메뉴 건너뛰기




Volumn 9, Issue , 2004, Pages 1318-1332

Evolution of assisted protein folding: The distribution of the main chaperoning systems within the phylogenetic domain Archaea

Author keywords

Anti Stress Mechanisms; Archaea; Chaperones; Chaperoning Systems; Chaperonins; GroEL; GroES; GrpE; Hsp40(DnaJ); Hsp60 chaperonins; Hsp70(DnaK); Methanosarcina acetivorans; Methanosarcina mazeii S 6; Prefoldins; Stress; Thermosome; Thermosome subunits

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; ARCHAEAL PROTEIN; CHAPERONIN;

EID: 2442718034     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1328     Document Type: Review
Times cited : (47)

References (62)
  • 1
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau B, E. Deuerling, C. Pfund & E. A. Craig: Getting newly synthesized proteins into shape. Cell 101, 119-122 (2000)
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 3
    • 0030910776 scopus 로고    scopus 로고
    • Mitochondrial biogenesis: The Tom and Tim machine
    • Pfanner N. & M. Meijer: Mitochondrial biogenesis: The Tom and Tim machine. Curr Biol 7, R100-R103 (1997)
    • (1997) Curr Biol , vol.7
    • Pfanner, N.1    Meijer, M.2
  • 4
    • 0033602228 scopus 로고    scopus 로고
    • Molecular chaperones: Pathways and networks
    • Ellis R. J.: Molecular chaperones: Pathways and networks. Curr Biol 9, R137-R139 (1999)
    • (1999) Curr Biol , vol.9
    • Ellis, R.J.1
  • 5
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J. C., N. J. Hoogenraad & F. U. Hartl: Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112, 41-50 (2003)
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 7
    • 0025892424 scopus 로고
    • A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria
    • Phipps B. M., A. Hoffmann, K. O. Stetter & W. Baumeister: A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. EMBO J 10, 1711-1722 (1991)
    • (1991) EMBO J , vol.10 , pp. 1711-1722
    • Phipps, B.M.1    Hoffmann, A.2    Stetter, K.O.3    Baumeister, W.4
  • 8
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent J. D., E. Nimmesgern, J. S. Wall, F. U. Hartl & A. L. Horwich: A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354, 490-493 (1991)
    • (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
  • 9
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos C. & W. J. Welch: Role of the major heat shock proteins as molecular chaperones. Annu Rev Cell Biol 9, 601-634 (1993)
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 11
    • 0033574162 scopus 로고    scopus 로고
    • The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
    • Rommelaere H., M. De Neve, R. Melki, J Vandekerckhove & C. Ampe: The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. Biochemistry 38, 3246-3257 (1999)
    • (1999) Biochemistry , vol.38 , pp. 3246-3257
    • Rommelaere, H.1    De Neve, M.2    Melki, R.3    Vandekerckhove, J.4    Ampe, C.5
  • 12
    • 0028958602 scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F. U. & J. Martin: Molecular chaperones in cellular protein folding. Curr Op Struct Biol 5, 92-102 (1995)
    • (1995) Curr Op Struct Biol , vol.5 , pp. 92-102
    • Hartl, F.U.1    Martin, J.2
  • 13
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ, conservation and adaptation of chaperone function
    • Cheetham M. E. & A. J. Caplan: Structure, function and evolution of DnaJ, conservation and adaptation of chaperone function. Cell Stress Chap 3, 28-36 (1998)
    • (1998) Cell Stress Chap , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 14
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha- and gamma-tubulin
    • Geisler S., K. Siegers & E. Schiebel: A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J 17, 952-966 (1998)
    • (1998) EMBO J , vol.17 , pp. 952-966
    • Geisler, S.1    Siegers, K.2    Schiebel, E.3
  • 15
