메뉴 건너뛰기




Volumn 401, Issue 1, 2007, Pages 287-297

Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions

Author keywords

Arabidopsis thaliana; Chloroplast; Cyclophilin; Immunophilin; Peptidyl prolyl cis trans isomerase (PPI); Peroxiredoxin

Indexed keywords

ARABIDOPSIS THALIANA; CHLOROPLASTS; CYCLOPHILIN; IMMUNOPHILIN; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (PPI); PEROXIREDOXIN;

EID: 33846295570     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061092     Document Type: Article
Times cited : (79)

References (47)
  • 1
    • 1942501867 scopus 로고    scopus 로고
    • Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis
    • He, Z., Li, L. and Luan, S. (2004) Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis. Plant Physiol. 134, 1248-1267
    • (2004) Plant Physiol , vol.134 , pp. 1248-1267
    • He, Z.1    Li, L.2    Luan, S.3
  • 2
    • 20044395966 scopus 로고    scopus 로고
    • Redox regulation in the chloroplast thylakoid lumen: A new frontier in photosynthesis research
    • Buchanan, B. B. and Luan, S. (2005) Redox regulation in the chloroplast thylakoid lumen: a new frontier in photosynthesis research. J. Exp. Bot. 56, 1439-1447
    • (2005) J. Exp. Bot , vol.56 , pp. 1439-1447
    • Buchanan, B.B.1    Luan, S.2
  • 3
    • 1942501872 scopus 로고    scopus 로고
    • The Arabidopsis cyclophilin gene family
    • Romano, P. G. N., Horton, P. and Gray, J. E. (2004) The Arabidopsis cyclophilin gene family. Plant Physiol. 134, 1268-1282
    • (2004) Plant Physiol , vol.134 , pp. 1268-1282
    • Romano, P.G.N.1    Horton, P.2    Gray, J.E.3
  • 4
    • 0021159379 scopus 로고
    • Cyclophilin: A specific cytosolic binding protein for cyclosporin A
    • Handschumacher, R. E., Harding, M. W., Rice, J. and Drugge, R. J. (1984) Cyclophilin: a specific cytosolic binding protein for cyclosporin A. Science 226, 544-547
    • (1984) Science , vol.226 , pp. 544-547
    • Handschumacher, R.E.1    Harding, M.W.2    Rice, J.3    Drugge, R.J.4
  • 5
    • 19344375177 scopus 로고    scopus 로고
    • Plant immunophilins: Functional versatility beyond protein maturation
    • Romano, P. G. N., Gray, J., Horton, P. and Luan, S. (2005) Plant immunophilins: functional versatility beyond protein maturation. New Phytol. 166, 753-769
    • (2005) New Phytol , vol.166 , pp. 753-769
    • Romano, P.G.N.1    Gray, J.2    Horton, P.3    Luan, S.4
  • 6
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
    • Bächinger, H. P. (1987) The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem. 262, 17144-17148
    • (1987) J. Biol. Chem , vol.262 , pp. 17144-17148
    • Bächinger, H.P.1
  • 7
    • 0024339276 scopus 로고
    • Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix
    • Davis, J. M., Boswell, B. A. and Bächinger, H. P. (1989) Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix J. Biol. Chem. 264, 8956-8962
    • (1989) J. Biol. Chem , vol.264 , pp. 8956-8962
    • Davis, J.M.1    Boswell, B.A.2    Bächinger, H.P.3
  • 8
    • 0026510141 scopus 로고
    • Peptidyl-prolyl cis-trans isomerases improve the efficiency of protein disulfide isomerase as a catalyst of protein folding
    • Schönbrunner, E. R. and Schmid, F. X. (1992) Peptidyl-prolyl cis-trans isomerases improve the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proc. Natl. Acad. Sci. U.S.A. 89, 4510-4513
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 4510-4513
    • Schönbrunner, E.R.1    Schmid, F.X.2
  • 10
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgard, P. O., Bergenhem, N., Johnsson, B. H., Svensson, M. and Carlsson, U. (1992) Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 258, 466-468
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgard, P.O.1    Bergenhem, N.2    Johnsson, B.H.3    Svensson, M.4    Carlsson, U.5
