Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (390 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.26, 5-year impact factor: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-4344586909&partnerID=40&md5=d60ad81d897a89232b10ea3a9dd55049
Keywords: Archaea, Protein Disulfide Oxidoreductase, Protein Disulfide-Isomerase, Pyrococcus Furiosus, Redox Sites, Adenosine Triphosphatase, Cation, Mutant Protein, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Archaebacterium, Article, Carboxy Terminal Sequence, Comparative Study, Controlled Study, Enzyme Active Site, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Phylogeny, Nonhuman, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Family, Sequence Homology, Temperature Dependence, Amino Acid Sequence, Animals, Cattle, Circular Dichroism, Cysteine, Insulin, Molecular Sequence Data, Mutation, Nadph Oxidoreductases, Oxidation-Reduction, Ribonucleases, Bacteria (microorganisms), Eukaryota,
Affiliations:
*** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy
Center for Structural Biochemistry, Karolinska Institutet, Huddinge, Sweden
Dipartimento di Chimica Biologica, Univ. Studi di Napoli Federico II, Napoli, Italy
Ist. di Biochimica Delle Proteine, C.N.R., Napoli, Italy
References:
McFarlan, S.C., Terrell, C.A., Hogenkamp, H.P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J. Biol. Chem., 267, pp. 10561-1056
Bhattacharyya, S., Habibi-Nazhad, B., Amegbey, G., Slupsky, C., Yee, A., Arrowsmith, C., Wishart, D.S., Identification of a novel archaebacterial thioredoxin: Determination of function through structure (2002) Biochemistry, 41, pp. 4760-4770
Bult, C.J., White, O., Olsen, G.J., Zhou, L., Fleischmann, R.D., Sutton, G.G., Blake, J.A., Venter, J.C., Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii (1996) Science, 273, pp. 1058-1073
Lee, D.Y., Ahn, B., Kim, K., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Cave, J.W., Cho, H.S., Batchelder, A.M., Yokota, H., Kim, R., Wemmer, D.E., Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii (2001) Protein Sci., 10, pp. 384-396
Guagliardi, A., Nobile, V., Bartolucci, S., Rossi, M., A thioredoxin from the extreme thermophilic archaeon Sulfolobus solfataricus (1994) Int. J. Biochem., 26, pp. 375-380
Guagliardi, A., De Pascale, D., Cannio, R., Nobile, V., Bartolucci, S., Rossi, M., The purification, cloning, and high level expression of a glutaredoxin-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (1995) J. Biol. Chem., 270, pp. 5748-5755
Bartolucci, S., De Pascale, D., Rossi, M., Protein disulfide oxidoreductase from Pyrococcus furiosus: Biochemical properties (2001) Methods Enzymol., 334, pp. 62-73
Ren, B., Tibbelin, G., De Pascale, D., Rossi, M., Bartolucci, S., Ladenstein, R., Crystallization and preliminary X-ray structure analysis of a hyperthermostable thioltransferase from the archaeon Pyrococcus furiosus (1997) J. Struct. Biol., 119, pp. 1-5
Ren, B., Ladenstein, R., Protein disulfide oxidoreductase from Pyrococcus furiosus: Structural properties (2001) Methods Enzymol., 334, pp. 74-88
Freedman, R.B., Novel disulfide oxidoreductase in search of a function (1998) Nat. Struct. Biol., 5, pp. 531-532
Ruddock, L.W., Hirst, T.R., Feedman, R.B., H-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol: Disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1996) Biochem. J., 315, pp. 1000-1005
Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
Barker, D.G., Cloning and amplified expression of the tyrosyl-tRNA synthetase genes of Bacillus stearothermophilus and Escherichia coli (1982) Eur. J. Biochem., 125, pp. 357-360
Saiki, R.K., Amplification of genomic DNA (1990) PCR Protocols: A Guide to Methods and Applications, pp. 13-20. , Innis, M.A., Gellfand, D.A., Sninski, J.J. & White, T.J., eds, Academic Press, New York
Kunkel, T.A., Rapid and efficient site-specific mutagenesis without phenotypic selection (1985) Proc. Natl Acad. Sci. USA, 82, pp. 488-492
Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl Acad. Sci. USA, 76, pp. 5653-5667
Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Klenk, D.C., Measurement of protein using bicinchoninic acid (1995) Anal. Biochem., 150, pp. 76-85
Rabilloud, T., Vuillard, L., Gilly, C., Lawrence, J.J., Silver-staining of proteins in polyacrylamide gels: A general overview (1994) Cell. Mol. Biol., 40, pp. 57-75
Hollecker, M., Creighton, T.E., Counting integral numbers of amino groups per polypeptide chain (1980) FEBS Lett., 119, pp. 187-190
Davies, G.E., Stark, G.R., Use of dimethyl sub-erimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins (1970) Proc. Natl Acad. Sci. USA, 66, pp. 651-656
Holmgren, A., Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide (1979) J. Biol. Chem., 254, pp. 9627-9632
Lambert, N., Freedman, R.B., Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction (1983) Biochem. J., 213, pp. 235-243
Kunitz, M., A spectrophotometric method for the measurement of ribonuclease activity (1946) J. Biol. Chem., 164, pp. 563-568
Catz, S.D., Johnson, J.L., Babior, B.M., Characterization of the nucleotide-binding capacity and the ATPase activity of the PIP3-binding protein JFC1 (2001) Proc. Natl Acad. Sci. USA, 28, pp. 11230-11235
Guagliardi, A., Cerchia, L., Bartolucci, S., Rossi, M., The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro (1994) Protein Sci., 3, pp. 1436-1443
Lanzetta, P.A., Alvarez, L.J., Reinach, P.S., Candia, O.A., An improved assay for nanomole amounts of inorganic phosphate (1979) Anal Biochem., 100, pp. 95-97
Vuori, K., Myllyla, R., Pihlajaniemi, T., Kivirikko, K.I., Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity (1992) J. Biol. Chem., 267, pp. 7211-7217
Saraste, M., Sibbald, P.R., Wittinghofer, A., The P-loop: A common motif in ATP- and GTP-binding proteins (1990) Trends Biochem. Sci., 15, pp. 430-434
Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W., Pearl, L.H., Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone (1997) Cell, 90, pp. 65-75
Bergerat, A., De Massy, B., Gadelle, D., Varoutas, P.C., Nicolas, A., Forterre, P., An atypical topoisomerase II from Archaea with implications for meiotic recombination (1997) Nature (London), 386, pp. 414-417
Jakob, U., Scheibel, T., Bose, S., Reinstein, J., Buchner, J., Assessment of the ATP binding properties of Hsp90 (1996) J. Biol. Chem., 271, pp. 10035-10041
Quemeneur, E., Guthapfel, R., Gueguen, P., A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase (1994) J. Biol. Chem., 269, pp. 5485-5488
Baross, J.A., Holden, J.F., Overview of hyperthermophiles and their heat-shock proteins (1996) Adv. Protein Chem., 48, pp. 1-34
Freedman, R.B., Klappa, P., Ruddock, L.W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Report, 3, pp. 136-140
Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., Creighton, T.E., Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy (1996) Biochemistry, 35, pp. 7684-7691
Darby, N.J., Kemmink, J., Creighton, T.E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Zapun, A., Creighton, T.E., Rowling, P.J., Freedman, R.B., Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum (1992) Proteins, 14, pp. 10-15
Robb, F.T., Maeder, D.L., Brown, J.R., DiRuggiero, J., Stump, M.D., Yeh, R.K., Weiss, R.B., Dunn, D.M., Genomic sequence of hyperthermophile, Pyrococcus furiosus: Implications for physiology and enzymology (2001) Methods Enzymol., 330, pp. 134-157
She, Q., Singh, R.K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M.J., Chan-Weiher, C.C., Van Der Oost, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proc. Natl Acad. Sci. USA, 98, pp. 7835-7840
Chinen, A., Uchiyama, I., Kobayashi, I., Comparison between Pyrococcus horikoshii and Pyrococcus abyssi genome sequences reveals linkage of restriction-modification genes with large genome polymorphisms (2000) Gene, 259, pp. 109-121
Kawarabayasi, Y., Hino, Y., Horikawa, H., Jin-n, O.K., Takahashi, M., Sekine, M., Baba, S., Kikuchi, H., Complete genome sequence of an aerobic thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain7 (2001) DNA Res., 8, pp. 123-140
