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1.
Nat Commun ; 15(1): 6379, 2024 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-39090097

RESUMO

Unsustainable wildlife trade imperils thousands of species, but efforts to identify and reduce these threats are hampered by rapidly evolving commercial markets. Businesses trading wildlife-derived products innovate to remain competitive, and the patents they file to protect their innovations also provide an early-warning of market shifts. Here, we develop a novel machine-learning approach to analyse patent-filing trends and apply it to patents filed from 1970-2020 related to six traded taxa that vary in trade legality, threat level, and use type: rhinoceroses, pangolins, bears, sturgeon, horseshoe crabs, and caterpillar fungus. We found 27,308 patents, showing 130% per-year increases, compared to a background rate of 104%. Innovation led to diversification, including new fertilizer products using illegal-to-trade rhinoceros horn, and novel farming methods for pangolins. Stricter regulation did not generally correlate with reduced patenting. Patents reveal how wildlife-related businesses predict, adapt to, and create market shifts, providing data to underpin proactive wildlife-trade management approaches.


Assuntos
Animais Selvagens , Comércio , Aprendizado de Máquina , Patentes como Assunto , Comércio de Vida Silvestre , Animais , Conservação dos Recursos Naturais , Perissodáctilos , Ursidae , Comércio de Vida Silvestre/legislação & jurisprudência , Comércio de Vida Silvestre/tendências
2.
Conserv Biol ; 2022 Jan 31.
Artigo em Inglês | MEDLINE | ID: mdl-35098582

RESUMO

An important rationale for legally-farmed and synthetic wildlife products are that they reduce illegal wild-sourced trade by supplying markets with sustainable alternatives. For this to work, more established illegal-product consumers must switch to legal alternatives than new legal-product consumers drawn to illegal wild products. Despite widespread debate on the magnitude and direction of switching, studies among actual consumers are lacking. We used an anonymous online survey of 1421 Traditional Chinese Medicine consumers in China to investigate switching between legal farmed, synthetic, and illegal wild bear bile. We examined past consumption behaviour, and applied a discrete choice experiment framed within worsening hypothetical disease scenarios, using latent class models to investigate groups with shared preferences. Bear bile consumers (86% respondents) were wealthier, more likely to have family who consumed bile, and less knowledgeable about bile treatments than non-consumers. Consumer preferences were heterogenous but most consumers preferred switching between bile types as disease worsened. We identified five distinct latent classes within our sample: 'law-abiding consumers' (34% respondents), who prefer legal products and were unlikely to switch; two 'all-natural consumer' groups (53%), who dislike synthetics but may switch between farmed and wild products; and two 'non-consumer' groups (12%) who prefer not to buy bile. People with past experience of bile consumption had different preferences than those without. Willingness to switch to wild products was related to believing they were legal, although the likelihood of switching was mediated by preferences for cheaper products sold in legal, familiar places. We show that consumers of wild bile may switch, given the availability of a range of legal alternatives, while legal-product consumers may switch to illegal products if the barriers to doing so are small. Understanding preferences that promote or impede switching should be a key consideration when attempting to predict consumer behaviour in complex wildlife markets. This article is protected by copyright. All rights reserved.


Wildlife consumer characteristics and preferences determine their likelihood and direction of switching between legal and illegal products.

3.
FEBS Lett ; 497(1): 45-9, 2001 May 18.
Artigo em Inglês | MEDLINE | ID: mdl-11376660

RESUMO

Currently described substrates of the bacterial Tat protein transport system are directed for export by signal peptides containing a pair of invariant arginine residues. The signal peptide of the TtrB subunit of Salmonella enterica tetrathionate reductase contains a single arginine residue but is nevertheless able to mediate Tat pathway transport. This naturally occurring example of a Tat signal peptide lacking a consensus arginine pair expands the range of sequences that can target a protein to the Tat pathway. The possible implications of this finding for the assembly of electron transfer complexes containing Rieske proteins in plant organelles are discussed.


Assuntos
Motivos de Aminoácidos/fisiologia , Oxirredutases/química , Oxirredutases/metabolismo , Sinais Direcionadores de Proteínas/fisiologia , Substituição de Aminoácidos , Arginina/genética , Proteínas de Bactérias/química , Proteínas de Bactérias/genética , Proteínas de Bactérias/metabolismo , Sequência Consenso/fisiologia , Dados de Sequência Molecular , Mutagênese Sítio-Dirigida , Oxirredutases/genética , Transporte Proteico/fisiologia , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Salmonella enterica/enzimologia , Homologia de Sequência de Aminoácidos , Relação Estrutura-Atividade , Frações Subcelulares/química
4.
Biochim Biophys Acta ; 1459(2-3): 325-30, 2000 Aug 15.
Artigo em Inglês | MEDLINE | ID: mdl-11004447

RESUMO

The Tat system is a recently discovered bacterial protein transport pathway that functions primarily in the biosynthesis of proteins containing redox active cofactors. Analogous transport systems are found in plant organelles. Remarkably and uniquely the Tat system functions to transported a diverse range of folded proteins across a biological membrane, a feat that must be achieved without rendering the membrane freely permeable to protons and other ions. Here we review the operation of the bacterial Tat system and propose a model for the structural organisation of the Tat preprotein translocase.


