Disulfide Bond Oxidoreductases
Mostrando 1-12 de 14 artigos, teses e dissertações.
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1. Estudos estruturais e funcionais das oxidoredutases de pontes dissulfeto da familia DsbA de Xylella fastidiosa / Structural and functional studies of the disulfide oxidorecdutases DsbA from Xylella fastidiosa
As oxidoredutases de pontes dissulfeto da família DsbA são responsáveis pela catálise da formação de pontes dissulfeto em proteínas secretadas para o periplasma, participando do processo de enovelamento de fatores de virulência de diversos organismos. É a proteína com maior potencial de oxidação atualmente caracterizada e tal propriedade é assoc
Publicado em: 2008
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2. Characterization of SrgA, a Salmonella enterica Serovar Typhimurium Virulence Plasmid-Encoded Paralogue of the Disulfide Oxidoreductase DsbA, Essential for Biogenesis of Plasmid-Encoded Fimbriae
Disulfide oxidoreductases are viewed as foldases that help to maintain proteins on productive folding pathways by enhancing the rate of protein folding through the catalytic incorporation of disulfide bonds. SrgA, encoded on the virulence plasmid pStSR100 of Salmonella enterica serovar Typhimurium and located downstream of the plasmid-borne fimbrial operon,
American Society for Microbiology.
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3. Two Pairs of Conserved Cysteines Are Required for the Oxidative Activity of Ero1p in Protein Disulfide Bond Formation in the Endoplasmic Reticulum
In the major pathway for protein disulfide-bond formation in the endoplasmic reticulum (ER), oxidizing equivalents flow from the conserved ER-membrane protein Ero1p to secretory proteins via protein disulfide isomerase (PDI). Herein, a mutational analysis of the yeast ERO1 gene identifies two pairs of conserved cysteines likely to form redox-active disu
The American Society for Cell Biology.
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4. The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm
Thioredoxin 1 is a major thiol-disulfide oxidoreductase in the cytoplasm of Escherichia coli. One of its functions is presumed to be the reduction of the disulfide bond in the active site of the essential enzyme ribonucleotide reductase. Thioredoxin 1 is kept in a reduced state by thioredoxin reductase. In a thioredoxin reductase null mutant however, most of
The National Academy of Sciences.
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5. A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation
Proteins of the ERV1/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses for which substantial sequence information is available. Nevertheless, the roles of these proteins are imprecisely known. Multiple alignments of ERV1/ALR proteins indicated an invariant C-X-X-C motif, but no similarity to the thioredoxin fold was revealed by second
The National Academy of Sciences.
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6. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC–DsbDα complex
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDα) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC–DsbDα complex. The 2.3
Oxford University Press.
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7. Complete pathway for protein disulfide bond formation encoded by poxviruses
We show that three cytoplasmic thiol oxidoreductases encoded by vaccinia virus comprise a complete pathway for formation of disulfide bonds in intracellular virion membrane proteins. The pathway was defined by analyzing conditional lethal mutants and effects of cysteine to serine substitutions and by trapping disulfide-bonded heterodimer intermediates for ea
The National Academy of Sciences.
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8. Protein Thiol Modifications Visualized In Vivo
Thiol-disulfide interconversions play a crucial role in the chemistry of biological systems. They participate in the major systems that control the cellular redox potential and prevent oxidative damage. In addition, thiol-disulfide exchange reactions serve as molecular switches in a growing number of redox-regulated proteins. We developed a differential thio
Public Library of Science.
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9. Evaluation of Bottlenecks in the Late Stages of Protein Secretion in Bacillus subtilis
Despite a high capacity for secretion of homologous proteins, the secretion of heterologous proteins by Bacillus subtilis is frequently inefficient. In the present studies, we have investigated and compared bottlenecks in the secretion of four heterologous proteins: Bacillus lichenifomis α-amylase (AmyL), Escherichia coli TEM β-lactamase (Bla), human pancr
American Society for Microbiology.
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10. Expression of Active Human Tissue-Type Plasminogen Activator in Escherichia coli
The formation of native disulfide bonds in complex eukaryotic proteins expressed in Escherichia coli is extremely inefficient. Tissue plasminogen activator (tPA) is a very important thrombolytic agent with 17 disulfides, and despite numerous attempts, its expression in an active form in bacteria has not been reported. To achieve the production of active tPA
American Society for Microbiology.
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11. H-NS Represses Salmonella enterica Serovar Typhimurium dsbA Expression during Exponential Growth
Disulfide bond formation catalyzed by disulfide oxidoreductases occurs in the periplasm and plays a major role in the proper folding and integrity of many proteins. In this study, we were interested in elucidating factors that influence the regulation of dsbA, a gene coding for the primary disulfide oxidoreductase found in Salmonella enterica serovar Typhimu
American Society for Microbiology.
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12. Effect of Sequences of the Active-Site Dipeptides of DsbA and DsbC on In Vivo Folding of Multidisulfide Proteins in Escherichia coli
We have examined the role of the active-site CXXC central dipeptides of DsbA and DsbC in disulfide bond formation and isomerization in the Escherichia coli periplasm. DsbA active-site mutants with a wide range of redox potentials were expressed either from the trc promoter on a multicopy plasmid or from the endogenous dsbA promoter by integration of the resp
American Society for Microbiology.