메뉴 건너뛰기




Volumn 222, Issue 2, 1998, Pages 249-255

FKBP-type peptidyl-prolyl cis-trans isomerase from a sulfur-dependent hyperthermophilic archaeon, Thermococcus sp. KS-1

Author keywords

FKBP; Gene cloning; Hyperthermophilic archaeon; Peptidyl prolyl cis trans isomerase

Indexed keywords

CYCLOPHILIN; CYCLOSPORIN A; DNA; FK 506 BINDING PROTEIN; IMMUNOSUPPRESSIVE AGENT; RECOMBINANT ENZYME; TACROLIMUS;

EID: 0032548180     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00484-3     Document Type: Article
Times cited : (18)

References (28)
  • 1
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult C.J.et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science. 273:1996;1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 2
    • 0028789790 scopus 로고
    • Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family
    • Callebaut I., Mornon J.-P. Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family. FEBS Lett. 371:1995;211-215.
    • (1995) FEBS Lett. , vol.371 , pp. 211-215
    • Callebaut, I.1    Mornon, J.-P.2
  • 3
    • 0028050923 scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and their effectors
    • Fischer G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33:1994;1415-1436.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 4
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer G., Wittmann-Liebold B., Lang K., Kiefhaber T., Schmid F.X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature. 337:1989;476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 5
    • 0031936258 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of an FK506-sensitive peptidyl prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus thermolithotrophicus
    • Furutani M., Iida T., Yamano S., Kamino K., Maruyama T. Biochemical and genetic characterization of an FK506-sensitive peptidyl prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus thermolithotrophicus. J. Bacteriol. 180:1998;388-394.
    • (1998) J. Bacteriol. , vol.180 , pp. 388-394
    • Furutani, M.1    Iida, T.2    Yamano, S.3    Kamino, K.4    Maruyama, T.5
  • 7
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK-506 is a cis-trans peptidyl-prolyl isomerase
    • Harding M.W., Galat A., Uehling D.E., Schreiber S.L. A receptor for the immunosuppressant FK-506 is a cis-trans peptidyl-prolyl isomerase. Nature. 341:1989;761-763.
    • (1989) Nature , vol.341 , pp. 761-763
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 8
    • 0025373627 scopus 로고
    • Substrate specifities of the peptidyl cis-trans isomerase activities of cyclophilin and FK506 binding protein: Evidence for the existence of a family of distinct enzymes
    • Harrison R.K., Stein R.L. Substrate specifities of the peptidyl cis-trans isomerase activities of cyclophilin and FK506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry. 29:1990;3813-3816.
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 9
    • 0028142311 scopus 로고
    • Growth requirements of hyperthermophilic sulfur-dependent heterotrophic archaea isolated from a shallow submarine geothermal system with reference to their essential amino acids
    • Hoaki T., Nishijima M., Kato M., Adachi K., Mizobuchi S., Hanzawa N., Maruyama T. Growth requirements of hyperthermophilic sulfur-dependent heterotrophic archaea isolated from a shallow submarine geothermal system with reference to their essential amino acids. Appl. Environ. Microbiol. 60:1994;2898-2904.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2898-2904
    • Hoaki, T.1    Nishijima, M.2    Kato, M.3    Adachi, K.4    Mizobuchi, S.5    Hanzawa, N.6    Maruyama, T.7
  • 10
    • 0030916764 scopus 로고    scopus 로고
    • The Escherichia coli slyD is a metal ion-regulated peptidyl-prolyl cis/trans isomerase
    • Hottenrott S., Schumann T., Plückthum A., Fischer G., Rahfeld J.-U. The Escherichia coli slyD is a metal ion-regulated peptidyl-prolyl cis/trans isomerase. J. Biol. Chem. 272:1997;15697-15701.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15697-15701
    • Hottenrott, S.1    Schumann, T.2    Plückthum, A.3    Fischer, G.4    Rahfeld, J.-U.5
  • 11
    • 0031578733 scopus 로고    scopus 로고
    • Gene for a cyclophilin-type peptidyl-prolyl cis-trans isomerase from a halophilic archaeum, Halobacterium cutirubrum
    • Iida T., Furutani M., Iwabuchi T., Maruyama T. Gene for a cyclophilin-type peptidyl-prolyl cis-trans isomerase from a halophilic archaeum, Halobacterium cutirubrum. Gene. 204:1997;139-144.
    • (1997) Gene , vol.204 , pp. 139-144
    • Iida, T.1    Furutani, M.2    Iwabuchi, T.3    Maruyama, T.4
  • 12
    • 0025009936 scopus 로고
    • Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes
    • Isaki L., Beers R., Wu H.C. Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes. J. Bacteriol. 172:1990;6512-6517.
    • (1990) J. Bacteriol. , vol.172 , pp. 6512-6517
    • Isaki, L.1    Beers, R.2    Wu, H.C.3
  • 13
    • 0032579989 scopus 로고    scopus 로고
    • Complete sequence and gene organization of the genome of a hyperthermophilic archaebacterium, Pyrococcus horikoshii OT3
    • Kawarabayashi Y.et al. Complete sequence and gene organization of the genome of a hyperthermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 5:1998;55-76.
    • (1998) DNA Res. , vol.5 , pp. 55-76
