PMID:7809142: Difference between revisions

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<span style = 'font-size: large'> '''Jordan, A, Pontis, E, Atta, M, Krook, M, Gibert, I, Barbé, J and Reichard, P'''  (1994) A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme.''Proc. Natl. Acad. Sci. U.S.A.'' '''91''':12892-6</span>
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!align=left  |Citation
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'''Jordan, A, Pontis, E, Atta, M, Krook, M, Gibert, I, Barbé, J and Reichard, P'''  (1994) A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme. ''Proc. Natl. Acad. Sci. U.S.A.'' '''91''':12892-6
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!align=left  |Abstract
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The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose corresponding protein sequences show some homology to the products of the genes nrdA and nrdB. When present on a plasmid, nrdE and nrdF together complement mutations in nrdA or nrdB. We have now obtained in nearly homogeneous form the two proteins encoded by the S. typhimurium nrdE and nrdF genes (R1E and R2F). They correspond to the R1 and R2 proteins. Each protein is a homodimer. Together they catalyze the reduction of CDP to dCDP, using dithiothreitol or reduced glutaredoxin, but not thioredoxin, as an electron donor. CDP reduction is strongly stimulated by low concentrations of dATP, presumably acting as an allosteric effector. Protein R2F contains an antiferromagnetically coupled dinuclear iron center and a tyrosyl free radical. The E. coli and S. typhimurium chromosome thus have maintained the information for a potentially active additional class I ribonucleotide reductase, whose role in vivo is as yet unknown. The allosteric regulation of this enzyme differs from that of the normally expressed reductase.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7809142 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC45546 PMC45546]


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|{{TableHeadingColor}} |'''Abstract''' || The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose corresponding protein sequences show some homology to the products of the genes nrdA and nrdB. When present on a plasmid, nrdE and nrdF together complement mutations in nrdA or nrdB. We have now obtained in nearly homogeneous form the two proteins encoded by the S. typhimurium nrdE and nrdF genes (R1E and R2F). They correspond to the R1 and R2 proteins. Each protein is a homodimer. Together they catalyze the reduction of CDP to dCDP, using dithiothreitol or reduced glutaredoxin, but not thioredoxin, as an electron donor. CDP reduction is strongly stimulated by low concentrations of dATP, presumably acting as an allosteric effector. Protein R2F contains an antiferromagnetically coupled dinuclear iron center and a tyrosyl free radical. The E. coli and S. typhimurium chromosome thus have maintained the information for a potentially active additional class I ribonucleotide reductase, whose role in vivo is as yet unknown. The allosteric regulation of this enzyme differs from that of the normally expressed reductase.
!align=left  |Keywords
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Allosteric Regulation; Amino Acid Sequence; Bacterial Proteins/isolation & purification; Catalysis; Cytidine Diphosphate/metabolism; Electron Spin Resonance Spectroscopy; Genes, Bacterial; Genetic Complementation Test; Glutaredoxins; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Proteins/pharmacology; Ribonucleotide Reductases/classification; Ribonucleotide Reductases/genetics; Ribonucleotide Reductases/metabolism; Salmonella typhimurium/enzymology; Thioredoxins/pharmacology
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7809142 PubMed]
 
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Latest revision as of 04:51, 15 September 2013

Citation

Jordan, A, Pontis, E, Atta, M, Krook, M, Gibert, I, Barbé, J and Reichard, P (1994) A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme. Proc. Natl. Acad. Sci. U.S.A. 91:12892-6

Abstract

The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose corresponding protein sequences show some homology to the products of the genes nrdA and nrdB. When present on a plasmid, nrdE and nrdF together complement mutations in nrdA or nrdB. We have now obtained in nearly homogeneous form the two proteins encoded by the S. typhimurium nrdE and nrdF genes (R1E and R2F). They correspond to the R1 and R2 proteins. Each protein is a homodimer. Together they catalyze the reduction of CDP to dCDP, using dithiothreitol or reduced glutaredoxin, but not thioredoxin, as an electron donor. CDP reduction is strongly stimulated by low concentrations of dATP, presumably acting as an allosteric effector. Protein R2F contains an antiferromagnetically coupled dinuclear iron center and a tyrosyl free radical. The E. coli and S. typhimurium chromosome thus have maintained the information for a potentially active additional class I ribonucleotide reductase, whose role in vivo is as yet unknown. The allosteric regulation of this enzyme differs from that of the normally expressed reductase.

Links

PubMed PMC45546

Keywords

Allosteric Regulation; Amino Acid Sequence; Bacterial Proteins/isolation & purification; Catalysis; Cytidine Diphosphate/metabolism; Electron Spin Resonance Spectroscopy; Genes, Bacterial; Genetic Complementation Test; Glutaredoxins; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Proteins/pharmacology; Ribonucleotide Reductases/classification; Ribonucleotide Reductases/genetics; Ribonucleotide Reductases/metabolism; Salmonella typhimurium/enzymology; Thioredoxins/pharmacology

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