Ruepp, A., Graml, W., Santos-Martinez, M.L., Koretke, K.K., Volker, C., Mewes, H.W., Frishman, D., Baumeister, W., The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum (2000) Nature (London), 407, pp. 508-513
Kawashima, T., Amano, N., Koike, H., Makino, S., Higuchi, S., Kawashima-Ohya, Y., Watanabe, K., Suzuki, M., Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium (2000) Proc. Natl Acad. Sci. USA, 97, pp. 14257-14262
Deckert, G., Warren, P.V., Gaasterland, T., Young, W.G., Lenox, L., Graham, D.E., Overbeek, R., Swanson, R.V., The complete genome of the hyperthermophilic bacterium Aquifex aeolicus (1998) Nature (London), 392, pp. 353-358
Bao, Q., Tian, Y., Li, W., Xu, Z., Xuan, Z., Hu, S., Dong, W., Yang, H., A complete sequence of the T. tengcongensis genome (2002) Genome Res., 12, pp. 689-700
Nelson, K.E., Eisen, J.A., Fraser, C.M., Genome of Thermotoga maritima MSB8 (2001) Methods Enzymol., 330, pp. 169-180
Makarova, K.S., Koonin, E.V., Comparative genomics of archaea: How much have we learned in six years, and what's next? (2003) Genome Biol., 4, pp. 115-145
Kashima, Y., Ishikawa, K., A hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii (2003) Arch. Biochem. Biophysics, 418, pp. 179-185
Mallick, P., Boutz, D.R., Eisenberg, D., Yeates, T.O., Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds (2002) Proc. Natl Acad. Sci. USA, 99, pp. 9679-9684
McFarlan, S. C., Terrell, C. A., Hogenkamp, H. P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J. Biol. Chem., 267, pp. 10561-1056
Bult, C. J., White, O., Olsen, G. J., Zhou, L., Fleischmann, R. D., Sutton, G. G., Blake, J. A., Venter, J. C., Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii (1996) Science, 273, pp. 1058-1073
Lee, D. Y., Ahn, B., Kim, K., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Cave, J. W., Cho, H. S., Batchelder, A. M., Yokota, H., Kim, R., Wemmer, D. E., Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii (2001) Protein Sci., 10, pp. 384-396
Freedman, R. B., Novel disulfide oxidoreductase in search of a function (1998) Nat. Struct. Biol., 5, pp. 531-532
Ruddock, L. W., Hirst, T. R., Feedman, R. B., H-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol: Disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1996) Biochem. J., 315, pp. 1000-1005
Barker, D. G., Cloning and amplified expression of the tyrosyl-tRNA synthetase genes of Bacillus stearothermophilus and Escherichia coli (1982) Eur. J. Biochem., 125, pp. 357-360
Saiki, R. K., Amplification of genomic DNA (1990) PCR Protocols: A Guide to Methods and Applications, pp. 13-20. , Innis, M. A., Gellfand, D. A., Sninski, J. J. & White, T. J., eds, Academic Press, New York
Kunkel, T. A., Rapid and efficient site-specific mutagenesis without phenotypic selection (1985) Proc. Natl Acad. Sci. USA, 82, pp. 488-492
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Klenk, D. C., Measurement of protein using bicinchoninic acid (1995) Anal. Biochem., 150, pp. 76-85
Davies, G. E., Stark, G. R., Use of dimethyl sub-erimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins (1970) Proc. Natl Acad. Sci. USA, 66, pp. 651-656
Catz, S. D., Johnson, J. L., Babior, B. M., Characterization of the nucleotide-binding capacity and the ATPase activity of the PIP3-binding protein JFC1 (2001) Proc. Natl Acad. Sci. USA, 28, pp. 11230-11235
Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., Candia, O. A., An improved assay for nanomole amounts of inorganic phosphate (1979) Anal Biochem., 100, pp. 95-97
Baross, J. A., Holden, J. F., Overview of hyperthermophiles and their heat-shock proteins (1996) Adv. Protein Chem., 48, pp. 1-34
Freedman, R. B., Klappa, P., Ruddock, L. W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Report, 3, pp. 136-140
Darby, N. J., Kemmink, J., Creighton, T. E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Robb, F. T., Maeder, D. L., Brown, J. R., DiRuggiero, J., Stump, M. D., Yeh, R. K., Weiss, R. B., Dunn, D. M., Genomic sequence of hyperthermophile, Pyrococcus furiosus: Implications for physiology and enzymology (2001) Methods Enzymol., 330, pp. 134-157