  • 11
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the Cyp-40 and the steroid aporeceptor associated protein p23
    • Freeman, B. C., Toft, D. O. and Morimoto, R. I. (1996) Molecular chaperone machines: chaperone activities of the Cyp-40 and the steroid aporeceptor associated protein p23. Science 274, 1718-1720
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 12
    • 0030778411 scopus 로고    scopus 로고
    • The dodo gene family encodes a novel protein involved in signal transduction and protein folding
    • Maleszka, R., Lupas, A., Hanes, S. D. and Miklos, G. L. (1997) The dodo gene family encodes a novel protein involved in signal transduction and protein folding. Gene 203, 89-93
    • (1997) Gene , vol.203 , pp. 89-93
    • Maleszka, R.1    Lupas, A.2    Hanes, S.D.3    Miklos, G.L.4
  • 13
    • 0037133154 scopus 로고    scopus 로고
    • Regulation of the tyrosine kinase ltk by the peptidyl-prolyl isomerase cyclophilin A
    • Brazin, K. N., Mallis, R. J., Fulton, D. B. and Andreotti, A. H. (2001) Regulation of the tyrosine kinase ltk by the peptidyl-prolyl isomerase cyclophilin A. Proc. Natl. Acad. Sci. U.S.A. 99, 1899-1904
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 1899-1904
    • Brazin, K.N.1    Mallis, R.J.2    Fulton, D.B.3    Andreotti, A.H.4
  • 15
    • 0028445305 scopus 로고
    • pCyP B: A chloroplast-localized, heat shock-responsive cyclophilin from fava bean
    • Luan S., Lane W. S. and Schreiber, S.L. (1994) pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from fava bean. Plant Cell 6, 885-692
    • (1994) Plant Cell , vol.6 , pp. 885-692
    • Luan, S.1    Lane, W.S.2    Schreiber, S.L.3
  • 16
    • 0031857049 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA corresponding to a stress-activated cyclophilin gene in Solanum commersonii
    • Meza-Zepeda, L. A., Baudo, M. M., Palva, E. T. and Heino, P. (1998) Isolation and characterization of a cDNA corresponding to a stress-activated cyclophilin gene in Solanum commersonii. J. Exp. Bot. 49, 1451-1452
    • (1998) J. Exp. Bot , vol.49 , pp. 1451-1452
    • Meza-Zepeda, L.A.1    Baudo, M.M.2    Palva, E.T.3    Heino, P.4
  • 17
    • 0035937462 scopus 로고    scopus 로고
    • Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40
    • Berardini, T. Z., Bollmann, K., Sun, H. and Poethig, R. S. (2001) Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40. Science 291, 2405-2407
    • (2001) Science , vol.291 , pp. 2405-2407
    • Berardini, T.Z.1    Bollmann, K.2    Sun, H.3    Poethig, R.S.4
  • 18
    • 0036470544 scopus 로고    scopus 로고
    • A cyclophilin function in pre-mRNA splicing
    • Horowitz, D. S., Lee, E. J., Mabon, S. A. and Misteli, T. (2002) A cyclophilin function in pre-mRNA splicing. EMBO J. 21, 470-480
    • (2002) EMBO J , vol.21 , pp. 470-480
    • Horowitz, D.S.1    Lee, E.J.2    Mabon, S.A.3    Misteli, T.4
  • 20
    • 0035839494 scopus 로고    scopus 로고
    • Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity
    • Lee, S. P., Hwang, Y. S., Kim, Y. J., Kwon, K.-S., Kim, H. J., Kim, K. and Chae, H. Z. (2001) Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity. J. Biol. Chem. 276, 29826-29832
    • (2001) J. Biol. Chem , vol.276 , pp. 29826-29832
    • Lee, S.P.1    Hwang, Y.S.2    Kim, Y.J.3    Kwon, K.-S.4    Kim, H.J.5    Kim, K.6    Chae, H.Z.7
  • 21
    • 5144228043 scopus 로고    scopus 로고
    • Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum
    • Bernier-Villamor, L., Navarro, E., Sevilla, F. and Lázaro, J.-J. (2004) Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum. J. Exp. Bot. 55, 2191-2199
    • (2004) J. Exp. Bot , vol.55 , pp. 2191-2199
    • Bernier-Villamor, L.1    Navarro, E.2    Sevilla, F.3    Lázaro, J.-J.4
  • 22
