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Volumn 1481, Issue 1, 2000, Pages 45-54

Contributions of protein disulfide isomerase domains to its chaperone activity

Author keywords

Chaperone; Domain combination; Domain hybrid; Oxidoreductase; Protein disulfide isomerase; Thioredoxin

Indexed keywords

CHAPERONE; LYSOZYME; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN;

EID: 0034739255     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00122-9     Document Type: Article
Times cited : (24)

References (41)
  • 1
    • 0027172321 scopus 로고
    • The bonds that tie: Catalyzed disulfide bond formation
    • Bardwell J.C.A., Beckwith J. The bonds that tie: catalyzed disulfide bond formation. Cell. 74:1993;769-771.
    • (1993) Cell , vol.74 , pp. 769-771
    • Bardwell, J.C.A.1    Beckwith, J.2
  • 2
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene
    • Pihlajaniemi T., Helaakoski T., Tasanen K., Myllyla R., Huhtala M.-L., Koivu J., Kivirikko K.I. Molecular cloning of the β-subunit of prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene. EMBO J. 6:1987;643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.-L.5    Koivu, J.6    Kivirikko, K.I.7
  • 3
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the subunit of 4-hydroxylase and as a protein disulfide isomerase
    • Koivu J., Myllyla R., Helaakoski T., Pihlajaniemi T., Tasanen K., Kivirikko K.I. A single polypeptide acts both as the subunit of 4-hydroxylase and as a protein disulfide isomerase. J. Biol. Chem. 262:1987;6447-6449.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllyla, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 4
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau J.R., Combs K.A., Spinner S.N., Joiner B.J. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem. 265:1990;9800-9807.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 5
    • 0027136018 scopus 로고
    • Protein disulfide isomerase is both an enzyme and a chaperone
    • Wang C.C., Tsou C.L. Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J. 7:1993;1515-1517.
    • (1993) FASEB J. , vol.7 , pp. 1515-1517
    • Wang, C.C.1    Tsou, C.L.2
  • 6
    • 0033210414 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
    • Noiva R. Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum. Cell Dev. Biol. 10:1999;481-493.
    • (1999) Cell Dev. Biol. , vol.10 , pp. 481-493
    • Noiva, R.1
  • 7
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai H., Wang C.C., Tsou C.L. Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem. 269:1994;24550-24552.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24550-24552
    • Cai, H.1    Wang, C.C.2    Tsou, C.L.3
  • 8
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of rhodanese
    • Song J.L., Wang C.C. Chaperone-like activity of protein disulfide isomerase in the refolding of rhodanese. Eur. J. Biochem. 231:1995;312-316.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 9
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A., Gilbert H.F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 269:1994;7764-7771.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.F.2
  • 11
    • 0029620311 scopus 로고    scopus 로고
    • Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell
    • Hayano T., Hirose M., Kikuchi M. Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett. 377:1996;505-511.
    • (1996) FEBS Lett. , vol.377 , pp. 505-511
    • Hayano, T.1    Hirose, M.2    Kikuchi, M.3
  • 12
    • 0031438770 scopus 로고    scopus 로고
    • Dependence of the anti-chaperone activity of protein disulfide isomerase on its chaperone activity
    • Song J.L., Quan H., Wang C.C. Dependence of the anti-chaperone activity of protein disulfide isomerase on its chaperone activity. Biochem. J. 328:1997;841-846.
    • (1997) Biochem. J. , vol.328 , pp. 841-846
    • Song, J.L.1    Quan, H.2    Wang, C.C.3
  • 13
    • 0022387362 scopus 로고
    • Sequence of protein disulfide isomerase and implications of its relationship to thioredoxin
    • Edman J.C., Ellis L., Blacher R.W., Roth R.A., Rutter W.J. Sequence of protein disulfide isomerase and implications of its relationship to thioredoxin. Nature. 317:1985;267-270.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 14
    • 0027959156 scopus 로고
    • Protein disulfide isomerase: Building bridges in protein folding
    • Freedman R.B., Hirst T.R., Tuite M.F. Protein disulfide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19:1994;331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 15
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr. Biol. 7:1997;239-245.
    • (1997) Curr. Biol. , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 16
    • 0033521682 scopus 로고    scopus 로고
    • The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
    • Koivunen P., Pirneskoski A., Karvonen P., Ljung J., Helaakoski T., Notbohm H., Kivirikko K.I. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide. EMBO J. 18:1999;65-74.
    • (1999) EMBO J. , vol.18 , pp. 65-74
    • Koivunen, P.1    Pirneskoski, A.2    Karvonen, P.3    Ljung, J.4    Helaakoski, T.5    Notbohm, H.6    Kivirikko, K.I.7
  • 17
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva R., Freedman R.B., Lennarz W.J. Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J. Biol. Chem. 268:1993;19210-19217.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19210-19217
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.J.3
  • 18
    • 0030836862 scopus 로고    scopus 로고
    • A mutant truncated protein disulfide isomerase with no chaperone activity
    • Dai Y., Wang C.C. A mutant truncated protein disulfide isomerase with no chaperone activity. J. Biol. Chem. 272:1997;27572-27576.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27572-27576
    • Dai, Y.1    Wang, C.C.2
  • 19
    • 0032481380 scopus 로고    scopus 로고
