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Volumn 139, Issue 2, 1998, Pages 149-158

Studies on the expression of the wheat prolyl isomerase FKBP73 during plant development

Author keywords

FK506 binding protein; Prolyl isomerase; Wheat

Indexed keywords

FK 506 BINDING PROTEIN; ISOMERASE;

EID: 0032585537     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(98)00168-X     Document Type: Article
Times cited : (14)

References (41)
  • 2
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding M.W., Galat A., Uehling D.E., Schreiber S.L. A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature. 341:1989;758-760.
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 5
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
    • Kallen J., Spitzfaden C., Zurini M.G. et al. Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature. 353:1991;276-279.
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1    Spitzfaden, C.2    Zurini, M.G.3
  • 7
    • 0028276439 scopus 로고
    • Immunophilins in protein folding and immunosuppression
    • Fruman D.A., Burakoff S.J., Bierer B.E. Immunophilins in protein folding and immunosuppression. FASEB J. 8:1994;391-400.
    • (1994) FASEB J. , vol.8 , pp. 391-400
    • Fruman, D.A.1    Burakoff, S.J.2    Bierer, B.E.3
  • 8
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman B.C., Toft D.O., Morimoto R.I. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science. 274:1996;1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 9
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of HSP90-associated proteins
    • Bose S., Weikl T., Bugl H., Buchner J. Chaperone function of HSP90-associated proteins. Science. 274:1996;1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 10
    • 0031615108 scopus 로고    scopus 로고
    • Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism
    • Leverson J.D., Ness S.A. Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism. Mol. Cell. 1:1998;203-211.
    • (1998) Mol. Cell , vol.1 , pp. 203-211
    • Leverson, J.D.1    Ness, S.A.2
  • 11
    • 0032559238 scopus 로고    scopus 로고
    • Prolyl isomerases and nuclear function
    • Hunter T. Prolyl isomerases and nuclear function. Cell. 92:1998;141-143.
    • (1998) Cell , vol.92 , pp. 141-143
    • Hunter, T.1
  • 12
    • 0025599920 scopus 로고
    • Structure and expression of cytosolic cyclophilin/peptidyl-prolyl-cis-trans Isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli
    • Gasser C.S., Gunning D.A., Budelier K.A., Brown S.M. Structure and expression of cytosolic cyclophilin/peptidyl-prolyl-cis-trans Isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli. Proc. Natl. Acad. Sci. 87:1990;9519-9523.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 9519-9523
    • Gasser, C.S.1    Gunning, D.A.2    Budelier, K.A.3    Brown, S.M.4
  • 13
    • 0026799384 scopus 로고
    • Plant organelles contain distinct peptidyl-prolyl-cis-trans isomerases
    • Breiman A., Fawcett T.W., Ghirardi M.L., Mattoo A.K. Plant organelles contain distinct peptidyl-prolyl-cis-trans isomerases. J. Biol. Chem. 267:1992;21293-21296.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21293-21296
    • Breiman, A.1    Fawcett, T.W.2    Ghirardi, M.L.3    Mattoo, A.K.4
  • 14
    • 0028445305 scopus 로고
    • PCyP B: A chloroplast-localized, heat shock-responsive cyclophilin from Fava Bean
    • Luan S., Lane W.S., Schreiber S.L. pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from Fava Bean. Plant Cell. 6:1994;885-892.
    • (1994) Plant Cell , vol.6 , pp. 885-892
    • Luan, S.1    Lane, W.S.2    Schreiber, S.L.3
  • 16
    • 0029937302 scopus 로고    scopus 로고
    • Molecular characterization of a FKBP-type immunophilin from higher plants
    • Luan S., Kudla J., Gruissem W., Schreiber S.L. Molecular characterization of a FKBP-type immunophilin from higher plants. Proc. Natl. Acad. Sci. USA. 93:1996;6964-6969.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6964-6969
    • Luan, S.1    Kudla, J.2    Gruissem, W.3    Schreiber, S.L.4
  • 17
    • 0000362850 scopus 로고