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis
    • Horling, F., Lamkemeyer, P., König, J., Finkemeier, I., Kandlbinder, A., Baier, M. and Dietz, K.-J. (2003) Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiol. 131, 317-325
    • (2003) Plant Physiol , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    König, J.3    Finkemeier, I.4    Kandlbinder, A.5    Baier, M.6    Dietz, K.-J.7
  • 24
    • 0042591328 scopus 로고    scopus 로고
    • Reaction mechanism of plant 2-Cys peroxiredoxin: Role of the C-terminus and the quaternary structure
    • König, J., Lotte, K., Plessow, R., Brockhinke, A., Baier, M. and Dietz, K.-J. (2003) Reaction mechanism of plant 2-Cys peroxiredoxin: role of the C-terminus and the quaternary structure. J. Biol. Chem. 278, 24409-24420
    • (2003) J. Biol. Chem , vol.278 , pp. 24409-24420
    • König, J.1    Lotte, K.2    Plessow, R.3    Brockhinke, A.4    Baier, M.5    Dietz, K.-J.6
  • 25
    • 0142057021 scopus 로고    scopus 로고
    • Plant peroxiredoxins
    • Dietz, K.-J. (2003) Plant peroxiredoxins. Annu. Rev. Plant Biol. 54, 93-107
    • (2003) Annu. Rev. Plant Biol , vol.54 , pp. 93-107
    • Dietz, K.-J.1
  • 27
    • 16844368306 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
    • Finkemeier, I., Goodman, M., Lamkemeyer, P., Kandlbinder, A., Sweetlove, L. J. and Dietz, K.-J. (2005) The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem. 280, 12168-12180
    • (2005) J. Biol. Chem , vol.280 , pp. 12168-12180
    • Finkemeier, I.1    Goodman, M.2    Lamkemeyer, P.3    Kandlbinder, A.4    Sweetlove, L.J.5    Dietz, K.-J.6
  • 28
    • 0028363956 scopus 로고
    • Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana
    • Lippuner, V., Chou, I. T., Scott, S. V., Ettinger, W. F., Theg, S. M. and Gasser, C. S. (1994) Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana. J. Biol. Chem. 269, 7863-7868
    • (1994) J. Biol. Chem , vol.269 , pp. 7863-7868
    • Lippuner, V.1    Chou, I.T.2    Scott, S.V.3    Ettinger, W.F.4    Theg, S.M.5    Gasser, C.S.6
  • 32
    • 0033200161 scopus 로고    scopus 로고
    • Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata
    • Montemartini, M., Kalisz, H. M., Hecht, H. J., Steinert, P. and Flohe, L. (1999) Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata. Eur. J. Biochem. 264, 516-524
    • (1999) Eur. J. Biochem , vol.264 , pp. 516-524
    • Montemartini, M.1    Kalisz, H.M.2    Hecht, H.J.3    Steinert, P.4    Flohe, L.5
  • 33
    • 0037117488 scopus 로고    scopus 로고
    • The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierachy of photosynthetic electron flux
    • König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schürmann, P. and Dietz, K.-J. (2002) The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierachy of photosynthetic electron flux. Proc. Natl. Acad. Sci. U.S.A. 99, 5738-5743
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 5738-5743
    • König, J.1    Baier, M.2    Horling, F.3    Kahmann, U.4    Harris, G.5    Schürmann, P.6    Dietz, K.-J.7
  • 36
    • 0021689983 scopus 로고
    • Conformational specificity of chymotrypsin toward proline-containing substrates
    • Fischer, G., Bang, H., Berger, E. and Schellenberger, A. (1984) Conformational specificity of chymotrypsin toward proline-containing substrates. Biochim. Biophys. Acta 791, 87-97
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 87-97
    • Fischer, G.1    Bang, H.2    Berger, E.3    Schellenberger, A.4
  • 37
    • 0025216877 scopus 로고
    • Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis
    • Liu, J., Albers, M. W., Chen, C.-M., Schreiber, S. L. and Walsh, C. T. (1990) Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 87, 2304-2308
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 2304-2308