She, Q., Singh, R. K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M. J., Chan-Weiher, C. C., Van Der Oost, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proc. Natl Acad. Sci. USA, 98, pp. 7835-7840
Nelson, K. E., Eisen, J. A., Fraser, C. M., Genome of Thermotoga maritima MSB8 (2001) Methods Enzymol., 330, pp. 169-180
Makarova, K. S., Koonin, E. V., Comparative genomics of archaea: How much have we learned in six years, and what's next? (2003) Genome Biol., 4, pp. 115-145
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.26, 5-year impact factor: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-4344586909&partnerID=40&md5=d60ad81d897a89232b10ea3a9dd55049
Keywords: Archaea, Protein Disulfide Oxidoreductase, Protein Disulfide-Isomerase, Pyrococcus Furiosus, Redox Sites, Adenosine Triphosphatase, Cation, Mutant Protein, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Archaebacterium, Article, Carboxy Terminal Sequence, Comparative Study, Controlled Study, Enzyme Active Site, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Phylogeny, Nonhuman, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Family, Sequence Homology, Temperature Dependence, Amino Acid Sequence, Animals, Cattle, Circular Dichroism, Cysteine, Insulin, Molecular Sequence Data, Mutation, Nadph Oxidoreductases, Oxidation-Reduction, Ribonucleases, Bacteria (microorganisms), Eukaryota,
Affiliations:
*** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy
Center for Structural Biochemistry, Karolinska Institutet, Huddinge, Sweden
Dipartimento di Chimica Biologica, Univ. Studi di Napoli Federico II, Napoli, Italy
Ist. di Biochimica Delle Proteine, C.N.R., Napoli, Italy
References:
McFarlan, S.C., Terrell, C.A., Hogenkamp, H.P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J. Biol. Chem., 267, pp. 10561-1056
Bhattacharyya, S., Habibi-Nazhad, B., Amegbey, G., Slupsky, C., Yee, A., Arrowsmith, C., Wishart, D.S., Identification of a novel archaebacterial thioredoxin: Determination of function through structure (2002) Biochemistry, 41, pp. 4760-4770
Bult, C.J., White, O., Olsen, G.J., Zhou, L., Fleischmann, R.D., Sutton, G.G., Blake, J.A., Venter, J.C., Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii (1996) Science, 273, pp. 1058-1073
Lee, D.Y., Ahn, B., Kim, K., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Cave, J.W., Cho, H.S., Batchelder, A.M., Yokota, H., Kim, R., Wemmer, D.E., Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii (2001) Protein Sci., 10, pp. 384-396
Guagliardi, A., Nobile, V., Bartolucci, S., Rossi, M., A thioredoxin from the extreme thermophilic archaeon Sulfolobus solfataricus (1994) Int. J. Biochem., 26, pp. 375-380
Guagliardi, A., De Pascale, D., Cannio, R., Nobile, V., Bartolucci, S., Rossi, M., The purification, cloning, and high level expression of a glutaredoxin-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (1995) J. Biol. Chem., 270, pp. 5748-5755
Bartolucci, S., De Pascale, D., Rossi, M., Protein disulfide oxidoreductase from Pyrococcus furiosus: Biochemical properties (2001) Methods Enzymol., 334, pp. 62-73
Ren, B., Tibbelin, G., De Pascale, D., Rossi, M., Bartolucci, S., Ladenstein, R., Crystallization and preliminary X-ray structure analysis of a hyperthermostable thioltransferase from the archaeon Pyrococcus furiosus (1997) J. Struct. Biol., 119, pp. 1-5
Ren, B., Ladenstein, R., Protein disulfide oxidoreductase from Pyrococcus furiosus: Structural properties (2001) Methods Enzymol., 334, pp. 74-88
Freedman, R.B., Novel disulfide oxidoreductase in search of a function (1998) Nat. Struct. Biol., 5, pp. 531-532
Ruddock, L.W., Hirst, T.R., Feedman, R.B., H-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol: Disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1996) Biochem. J., 315, pp. 1000-1005
Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
Barker, D.G., Cloning and amplified expression of the tyrosyl-tRNA synthetase genes of Bacillus stearothermophilus and Escherichia coli (1982) Eur. J. Biochem., 125, pp. 357-360
