Mutagénesis , Filogenia , Aminoacil-ARN de Transferencia/genética , Homología de Secuencia de AminoácidoRESUMEN
The genomic sequences of Methanococcus jannaschii and Methanobacterium thermoautotrophicum contain a structurally uncommon seryl-tRNA synthetase (SerRS) sequence and lack an open reading frame (ORF) for the canonical cysteinyl-tRNA synthetase (CysRS). Therefore, it is not clear if Cys-tRNACys is formed by direct aminoacylation or by a transformation of serine misacylated to tRNACys. To address this question, we prepared SerRS from two methanogenic archaea and measured the enzymatic properties of these proteins. SerRS was purified from M. thermoautotrophicum; its N-terminal peptide sequence matched the sequence deduced from the relevant ORF in the genomic data of M. thermoautotrophicum and M. jannaschii. In addition, SerRS was expressed from a cloned Methanococcus maripaludis serS gene. The two enzymes charged serine to their homologous tRNAs and also accepted Escherichia coli tRNA as substrate for aminoacylation. Gel shift experiments showed that M. thermoautotrophicum SerRS did not mischarge tRNACys with serine. This indicates that Cys-tRNACys is formed by direct acylation in these organisms.
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Methanobacterium/enzimología , Methanococcus/enzimología , Serina-ARNt Ligasa/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Clonación Molecular , ADN de Archaea , Expresión Génica , Humanos , Methanobacterium/genética , Methanococcus/genética , Datos de Secuencia Molecular , ARN de Archaea/metabolismo , ARN de Transferencia/metabolismo , Homología de Secuencia de Aminoácido , Serina-ARNt Ligasa/aislamiento & purificación , Serina-ARNt Ligasa/metabolismoRESUMEN
The mechanism of aminoacyl-tRNA synthesis differs substantially between Archaea, Bacteria and Eukarya. Sequencing of archaeal genomes has suggested that the asparaginyl-, cysteinyl-, glutaminyl- and lysyl-tRNA synthetases are absent from a number of organisms in this kingdom. The absence of the asparaginyl- and glutaminyl-tRNA synthetases is in agreement with the observation that Asn-tRNA and Gln-tRNA are synthesized by tRNA-dependent transamidation of Asp-tRNA and Glu-tRNA respectively in the archaeon Haloferax volcanii. Biochemical and genetic studies have now shown that while the cysteinyl- and lysyl-tRNA synthetases are present, the enzymes responsible for these activities are unique to Archaea.