    • Effects of abiotic stresses on cyclophilin gene expression in maize and bean and sequence analysis of bean cyclophilin cDNA
    • Marivet J., Fredo P., Bukard G. Effects of abiotic stresses on cyclophilin gene expression in maize and bean and sequence analysis of bean cyclophilin cDNA. Plant Sci. 84:1992;171-178.
    • (1992) Plant Sci. , vol.84 , pp. 171-178
    • Marivet, J.1    Fredo, P.2    Bukard, G.3
  • 18
    • 0028534732 scopus 로고
    • Bean cyclophilin gene expression during plant development and stress conditions
    • Marivet J., Margis-Pinheiro M., Frendo P., Burkard G. Bean cyclophilin gene expression during plant development and stress conditions. Plant Mol. Biol. 26:1994;1181-1189.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1181-1189
    • Marivet, J.1    Margis-Pinheiro, M.2    Frendo, P.3    Burkard, G.4
  • 19
    • 0028951175 scopus 로고
    • DNA sequence analysis of a cyclophilin gene from maize: Developmental expression and regulation by salicylic acid
    • Marivet J., Frendo P., Burkard G. DNA sequence analysis of a cyclophilin gene from maize: developmental expression and regulation by salicylic acid. Mol. Gen. Genet. 247:1995;222-228.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 222-228
    • Marivet, J.1    Frendo, P.2    Burkard, G.3
  • 21
    • 0030292782 scopus 로고    scopus 로고
    • A novel wheat peptidyl-prolyl-cis-trans isomerase: CDNA isolation, structure, enzymatic activity, and expression
    • Blecher O., Erel N., Callebaut I., Aviezer K., Breiman A. A novel wheat peptidyl-prolyl-cis-trans isomerase: cDNA isolation, structure, enzymatic activity, and expression. Plant Mol. Biol. 32:1996;493-504.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 493-504
    • Blecher, O.1    Erel, N.2    Callebaut, I.3    Aviezer, K.4    Breiman, A.5
  • 22
    • 0029958048 scopus 로고    scopus 로고
    • Novel structure of a high molecular weight FK506 binding protein from Arabidopsis thaliana
    • Vucich V.A., Gasser C.S. Novel structure of a high molecular weight FK506 binding protein from Arabidopsis thaliana. Mol. Gen. Genet. 252:1996;510-517.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 510-517
    • Vucich, V.A.1    Gasser, C.S.2
  • 23
    • 0031456116 scopus 로고    scopus 로고
    • Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins
    • Chou I.T., Gasser C.S. Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins. Plant Mol. Biol. 35:1997;873-892.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 873-892
    • Chou, I.T.1    Gasser, C.S.2
  • 24
    • 0013501043 scopus 로고    scopus 로고
    • A novel heat stress induced peptidyl-prolyl-cis-trans isomerase belonging to the FK506 binding protein (FKBP) family in wheat
    • in press.
    • I. Kurek, K. Aviezer, E. Herman, N. Erel, O. Blecher, A. Breiman, A novel heat stress induced peptidyl-prolyl-cis-trans isomerase belonging to the FK506 binding protein (FKBP) family in wheat, Plant Physiol (1998) in press.
    • (1998) Plant Physiol
    • Kurek, I.1    Aviezer, K.2    Herman, E.3    Erel, N.4    Blecher, O.5    Breiman, A.6
  • 25
    • 0031945523 scopus 로고    scopus 로고
    • Mutation in the Arabidopsis pasticcino 1 gene, a new FKBP-like protein, has a dramatic effect on plant development
    • Vittorioso P., Cowing R., Faure J.D., Caboche M., Bellini C. Mutation in the Arabidopsis pasticcino 1 gene, a new FKBP-like protein, has a dramatic effect on plant development. Mol. Cell Biol. 18:1998;3034-3043.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3034-3043
    • Vittorioso, P.1    Cowing, R.2    Faure, J.D.3    Caboche, M.4    Bellini, C.5
  • 26
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W.B., Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18:1997;306-360.
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 27
    • 0029856744 scopus 로고    scopus 로고
    • Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants
    • J.K. Owens-Grillo, L.F. Stancato, K. Hoffmann, W.B. Pratt, P. Krishna, Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants, Biochemistry (1996) 15249-15255.
    • (1996) Biochemistry , pp. 15249-15255