    • Kawarabayashi, Y.1
  • 14
    • 0029867394 scopus 로고    scopus 로고
    • Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases
    • Kay J.E. Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases. Biochem. J. 314:1996;361-385.
    • (1996) Biochem. J. , vol.314 , pp. 361-385
    • Kay, J.E.1
  • 15
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon, Archaeoglobus fulgidus
    • Klenk H.-P.et al. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon, Archaeoglobus fulgidus. Nature. 390:1997;364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.-P.1
  • 16
    • 0028306243 scopus 로고
    • Cyclosporin A sensitive peptidyl-prolyl cis-trans isomerase in a halophilic archaeum, Halobacterium cutirubrum
    • Nagashima K., Mitsuhashi S., Kamino K., Maruyama T. Cyclosporin A sensitive peptidyl-prolyl cis-trans isomerase in a halophilic archaeum, Halobacterium cutirubrum. Biochem. Biophys. Res. Commun. 198:1994;466-472.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 466-472
    • Nagashima, K.1    Mitsuhashi, S.2    Kamino, K.3    Maruyama, T.4
  • 18
    • 0028349613 scopus 로고
    • A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli
    • Rahfeld J.-U., Schierhorn A., Mann K., Fischer G. A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett. 343:1994;65-69.
    • (1994) FEBS Lett. , vol.343 , pp. 65-69
    • Rahfeld, J.-U.1    Schierhorn, A.2    Mann, K.3    Fischer, G.4
  • 19
    • 0029809115 scopus 로고    scopus 로고
    • Isolation and amina acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria
    • Rahfeld J.-U., Rücknagel K.P., Stoller G., Horne S.M., Schierhorn A., Young K.D., Fischer G. Isolation and amina acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria. J. Biol. Chem. 271:1996;22130-22138.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22130-22138
    • Rahfeld, J.-U.1    Rücknagel, K.P.2    Stoller, G.3    Horne, S.M.4    Schierhorn, A.5    Young, K.D.6    Fischer, G.7
  • 20
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekierka J.J., Hung S.H.Y., Poe M., Lin S.C., Sigal N.H. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature. 341:1989;755-757.
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.Y.2    Poe, M.3    Lin, S.C.4    Sigal, N.H.5
  • 21
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum DH: Functional analysis and comparative genomics
    • Smith D.R.et al. Complete genome sequence of Methanobacterium thermoautotrophicum DH: functional analysis and comparative genomics. J. Bacteriol. 179:1997;7135-7155.
    • (1997) J. Bacteriol. , vol.179 , pp. 7135-7155
    • Smith, D.R.1
  • 22
    • 0025061678 scopus 로고
    • Molecular cloning and overexpression of the human FK506-binding protein
    • Standaert R.F., Galat A., Verdine G.L., Schreiber S.L. Molecular cloning and overexpression of the human FK506-binding protein. Nature. 346:1990;671-674.
    • (1990) Nature , vol.346 , pp. 671-674
    • Standaert, R.F.1    Galat, A.2    Verdine, G.L.3    Schreiber, S.L.4
  • 23
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller G., Rücknagel K.P., Nierhaus K.H., Schmid F.X., Fischer G., Rahfeld J.-U. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14:1995;4939-4948.
    • (1995) EMBO J. , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rücknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.-U.6
  • 24
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi N., Hayano T., Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature. 337:1989;473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 25
    • 0025158309 scopus 로고
    • Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding
    • Tropschug M., Watcher E., Mayer S., Schönbrunner E.R., Schmid F.X. Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding. Nature. 346:1990;674-677.
    • (1990) Nature , vol.346 , pp. 674-677
    • Tropschug, M.1    Watcher, E.2    Mayer, S.3    Schönbrunner, E.R.4    Schmid, F.X.5
  • 26
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne G.D., Standaert R.F., Karplus P.A., Schreber S.L., Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229:1993;105-124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreber, S.L.4    Clardy, J.5
  • 27
    • 10644224511 scopus 로고
    • Formation of methane by bacterial extracts
    • Wolin E.A., Wolin M.J., Wolfe R.S. Formation of methane by bacterial extracts. J. Biol. Chem. 238:1963;2882-2886.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2882-2886
    • Wolin, E.A.1    Wolin, M.J.2    Wolfe, R.S.3
  • 28
    • 0031592944 scopus 로고    scopus 로고
    • Structural and functional characterization of homo-oligomeric complexes of recombinant α and β chaperonin subunits from the hyperthermophilic archaeum, Thermococcus strain KS-1
    • Yoshida T., Yohda M., Iida T., Maruyama T., Taguchi H., Yoshida M., Yazaki K., Ohta T., Endo I., Kagawa Y. Structural and functional characterization of homo-oligomeric complexes of recombinant α and β chaperonin subunits from the hyperthermophilic archaeum, Thermococcus strain KS-1. J. Mol. Biol. 273:1997;635-645.
    • (1997) J. Mol. Biol. , vol.273 , pp. 635-645
    • Yoshida, T.1    Yohda, M.2    Iida, T.3    Maruyama, T.4    Taguchi, H.5    Yoshida, M.6    Yazaki, K.7    Ohta, T.8    Endo, I.9    Kagawa, Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.