Assuntos
Adenosina Trifosfatases/metabolismo , Bactérias/metabolismo , Proteínas de Bactérias , Proteínas de Transporte/metabolismo , Proteínas de Escherichia coli , Proteínas de Membrana Transportadoras , Transporte Proteico , Adenosina Trifosfatases/química , Bactérias/genética , Proteínas de Transporte/química , Transporte de Elétrons , Metabolismo Energético , Escherichia coli , Genes Reguladores , Membranas Intracelulares/química , Membranas Intracelulares/metabolismo , Canais de Translocação SEC , Proteínas SecA
5.
J Bacteriol ; 181(22): 6907-13, 1999 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-10559155

RESUMO

A pleiotropic mutant of Paracoccus denitrificans, which has a severe defect that affects its anaerobic growth when either nitrate, nitrite, or nitrous oxide is used as the terminal electron acceptor and which is also unable to use ethanolamine as a carbon and energy source for aerobic growth, was isolated. This phenotype of the mutant is expressed only during growth on minimal media and can be reversed by addition of cobalamin (vitamin B(12)) or cobinamide to the media or by growth on rich media. Sequence analysis revealed the mutation causing this phenotype to be in a gene homologous to cobK of Pseudomonas denitrificans, which encodes precorrin-6x reductase of the cobalamin biosynthesis pathway. Convergently transcribed with cobK is a gene homologous to cobJ of Pseudomonas denitrificans, which encodes precorrin-3b methyltransferase. The inability of the cobalamin auxotroph to grow aerobically on ethanolamine implies that wild-type P. denitrificans (which can grow on ethanolamine) expresses a cobalamin-dependent ethanolamine ammonia lyase and that this organism synthesizes cobalamin under both aerobic and anaerobic growth conditions. Comparison of the cobK and cobJ genes with their orthologues suggests that P. denitrificans uses the aerobic pathway for cobalamin synthesis. It is paradoxical that under anaerobic growth conditions, P. denitrificans appears to use the aerobic (oxygen-requiring) pathway for cobalamin synthesis. Anaerobic growth of the cobalamin auxotroph could be restored by the addition of deoxyribonucleosides to minimal media. These observations provide evidence that P. denitrificans expresses a cobalamin-dependent ribonucleotide reductase, which is essential for growth only under anaerobic conditions.


Assuntos
Proteínas de Bactérias , Metiltransferases/genética , Oxirredutases/genética , Paracoccus denitrificans/crescimento & desenvolvimento , Paracoccus denitrificans/genética , Vitamina B 12/metabolismo , Sequência de Aminoácidos , Anaerobiose , Deleção de Genes , Regulação Bacteriana da Expressão Gênica , Teste de Complementação Genética , Metiltransferases/química , Metiltransferases/metabolismo , Dados de Sequência Molecular , Oxirredutases/química , Oxirredutases/metabolismo , Paracoccus denitrificans/enzimologia , Regiões Promotoras Genéticas , Alinhamento de Sequência , Análise de Sequência de DNA
6.
Mol Microbiol ; 32(2): 275-87, 1999 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-10231485

RESUMO

A range of bacteria are able to use tetrathionate as a terminal respiratory electron acceptor. Here we report the identification and characterization of the ttrRSBCA locus required for tetrathionate respiration in Salmonella typhimurium LT2a. The ttr genes are located within Salmonella pathogenicity island 2 at centisome 30.5. ttrA, ttrB and ttrC are the tetrathionate reductase structural genes. Sequence analysis suggests that TtrA contains a molybdopterin guanine dinucleotide cofactor and a [4Fe-4S] cluster, that TtrB binds four [4Fe-4S] clusters, and that TtrC is an integral membrane protein containing a quinol oxidation site. TtrA and TtrB are predicted to be anchored by TtrC to the periplasmic face of the cytoplasmic membrane implying a periplasmic site for tetrathionate reduction. It is inferred that the tetrathionate reductase, together with thiosulphate and polysulphide reductases, make up a previously unrecognized class of molybdopterin-dependent enzymes that carry out the reductive cleavage of sulphur-sulphur bonds. Cys-256 in TtrA is proposed to be the amino acid ligand to the molybdopterin cofactor. TtrS and TtrR are the sensor and response regulator components of a two-component regulatory system that is absolutely required for transcription of the ttrBCA operon. Expression of an active tetrathionate reduction system also requires the anoxia-responsive global transcriptional regulator Fnr. The ttrRSBCA gene cluster confers on Escherichia coli the ability to respire with tetrathionate as electron acceptor.


Assuntos
Oxirredutases/genética , Oxirredutases/metabolismo , Salmonella typhimurium/enzimologia , Salmonella typhimurium/genética , Ácido Tetratiônico/metabolismo , Sequência de Aminoácidos , Sequência de Bases , Mapeamento Cromossômico , Elementos de DNA Transponíveis/genética , Genes Bacterianos , Dados de Sequência Molecular , Mutagênese Insercional , Óperon , Oxirredução , Oxirredutases/química , Regiões Promotoras Genéticas , Análise de Sequência de DNA
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