    • 0032560551 scopus 로고    scopus 로고
    • The thermosome: Archetype of group II chaperonins
    • Klumpp M. & W. Baumeister: The thermosome: archetype of group II chaperonins. FEBS Lett 430, 73-77 (1998)
    • (1998) FEBS Lett , vol.430 , pp. 73-77
    • Klumpp, M.1    Baumeister, W.2
  • 17
    • 0034856940 scopus 로고    scopus 로고
    • Chaperone-assisted protein folding in the cell cytoplasm
    • Houry W. A.: Chaperone-assisted protein folding in the cell cytoplasm. Curr Prot & Pep Sci 2, 244-227 (2001)
    • (2001) Curr Prot & Pep Sci , vol.2 , pp. 244-1227
    • Houry, W.A.1
  • 20
    • 0026692645 scopus 로고
    • Cloning of the Hsp70 gene from Halobacterium marismortui: Relatedness of archaebacterial Hsp70 to its eubacterial homologs and a model for the evolution of the Hsp70 gene
    • Gupta R. S. & B. Singh: Cloning of the Hsp70 gene from Halobacterium marismortui: relatedness of archaebacterial Hsp70 to its eubacterial homologs and a model for the evolution of the Hsp70 gene. J Bacteriol 174, 4594-4605 (1992)
    • (1992) J Bacteriol , vol.174 , pp. 4594-4605
    • Gupta, R.S.1    Singh, B.2
  • 21
    • 0028909379 scopus 로고
    • Archaeal grpE: Transcription in two different morphologic stages of Methanosarcina mazei and comparison with dnaK and dnaJ
    • Conway de Macario E., M. Clarens & A. J. L. Macario: Archaeal grpE: transcription in two different morphologic stages of Methanosarcina mazei and comparison with dnaK and dnaJ. J Bacteriol 177, 544-550 (1995)
    • (1995) J Bacteriol , vol.177 , pp. 544-550
    • Conway De Macario, E.1    Clarens, M.2    Macario, A.J.L.3
  • 22
    • 0029923838 scopus 로고    scopus 로고
    • The origin of the eukaryotic cell
    • Gupta R. S. & G. B. Golding: The origin of the eukaryotic cell. Trends Biochem Sci 21, 166-171 (1996)
    • (1996) Trends Biochem Sci , vol.21 , pp. 166-171
    • Gupta, R.S.1    Golding, G.B.2
  • 23
    • 0031022823 scopus 로고    scopus 로고
    • Sequencing of heat shock protein 70 (DnaK) homologs from Deinococcus proteolyticus and Thermomicrobium roseum and their integration in a protein-based phylogeny of prokaryotes
    • Gupta R. S., K. Bustard, M. Falah & D. Singh: Sequencing of heat shock protein 70 (DnaK) homologs from Deinococcus proteolyticus and Thermomicrobium roseum and their integration in a protein-based phylogeny of prokaryotes. J Bacteriol 179, 345-357 (1997)
    • (1997) J Bacteriol , vol.179 , pp. 345-357
    • Gupta, R.S.1    Bustard, K.2    Falah, M.3    Singh, D.4
  • 24
    • 0031794743 scopus 로고    scopus 로고
    • Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes
    • Gupta R. S.: Protein phylogenies and signature sequences: a reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes. Microbiol Mol Biol Rev 62, 1435-1491 (1998a)
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1435-1491
    • Gupta, R.S.1
  • 25
    • 0031880993 scopus 로고    scopus 로고
    • What are archaebacteria: Life's third domain or monoderm prokaryotes related to Gram-positive bacteria? A new proposal for the classification of prokaryotic organisms
    • Gupta R. S.: What are archaebacteria: life's third domain or monoderm prokaryotes related to Gram-positive bacteria? A new proposal for the classification of prokaryotic organisms. Mol Microbiol 29, 695-707 (1998b)
    • (1998) Mol Microbiol , vol.29 , pp. 695-707
    • Gupta, R.S.1
  • 27
    • 0037121087 scopus 로고    scopus 로고
    • Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution
    • Emelyanov V. V.: Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution. Gene 299, 125-133 (2002)
    • (2002) Gene , vol.299 , pp. 125-133
    • Emelyanov, V.V.1
  • 28
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hohfeld J., Y. Minami & F. U. Hartl: Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598 (1995)
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 29
