메뉴 건너뛰기




Volumn 29, Issue 3, 1998, Pages 775-785

A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; CHAPERONIN;

EID: 0031904531     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00971.x     Document Type: Article
Times cited : (14)

References (32)
  • 2
    • 0028240897 scopus 로고
    • A new generation of information retrieval tools for biologist: The example of the ExPASy WWW server
    • D.
    • Appel, R., D., Bairoch, A., and Hochstrasser, D.F. (1994) A new generation of information retrieval tools for biologist: the example of the ExPASy WWW server. Trends Biochem Sci 19: 258-260.
    • (1994) Trends Biochem Sci , vol.19 , pp. 258-260
    • Appel, R.1    Bairoch, A.2    Hochstrasser, D.F.3
  • 3
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii
    • Bult, C.J., White, O., Olsen, G.J., Zhou, L., Fleischmann, R.D., Sutton, G.G. et al. (1996) Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii. Science 273: 1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Fleischmann, R.D.5    Sutton, G.G.6
  • 6
    • 0016426743 scopus 로고
    • Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius
    • De Rosa, M., Gambacorta, A., and Bu'lock, J.D. (1975) Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius. J Gen Microbiol 86: 156-164.
    • (1975) J Gen Microbiol , vol.86 , pp. 156-164
    • De Rosa, M.1    Gambacorta, A.2    Bu'lock, J.D.3
  • 7
    • 0026343673 scopus 로고
    • Molecular cloning of soluble aminopeptidases from Saccaromyces cerevisiae
    • García-Alvarez, N., Cueva, R., Suárez-Rendueles, P. (1991) Molecular cloning of soluble aminopeptidases from Saccaromyces cerevisiae. Eur J Biochem 202: 993-1002.
    • (1991) Eur J Biochem , vol.202 , pp. 993-1002
    • García-Alvarez, N.1    Cueva, R.2    Suárez-Rendueles, P.3
  • 8
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., Wickner, S, and Maurizi, M.R. (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11: 815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 9
    • 0028788591 scopus 로고
    • Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin
    • Guagliardi, A., Cerchia, L., and Rossi, M. (1995) Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. J Biol Chem 270: 28126-28132.
    • (1995) J Biol Chem , vol.270 , pp. 28126-28132
    • Guagliardi, A.1    Cerchia, L.2    Rossi, M.3
  • 10
    • 0025171939 scopus 로고
    • Isolation and characterization of an intracellular aminopeptidase from the extreme themophilic archaebacterium Sulfolobus solfataricus
    • Hanner, M., Redl, B., and Stoffler, G. (1990) Isolation and characterization of an intracellular aminopeptidase from the extreme themophilic archaebacterium Sulfolobus solfataricus. Biochim Biophys Acta 1033: 148-153.
    • (1990) Biochim Biophys Acta , vol.1033 , pp. 148-153
    • Hanner, M.1    Redl, B.2    Stoffler, G.3
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 12
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl, F.U., Hlodan, R., and Langer, T. (1994) Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci 19: 20-25.
    • (1994) Trends Biochem Sci , vol.19 , pp. 20-25
    • Hartl, F.U.1    Hlodan, R.2    Langer, T.3
  • 13
    • 0028806653 scopus 로고
    • The heat shock proteins from a hyperthermophylic archaeon are related to the cytosolic chaperonin in eukaryotes
    • Kagawa, H.K., Osipiuk, J., Maltsev, N., Overbeek, R., Quaite-Randall, E., Joachimiak, A., and Trent, J.D. (1995) The heat shock proteins from a hyperthermophylic archaeon are related to the cytosolic chaperonin in eukaryotes. J Mol Biol 253: 712-725.
    • (1995) J Mol Biol , vol.253 , pp. 712-725
    • Kagawa, H.K.1    Osipiuk, J.2    Maltsev, N.3    Overbeek, R.4    Quaite-Randall, E.5    Joachimiak, A.6    Trent, J.D.7
  • 14
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H.P., Clayton, R.A., Tomb, J.F., White, O., Nelson, K.E., Ketchum, K.A. et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6
  • 15
    • 0028116350 scopus 로고
    • The molecular chaperonin TF55 from the thermophilic archaeon Sulfolobus solfataricus. A biochemical and structural characterization
    • Knapp, S., Schmidt-Krey, I., Hebert, H., Bergman, T., Jornvall, H., and Ladenstein, R. (1994) The molecular chaperonin TF55 from the thermophilic archaeon Sulfolobus solfataricus. A biochemical and structural characterization. J Mol Biol 242: 397-407.
    • (1994) J Mol Biol , vol.242 , pp. 397-407
    • Knapp, S.1    Schmidt-Krey, I.2    Hebert, H.3    Bergman, T.4    Jornvall, H.5    Ladenstein, R.6
  • 16
    • 0028834732 scopus 로고
    • Characterization of the 16S ribosomal RNA genes and phylogenetic relationships of sulfur-dependent thermoacidophilic archaebacteria
    • Kurosawa, N., Ohkura, K., Horiuchi, T., and Itoh, Y.H. (1995) Characterization of the 16S ribosomal RNA genes and phylogenetic relationships of sulfur-dependent thermoacidophilic archaebacteria. J Gen Appl Microbiol 41: 75-81.
    • (1995) J Gen Appl Microbiol , vol.41 , pp. 75-81
    • Kurosawa, N.1    Ohkura, K.2    Horiuchi, T.3    Itoh, Y.H.4
  • 17
    • 0023051328 scopus 로고
    • Differential features of ribosomes and of poly (U)-programmed cell-free systems derived from sulphur-dependent archaebacterial species