Saiki, R.K., Amplification of genomic DNA (1990) PCR Protocols: A Guide to Methods and Applications, pp. 13-20. , Innis, M.A., Gellfand, D.A., Sninski, J.J. & White, T.J., eds, Academic Press, New York
Kunkel, T.A., Rapid and efficient site-specific mutagenesis without phenotypic selection (1985) Proc. Natl Acad. Sci. USA, 82, pp. 488-492
Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl Acad. Sci. USA, 76, pp. 5653-5667
Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Klenk, D.C., Measurement of protein using bicinchoninic acid (1995) Anal. Biochem., 150, pp. 76-85
Rabilloud, T., Vuillard, L., Gilly, C., Lawrence, J.J., Silver-staining of proteins in polyacrylamide gels: A general overview (1994) Cell. Mol. Biol., 40, pp. 57-75
Hollecker, M., Creighton, T.E., Counting integral numbers of amino groups per polypeptide chain (1980) FEBS Lett., 119, pp. 187-190
Davies, G.E., Stark, G.R., Use of dimethyl sub-erimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins (1970) Proc. Natl Acad. Sci. USA, 66, pp. 651-656
Holmgren, A., Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide (1979) J. Biol. Chem., 254, pp. 9627-9632
Lambert, N., Freedman, R.B., Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction (1983) Biochem. J., 213, pp. 235-243
Kunitz, M., A spectrophotometric method for the measurement of ribonuclease activity (1946) J. Biol. Chem., 164, pp. 563-568
Catz, S.D., Johnson, J.L., Babior, B.M., Characterization of the nucleotide-binding capacity and the ATPase activity of the PIP3-binding protein JFC1 (2001) Proc. Natl Acad. Sci. USA, 28, pp. 11230-11235
Guagliardi, A., Cerchia, L., Bartolucci, S., Rossi, M., The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro (1994) Protein Sci., 3, pp. 1436-1443
Lanzetta, P.A., Alvarez, L.J., Reinach, P.S., Candia, O.A., An improved assay for nanomole amounts of inorganic phosphate (1979) Anal Biochem., 100, pp. 95-97
Vuori, K., Myllyla, R., Pihlajaniemi, T., Kivirikko, K.I., Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity (1992) J. Biol. Chem., 267, pp. 7211-7217
Saraste, M., Sibbald, P.R., Wittinghofer, A., The P-loop: A common motif in ATP- and GTP-binding proteins (1990) Trends Biochem. Sci., 15, pp. 430-434
Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W., Pearl, L.H., Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone (1997) Cell, 90, pp. 65-75
Bergerat, A., De Massy, B., Gadelle, D., Varoutas, P.C., Nicolas, A., Forterre, P., An atypical topoisomerase II from Archaea with implications for meiotic recombination (1997) Nature (London), 386, pp. 414-417
Jakob, U., Scheibel, T., Bose, S., Reinstein, J., Buchner, J., Assessment of the ATP binding properties of Hsp90 (1996) J. Biol. Chem., 271, pp. 10035-10041
Quemeneur, E., Guthapfel, R., Gueguen, P., A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase (1994) J. Biol. Chem., 269, pp. 5485-5488
Baross, J.A., Holden, J.F., Overview of hyperthermophiles and their heat-shock proteins (1996) Adv. Protein Chem., 48, pp. 1-34
Freedman, R.B., Klappa, P., Ruddock, L.W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Report, 3, pp. 136-140
Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., Creighton, T.E., Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy (1996) Biochemistry, 35, pp. 7684-7691
Darby, N.J., Kemmink, J., Creighton, T.E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Zapun, A., Creighton, T.E., Rowling, P.J., Freedman, R.B., Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum (1992) Proteins, 14, pp. 10-15
Robb, F.T., Maeder, D.L., Brown, J.R., DiRuggiero, J., Stump, M.D., Yeh, R.K., Weiss, R.B., Dunn, D.M., Genomic sequence of hyperthermophile, Pyrococcus furiosus: Implications for physiology and enzymology (2001) Methods Enzymol., 330, pp. 134-157
She, Q., Singh, R.K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M.J., Chan-Weiher, C.C., Van Der Oost, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proc. Natl Acad. Sci. USA, 98, pp. 7835-7840