    • 0029126927 scopus 로고
    • Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators
    • Levy E. J., J. McCarty, B. Bukau & W. J. Chirico: Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators. FEBS Lett. 368, 435-440 (1995)
    • (1995) FEBS Lett , vol.368 , pp. 435-440
    • Levy, E.J.1    McCarty, J.2    Bukau, B.3    Chirico, W.J.4
  • 30
    • 0029741321 scopus 로고    scopus 로고
    • Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40
    • Minami Y., J. Hohfeld, K. Ohtsuka & F. U. Hartl: Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. J Biol Chem 271, 19617-19624 (1996)
    • (1996) J Biol Chem , vol.271 , pp. 19617-19624
    • Minami, Y.1    Hohfeld, J.2    Ohtsuka, K.3    Hartl, F.U.4
  • 33
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F. U. & M. Hayer-Hartl: Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (2002)
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 34
    • 0043028205 scopus 로고    scopus 로고
    • What is a co-chaperone?
    • Caplan A. J.: What is a co-chaperone? Cell Stress Chap 8, 105-107 (2003)
    • (2003) Cell Stress Chap , vol.8 , pp. 105-107
    • Caplan, A.J.1
  • 35
    • 0026935588 scopus 로고
    • Heat-shock proteins and stress tolerance in microorganisms
    • Lindquist S.: Heat-shock proteins and stress tolerance in microorganisms. Curr Op Genet Dev 2, 748-755 (1992)
    • (1992) Curr Op Genet Dev , vol.2 , pp. 748-755
    • Lindquist, S.1
  • 36
    • 0035260487 scopus 로고    scopus 로고
    • The molecular chaperone system and other anti-stress mechanisms in archaea
    • Macario A. J. L. & E. Conway de Macario: The molecular chaperone system and other anti-stress mechanisms in archaea. Front. Biosci. 6, d262-283 (2001) http://www.bioscience.org/2001/v6/d/macario/fulltext.htm
    • (2001) Front Biosci , vol.6
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 37
  • 38
    • 0035783169 scopus 로고    scopus 로고
    • Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • Ben-Zvi A. P. & P. Goloubinoff: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J Struct Biol 135, 84-93 (2001)
    • (2001) J Struct Biol , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 43
    • 0032878862 scopus 로고    scopus 로고
    • The genes coding for the hsp70(dnaK) molecular chaperone machine occur in the moderate thermophilic archaeon Methanosarcina thermophila TM-1
    • Hofman-Bang J. P., M. Lange, E. Conway de Macario, A. J. L. Macario & B. K. Ahring: The genes coding for the hsp70(dnaK) molecular chaperone machine occur in the moderate thermophilic archaeon Methanosarcina thermophila TM-1. Gene 238, 387-395 (1999)
    • (1999) Gene , vol.238 , pp. 387-395
    • Hofman-Bang, J.P.1    Lange, M.2    Conway De Macario, E.3    Macario, A.J.L.4    Ahring, B.K.5
  • 45
    • 0032956536 scopus 로고    scopus 로고
    • Discontinuous occurrence of the hsp70(dnaK) gene among archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein
    • Gribaldo S., V. Lumia, R. Creti, E. Conway de Macario, A. Sanangelantoni & P. Cammarano: Discontinuous occurrence of the hsp70(dnaK) gene among archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein. J Bacteriol 181, 434-443 (1999)
    • (1999) J Bacteriol , vol.181 , pp. 434-443
    • Gribaldo, S.1    Lumia, V.2    Creti, R.3    Conway De Macario, E.4    Sanangelantoni, A.5    Cammarano, P.6
  • 46
    • 0025788262 scopus 로고
    • Characterization of the groEL-like genes in Streptomyces albus
    • Mazodier P., G. Guglielmi, J. Davies & C. J. Thompson: Characterization of the groEL-like genes in Streptomyces albus. J Bacteriol 173, 7382-7386 (1991)
    • (1991) J Bacteriol , vol.173 , pp. 7382-7386
    • Mazodier, P.1    Guglielmi, G.2    Davies, J.3    Thompson, C.J.4
  • 47
    • 0025787885 scopus 로고
    • A dnaK homolog in the archaebacterium Methanosarcina mazei S6