    • Londei, P., Altamura, S., Cammarano, P., and Petrucci, L. (1986) Differential features of ribosomes and of poly (U)-programmed cell-free systems derived from sulphur-dependent archaebacterial species. Eur J Biochem 157: 455-462.
    • (1986) Eur J Biochem , vol.157 , pp. 455-462
    • Londei, P.1    Altamura, S.2    Cammarano, P.3    Petrucci, L.4
  • 18
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and Lipman, D.J. (1988) Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 85: 2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 19
    • 0025892424 scopus 로고
    • A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria
    • Phipps, B.M., Hoffmann, A., Stetter, K.O., and Baumeister, W. (1991) A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. EMBO J 10: 1711-1722.
    • (1991) EMBO J , vol.10 , pp. 1711-1722
    • Phipps, B.M.1    Hoffmann, A.2    Stetter, K.O.3    Baumeister, W.4
  • 20
    • 0028867591 scopus 로고
    • Conformational cycle of the archeaosome, a TCP1-like chaperonin from Sulfolobus shibatae
    • Quaite-Randall, E., Trent, J.D., Josephs, R., and Joachimiak, A. (1995) Conformational cycle of the archeaosome, a TCP1-like chaperonin from Sulfolobus shibatae. J Biol Chem 270: 28818-28823.
    • (1995) J Biol Chem , vol.270 , pp. 28818-28823
    • Quaite-Randall, E.1    Trent, J.D.2    Josephs, R.3    Joachimiak, A.4
  • 21
    • 0025630439 scopus 로고
    • Mutational analysis of an archaebacterial promoter: Essential role of a TATA box for transcription efficiency and start-site selection in vitro
    • Reiter, W.D., Hudepohl, W., and Zillig, W. (1990) Mutational analysis of an archaebacterial promoter: essential role of a TATA box for transcription efficiency and start-site selection in vitro. Proc Natl Acad Sci USA 87: 9509-9513.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9509-9513
    • Reiter, W.D.1    Hudepohl, W.2    Zillig, W.3
  • 22
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: Functional analysis and comparative genomics
    • Smith, D.R., Doucette-Stamm, L.A., Deloughery, C., Lee, H., Dubois, J., Aldredge, T. et al. (1997) Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics. J Bacteriol 179: 7135-7155.
    • (1997) J Bacteriol , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3    Lee, H.4    Dubois, J.5    Aldredge, T.6
  • 23
    • 0026624779 scopus 로고
    • Characterization of the Lactococcus lactis pepN gene encoding an aminopeptidase homologous to mammalian aminopeptidase N
    • Tan, P.S., van Alen-Boerrigter, I.J., Poolman, B., Siezen, R.J., de Vos, W.M., and Konings, W.N. (1992) Characterization of the Lactococcus lactis pepN gene encoding an aminopeptidase homologous to mammalian aminopeptidase N. FEBS Lett 306: 9-16.
    • (1992) FEBS Lett , vol.306 , pp. 9-16
    • Tan, P.S.1    Van Alen-Boerrigter, I.J.2    Poolman, B.3    Siezen, R.J.4    De Vos, W.M.5    Konings, W.N.6
  • 24
    • 0027208935 scopus 로고
    • Aminopeptidases: Towards a mechanism of action
    • Taylor, A. (1993) Aminopeptidases: towards a mechanism of action. Trends Biochem Sci 18: 167-172.
    • (1993) Trends Biochem Sci , vol.18 , pp. 167-172
    • Taylor, A.1
  • 25
    • 0025234729 scopus 로고
    • Acquired thermotolerance and heat shock in the extremely thermophilic archaebacterium Sulfolobus sp. strain B1
    • Trent, J.D., Osipiuk, J., and Pinkau, T. (1990) Acquired thermotolerance and heat shock in the extremely thermophilic archaebacterium Sulfolobus sp. strain B1. J Bacteriol 172: 1478-1484.
    • (1990) J Bacteriol , vol.172 , pp. 1478-1484
    • Trent, J.D.1    Osipiuk, J.2    Pinkau, T.3
  • 26
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent, J.D., Nimmesgern, E., Wall, J.S., Hartl, F.U., and Horwich, A.L. (1991) A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354: 490-493.
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.U.4    Horwich, A.L.5
  • 28
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci USA 93: 12142-12149.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 29
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner, I., Arlt, H., van Dyck, L., Langer, T., and Neupert, W. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13: 5135-5145.
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    Van Dyck, L.3    Langer, T.4    Neupert, W.5
  • 30
    • 0028791460 scopus 로고
    • Expression of an archaeal chaperonin in E. coli: Formation of homo- (alpha, beta) and hetero-oligomeric (alpha + beta) thermosome complexes
    • Waldmann, T., Nitsch, M., Klumpp, M., and Baumeister, W. (1995) Expression of an archaeal chaperonin in E. coli: formation of homo- (alpha, beta) and hetero-oligomeric (alpha + beta) thermosome complexes. FEBS Lett. 376: 67-73.
    • (1995) FEBS Lett. , vol.376 , pp. 67-73
    • Waldmann, T.1    Nitsch, M.2    Klumpp, M.3    Baumeister, W.4
  • 31
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., et al. (1995) The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14: 1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6
  • 32
    • 0027426760 scopus 로고
    • Confusion in the assignments of Sulfolobus sequences to Sulfolobus species
    • Zillig, W. (1993) Confusion in the assignments of Sulfolobus sequences to Sulfolobus species. Nucleic Acids Res 21: 5273.
    • (1993) Nucleic Acids Res , vol.21 , pp. 5273
    • Zillig, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.