Chinen, A., Uchiyama, I., Kobayashi, I., Comparison between Pyrococcus horikoshii and Pyrococcus abyssi genome sequences reveals linkage of restriction-modification genes with large genome polymorphisms (2000) Gene, 259, pp. 109-121
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Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase
Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol-disulfide exchange reactions with a CXXC sequence motif at their active site. A disulfide oxidoreductase, a highly thermostable protein, was isolated from Pyrococcus furiosus (PfPDO), which is characterized by two redox sites (CXXC) and an unusual molecular mass. Its 3D structure at high resolution suggests that it may be related to the multidomain protein disulfide-isomerase (PDI), which is currently known only in eukaryotes. This work focuses on the functional characterization of PfPDO as well as its relation to the eukaryotic PDIs. Assays of oxidative, reductive, and isomerase activities of PfPDO were performed, which revealed that the archaeal protein not only has oxidative and reductive activity, but also isomerase activity. On the basis of structural data, two single mutants (C35S and C146S) and a double mutant (C35S/C146S) of PfPDO were constructed and analyzed to elucidate the specific roles of the two redox sites. The results indicate that the CPYC site in the C-terminal half of the protein is fundamental to reductive/oxidative activity, whereas isomerase activity requires both active sites. In comparison with PDI, the ATPase activity was tested for PfPDO, which was found to be cation-dependent with a basic pH optimum and an optimum temperature of 90 degreesC. These results and an investigation on genomic sequence databases indicate that PfPDO may be an ancestor of the eukaryotic PDI and belongs to a novel protein disulfide oxidoreductase family.
Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol-disulfide exchange reactions with a CXXC sequence motif at their active site. A disulfide oxidoreductase, a highly thermostable protein, was isolated from Pyrococcus furiosus (PfPDO), which is characterized by two redox sites (CXXC) and an unusual molecular mass. Its 3D structure at high resolution suggests that it may be related to the multidomain protein disulfide-isomerase (PDI), which is currently known only in eukaryotes. This work focuses on the functional characterization of PfPDO as well as its relation to the eukaryotic PDIs. Assays of oxidative, reductive, and isomerase activities of PfPDO were performed, which revealed that the archaeal protein not only has oxidative and reductive activity, but also isomerase activity. On the basis of structural data, two single mutants (C35S and C146S) and a double mutant (C35S/C146S) of PfPDO were constructed and analyzed to elucidate the specific roles of the two redox sites. The results indicate that the CPYC site in the C-terminal half of the protein is fundamental to reductive/oxidative activity, whereas isomerase activity requires both active sites. In comparison with PDI, the ATPase activity was tested for PfPDO, which was found to be cation-dependent with a basic pH optimum and an optimum temperature of 90 degreesC. These results and an investigation on genomic sequence databases indicate that PfPDO may be an ancestor of the eukaryotic PDI and belongs to a novel protein disulfide oxidoreductase family.
Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase
| ▼ Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions |
Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.125
View Export to BibTeX Export to EndNote
Bonomo RP, De Flora A, Rizzarelli E, Santoro AM, Tabbì G, Tonetti M
Copper(II) complexes encapsulated in human red blood cells (587 views)
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20 Records (20 excluding Abstracts).
Total impact factor: 77.441 (77.441 excluding Abstracts).
Total 5 year impact factor: 80.23 (80.23 excluding Abstracts).
Total impact factor: 77.441 (77.441 excluding Abstracts).
Total 5 year impact factor: 80.23 (80.23 excluding Abstracts).
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