    • Macario A. J. L., C. B. Dugan & E. Conway de Macario: A dnaK homolog in the archaebacterium Methanosarcina mazei S6. Gene 108, 133-137 (1991)
    • (1991) Gene , vol.108 , pp. 133-137
    • Macario, A.J.L.1    Dugan, C.B.2    Conway De Macario, E.3
  • 49
    • 0033598189 scopus 로고    scopus 로고
    • Recurrent paralogy in the evolution of archaeal chaperonins
    • Archibald J. M., J. M. Logsdon Jr & W. F. Doolittle: Recurrent paralogy in the evolution of archaeal chaperonins. Curr Biol 9, 1053-1056 (1999)
    • (1999) Curr Biol , vol.9 , pp. 1053-1056
    • Archibald, J.M.1    Logsdon Jr., J.M.2    Doolittle, W.F.3
  • 50
    • 0025911026 scopus 로고
    • Heat shock response of the archaebacterium Methanococcus voltae
    • Hebert A. M., A. M. Kropinski & K. F. Jarrell: Heat shock response of the archaebacterium Methanococcus voltae. J Bacteriol 173, 3224-3227 (1991)
    • (1991) J Bacteriol , vol.173 , pp. 3224-3227
    • Hebert, A.M.1    Kropinski, A.M.2    Jarrell, K.F.3
  • 51
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta R. S.: Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol Microbiol 15, 1-11 (1995)
    • (1995) Mol Microbiol , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 55
    • 0001010955 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic cytosolic chaperonin- containing TCP-1
    • Ed: B. Bukau. Harwood Academic Publishers, Australia
    • Willison K. R.: Composition and function of the eukaryotic cytosolic chaperonin-containing TCP-1. In: Molecular chaperones and folding catalysis. Ed: B. Bukau. Harwood Academic Publishers, Australia. pp.555-571 (1999)
    • (1999) Molecular Chaperones and Folding Catalysis , pp. 555-571
    • Willison, K.R.1
  • 56
    • 0035783161 scopus 로고    scopus 로고
    • Gene duplication and the evolution of group II chaperonins: Implications for structure and function
    • Archibald J. M., C. Blouin & W. F. Doolittle: Gene duplication and the evolution of group II chaperonins: Implications for structure and function. J Struct Biol 135, 157-169 (2001)
    • (2001) J Struct Biol , vol.135 , pp. 157-169
    • Archibald, J.M.1    Blouin, C.2    Doolittle, W.F.3
  • 57
    • 0036303409 scopus 로고    scopus 로고
    • Gene duplication and gene conversion shape the evolution of archaeal chaperonins
    • Archibald, J. M. & A. J. Roger: Gene duplication and gene conversion shape the evolution of archaeal chaperonins. J Mol Biol 316, 1042-1050 (2002)
    • (2002) J Mol Biol , vol.316 , pp. 1042-1050
    • Archibald, J.M.1    Roger, A.J.2
  • 60
    • 0344500848 scopus 로고    scopus 로고
    • The archaeal molecular chaperone machine: Peculiarities and paradoxes
    • Macario A. J. L. & E. Conway de Macario: The archaeal molecular chaperone machine: peculiarities and paradoxes. Genetics 152, 1277-1283 (1999)
    • (1999) Genetics , vol.152 , pp. 1277-1283
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 61
    • 0028048970 scopus 로고
    • Identification of a grpE heat-shock gene homolog in the archaeon Methanosarcina mazei
    • Conway de Macario E., C. B. Dugan & A. J. L. Macario: Identification of a grpE heat-shock gene homolog in the archaeon Methanosarcina mazei. J Mol Biol 240, 95-101 (1994)
    • (1994) J Mol Biol , vol.240 , pp. 95-101
    • Conway De Macario, E.1    Dugan, C.B.2    Macario, A.J.L.3
  • 62
    • 0029040448 scopus 로고
    • The archaeal dnaK-dnaJ gene cluster: Organization and expression in the methanogen Methanosarcina mazei
    • Clarens M., A. J. L. Macario & E. Conway de Macario: The archaeal dnaK-dnaJ gene cluster: organization and expression in the methanogen Methanosarcina mazei. J Mol Biol 250, 191-201 (1995)
    • (1995) J Mol Biol , vol.250 , pp. 191-201
    • Clarens, M.1    Macario, A.J.L.2    Conway De Macario, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.