    • The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P., Ruddock L.W., Darby N.J., Freedman R.B. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 17:1998;927-935.
    • (1998) EMBO J. , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 20
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
    • Darby N.J., Penka E., Vincentelli R. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J. Mol. Biol. 276:1998;239-247.
    • (1998) J. Mol. Biol. , vol.276 , pp. 239-247
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 23
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • Quan H., Fan G.B., Wang C.C. Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J. Biol. Chem. 270:1995;17078-17080.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.B.2    Wang, C.C.3
  • 24
    • 0020787176 scopus 로고
    • Kinetics and specificity of homogeneous protein disulfide-isomerase in protein disulfide isomerization and in thiol-protein-disulfide oxidoreduction
    • Lambert N., Freedman R.B. Kinetics and specificity of homogeneous protein disulfide-isomerase in protein disulfide isomerization and in thiol-protein-disulfide oxidoreduction. Biochem. J. 213:1983;225-234.
    • (1983) Biochem. J. , vol.213 , pp. 225-234
    • Lambert, N.1    Freedman, R.B.2
  • 25
    • 0025230522 scopus 로고
    • Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride
    • Liang S.J., Lin Y.Z., Zhou J.M., Tsou C.L., Wu P., Zhou Z. Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride. Biochim. Biophys. Acta. 1038:1990;240-246.
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 240-246
    • Liang, S.J.1    Lin, Y.Z.2    Zhou, J.M.3    Tsou, C.L.4    Wu, P.5    Zhou, Z.6
  • 26
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0031570355 scopus 로고    scopus 로고
    • Di-fluoresceinthiocarbamyl-insulin: A fluorescent substrate for the assay of protein disulfide oxidoreductase activity
    • Heuck A.P., Wolosiuk R.A. Di-fluoresceinthiocarbamyl-insulin: A fluorescent substrate for the assay of protein disulfide oxidoreductase activity. Anal. Biochem. 248:1997;94-101.
    • (1997) Anal. Biochem. , vol.248 , pp. 94-101
    • Heuck, A.P.1    Wolosiuk, R.A.2
  • 30
    • 0029819346 scopus 로고    scopus 로고
    • Identifying and characterizing a structural domain of protein disulfide isomerase
    • Darby N.J., Kemmink J., Creighton T.E. Identifying and characterizing a structural domain of protein disulfide isomerase. Biochemistry. 35:1996;10517-10528.
    • (1996) Biochemistry , vol.35 , pp. 10517-10528
    • Darby, N.J.1    Kemmink, J.2    Creighton, T.E.3
  • 32
    • 0033028924 scopus 로고    scopus 로고
    • Identifying and characterizing a second structural domain of protein disulfide isomerase
    • Darby N.J., Straaten M.V., Penka E., Vincentelli R., Kemmink J. Identifying and characterizing a second structural domain of protein disulfide isomerase. FEBS Lett. 448:1999;167-172.
    • (1999) FEBS Lett. , vol.448 , pp. 167-172
    • Darby, N.J.1    Straaten, M.V.2    Penka, E.3    Vincentelli, R.4    Kemmink, J.5
  • 33
    • 0031954077 scopus 로고    scopus 로고
    • Experimental and theoretical analysis of the domain architecture of mammalian protein disulfide-isomerase
    • Freedman R.B., Gane P.J., Hawkins H.C., Hlodan R., Mclaughlin S.H., Parry J.W.L. Experimental and theoretical analysis of the domain architecture of mammalian protein disulfide-isomerase. Biol. Chem. 379:1998;321-328.
    • (1998) Biol. Chem. , vol.379 , pp. 321-328
    • Freedman, R.B.1    Gane, P.J.2    Hawkins, H.C.3    Hlodan, R.4    Mclaughlin, S.H.5    Parry, J.W.L.6
  • 34
    • 0029093531 scopus 로고
    • Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
    • Darby N.J., Creighton T.E. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry. 34:1995;11725-11735.
    • (1995) Biochemistry , vol.34 , pp. 11725-11735
    • Darby, N.J.1    Creighton, T.E.2
  • 35
    • 0025331418 scopus 로고
    • Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • Lundström J., Holmgren A. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J. Biol. Chem. 265:1990;9114-9120.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9114-9120
    • Lundström, J.1    Holmgren, A.2
  • 36
    • 0030866362 scopus 로고    scopus 로고
    • Fluoresceinthiocarbamyl-insulin: A potential analytical tool for the assay of disulfide bond reduction
    • Heuck A.P., Wolosiuk R.A. Fluoresceinthiocarbamyl-insulin: A potential analytical tool for the assay of disulfide bond reduction. J. Biochem. Biophys. Methods. 34:1997;213-225.
    • (1997) J. Biochem. Biophys. Methods , vol.34 , pp. 213-225
    • Heuck, A.P.1    Wolosiuk, R.A.2
  • 37
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich M., Glockshuber R. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Folding Design. 3:1998;161-171.
    • (1998) Folding Design , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 38
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thioldisulfide interchange reactions involving oxidized glutathione
    • Szajewski R.P., Whitesides G.M. Rate constants and equilibrium constants for thioldisulfide interchange reactions involving oxidized glutathione. J. Am. Chem. Soc. 102:1980;2011-2026.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whitesides, G.M.2
  • 40
    • 0026778032 scopus 로고
    • Hsp90 chaperones protein folding in vitro
    • Wiech H., Buchner J., Zimmermann R., Jakob U. Hsp90 chaperones protein folding in vitro. Nature. 358:1992;169-170.
    • (1992) Nature , vol.358 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 41
    • 0028242359 scopus 로고
    • The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of PDI
    • Puig A., Lyles M.M., Noiva R., Gilbert H.F. The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of PDI. J. Biol. Chem. 269:1994;19128-19135.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19128-19135
    • Puig, A.1    Lyles, M.M.2    Noiva, R.3    Gilbert, H.F.4


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