    • Liu, J.1    Albers, M.W.2    Chen, C.-M.3    Schreiber, S.L.4    Walsh, C.T.5
  • 38
    • 0040799938 scopus 로고    scopus 로고
    • Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin: Thioredoxin reductase, and thioredoxin f-regulated enzymes
    • Hirasawa, M., Schürmann, P., Jacquot, J.-P., Manieri, W., Jacquot, P., Keryer, E., Hartman, F. C. and Knaff, D. B. (1999) Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin: thioredoxin reductase, and thioredoxin f-regulated enzymes. Biochemistry 38, 5200-5205
    • (1999) Biochemistry , vol.38 , pp. 5200-5205
    • Hirasawa, M.1    Schürmann, P.2    Jacquot, J.-P.3    Manieri, W.4    Jacquot, P.5    Keryer, E.6    Hartman, F.C.7    Knaff, D.B.8
  • 39
    • 70449159833 scopus 로고
    • Ultraviolet fluorescence of the aromatic amino acids
    • Teale, F. W. J. and Weber, G. (1957) Ultraviolet fluorescence of the aromatic amino acids. Biochem. J. 65, 476-482
    • (1957) Biochem. J , vol.65 , pp. 476-482
    • Teale, F.W.J.1    Weber, G.2
  • 40
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E. A., Vedenkins, N. S. and Ivkova, M. N. (1973) Fluorescence and the location of tryptophan residues in protein molecules. Pnotochem. Photobiol. 18, 263-279
    • (1973) Pnotochem. Photobiol , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkins, N.S.2    Ivkova, M.N.3
  • 41
    • 0036001082 scopus 로고    scopus 로고
    • The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation
    • Dietz, K.-J., Horling, F., König, J. and Baier, M. (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. J. Exp. Bot. 53, 1321-1329
    • (2002) J. Exp. Bot , vol.53 , pp. 1321-1329
    • Dietz, K.-J.1    Horling, F.2    König, J.3    Baier, M.4
  • 42
    • 0033521117 scopus 로고    scopus 로고
    • Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans
    • Dornan, J., Page, A. P., Taylor, P., Wu, S.-Y., Winter, A. D., Husi, H. and Walkinshaw, M. D. (1999) Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans. J. Biol. Chem. 274, 34877-34883
    • (1999) J. Biol. Chem , vol.274 , pp. 34877-34883
    • Dornan, J.1    Page, A.P.2    Taylor, P.3    Wu, S.-Y.4    Winter, A.D.5    Husi, H.6    Walkinshaw, M.D.7
  • 43
    • 20044391221 scopus 로고    scopus 로고
    • Thioredoxin affinity chromatography: A useful method for further understanding the thioredoxin network
    • Hisabori, T., Hara, S., Fujii, T., Yamazaki, D., Hosoya-Matsuda, N. and Motohashi, K. (2005) Thioredoxin affinity chromatography: a useful method for further understanding the thioredoxin network. J. Exp. Bot. 56, 1463-1468
    • (2005) J. Exp. Bot , vol.56 , pp. 1463-1468
    • Hisabori, T.1    Hara, S.2    Fujii, T.3    Yamazaki, D.4    Hosoya-Matsuda, N.5    Motohashi, K.6
  • 45
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin- cyclosporin A and FKBP-FK506 complexes
    • Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I. and Schreiber, S. L. (1991) Calcineurin is a common target of cyclophilin- cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 46
    • 0027192328 scopus 로고
    • Specific interaction of the cyclophilin-cyclosporin complex with the B subunit of calcineurin
    • Li, W. and Handschumacher, R. E. (1993) Specific interaction of the cyclophilin-cyclosporin complex with the B subunit of calcineurin. J. Biol. Chem. 268, 14040-14044
    • (1993) J. Biol. Chem , vol.268 , pp. 14040-14044
    • Li, W.1    Handschumacher, R.E.2
  • 47
    • 0345306681 scopus 로고    scopus 로고
    • Redox regulation, redox signalling and redox homeostasis in plant cells
    • Dietz, K. J. (2003) Redox regulation, redox signalling and redox homeostasis in plant cells. Intern. Rev. Cytol. 228, 141-193
    • (2003) Intern. Rev. Cytol , vol.228 , pp. 141-193
    • Dietz, K.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.