    • Owens-Grillo, J.K.1    Stancato, L.F.2    Hoffmann, K.3    Pratt, W.B.4    Krishna, P.5
  • 28
    • 0013535288 scopus 로고    scopus 로고
    • High molecular weight FKBPs are components of HSP90 heterocomplexes in wheat germ lysate
    • in press.
    • R.K. Reddy, I. Kurek, A.M. Silverstein, A. Breiman, P. Krishna, High molecular weight FKBPs are components of HSP90 heterocomplexes in wheat germ lysate, Plant Physiol. (1998) in press.
    • (1998) Plant Physiol.
    • Reddy, R.K.1    Kurek, I.2    Silverstein, A.M.3    Breiman, A.4    Krishna, P.5
  • 29
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassay with tobacco tissue cultures
    • Murashige T., Skoog F. A revised medium for rapid growth and bioassay with tobacco tissue cultures. Plant Physiol. 15:1962;473-497.
    • (1962) Plant Physiol. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the 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
  • 33
  • 34
    • 0025234334 scopus 로고
    • Protein analysis using high-resolution two-dimensional polyacrylamide gel electrophoresis
    • Dunbar B.S., Kimura H., Timmons T.M. Protein analysis using high-resolution two-dimensional polyacrylamide gel electrophoresis. Methods Enzymol. 182:1990;441-459.
    • (1990) Methods Enzymol. , vol.182 , pp. 441-459
    • Dunbar, B.S.1    Kimura, H.2    Timmons, T.M.3
  • 35
    • 0024638573 scopus 로고
    • Temporally modular gene expression during cotyledon development
    • Hughes D.W., Galau G.U. Temporally modular gene expression during cotyledon development. Genes Devel. 3:1989;358-369.
    • (1989) Genes Devel. , vol.3 , pp. 358-369
    • Hughes, D.W.1    Galau, G.U.2
  • 36
    • 0026810741 scopus 로고
    • Developmental and organ-specific expression of an ABA-and stress-induced protein in barley
    • Hong B., Barg R., Ho T.D. Developmental and organ-specific expression of an ABA-and stress-induced protein in barley. Plant Mol. Biol. 18:1992;663-674.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 663-674
    • Hong, B.1    Barg, R.2    Ho, T.D.3
  • 37
    • 0027947292 scopus 로고
    • Developmental control of small heat shock protein expression during pea seed maturation
    • DeRocher A.E., Vierling E. Developmental control of small heat shock protein expression during pea seed maturation. Plant J. 5:1994;93-102.
    • (1994) Plant J. , vol.5 , pp. 93-102
    • DeRocher, A.E.1    Vierling, E.2
  • 38
    • 0031591585 scopus 로고    scopus 로고
    • Distribution patterns of HSP90 protein in rice
    • Pareek A., Singla S.L., Kush A.K., Grover A. Distribution patterns of HSP90 protein in rice. Plant Sci. 125:1997;221-230.
    • (1997) Plant Sci. , vol.125 , pp. 221-230
    • Pareek, A.1    Singla, S.L.2    Kush, A.K.3    Grover, A.4
  • 39
    • 0031081435 scopus 로고    scopus 로고
    • Analysis of the native forms of the 90 kDa heat shock protein (hsp90) in plant cytosolic extract
    • Krishna P., Reddy R.K., Sacco M., Frappier J.R., Felsheim R.F. Analysis of the native forms of the 90 kDa heat shock protein (hsp90) in plant cytosolic extract. Plant Mol. Biol. 33:1997;457-466.
    • (1997) Plant Mol. Biol. , vol.33 , pp. 457-466
    • Krishna, P.1    Reddy, R.K.2    Sacco, M.3    Frappier, J.R.4    Felsheim, R.F.5
  • 40
    • 0025290187 scopus 로고
    • The 56-59 kDa protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70 and 90 kDa heat shock proteins
    • Sanchez E.R., Faber L.E., Henzel W.J., Pratt W.B. The 56-59 kDa protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70 and 90 kDa heat shock proteins. Biochemistry. 29:1990;5145-5152.
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Faber, L.E.2    Henzel, W.J.3    Pratt, W.B.4
  • 41
    • 0001272136 scopus 로고
    • Chromosomal rearrangements in the rye genome relative to that of wheat
    • Devos K.M., Atkinson M.D., Chinoy C.N. et al. Chromosomal rearrangements in the rye genome relative to that of wheat. Theor. Appl. Genet. 85:1993;673-680.
    • (1993) Theor. Appl. Genet. , vol.85 , pp. 673-680
    • Devos, K.M.1    Atkinson, M.D.2    Chinoy, C.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.