메뉴 건너뛰기




Volumn 59, Issue 4, 2010, Pages 497-505

The Hsp70 chaperones of the Tritryps are characterized by unusual features and novel members

Author keywords

Heat shock proteins; Hsp40; Hsp70; Kinetoplastid; Molecular chaperone; Trypanosome

Indexed keywords

HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70;

EID: 77958456516     PISSN: 13835769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.parint.2010.08.008     Document Type: Review
Times cited : (28)

References (54)
  • 1
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005, 62:670-684.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 2
    • 49749100105 scopus 로고    scopus 로고
    • Multiple Hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity
    • Kabani M., Martineau C.N. Multiple Hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity. Curr Genomics 2008, 9:338-348.
    • (2008) Curr Genomics , vol.9 , pp. 338-348
    • Kabani, M.1    Martineau, C.N.2
  • 3
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversity between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos M.J., Hageman J., Carra S., Kampinga H.M. Structural and functional diversity between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008, 47:700-2011.
    • (2008) Biochemistry , vol.47 , pp. 700-2011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.M.4
  • 5
    • 67650151032 scopus 로고    scopus 로고
    • Heat shock protein 40: structural studies and their functional implications
    • Li J., Qian X., Sha B. Heat shock protein 40: structural studies and their functional implications. Protein Pept Lett 2009, 16:606-612.
    • (2009) Protein Pept Lett , vol.16 , pp. 606-612
    • Li, J.1    Qian, X.2    Sha, B.3
  • 6
    • 2642689664 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
    • Demand J., Lüders J., Höfeld J. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol Cell Biol 1998, 18:2023-2028.
    • (1998) Mol Cell Biol , vol.18 , pp. 2023-2028
    • Demand, J.1    Lüders, J.2    Höfeld, J.3
  • 7
    • 7044240678 scopus 로고    scopus 로고
    • Hop: more than an Hsp70/Hsp90 adaptor protein
    • Odunuga O.O., Longshaw V.M., Blatch G.L. Hop: more than an Hsp70/Hsp90 adaptor protein. BioEssays 2004, 26:1058-1068.
    • (2004) BioEssays , vol.26 , pp. 1058-1068
    • Odunuga, O.O.1    Longshaw, V.M.2    Blatch, G.L.3
  • 8
    • 22344447035 scopus 로고    scopus 로고
    • Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions
    • Hennessy F., Nicoll W.S., Zimmermann R., Cheetham M.E., Blatch G.L. Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci 2005, 14:1687-1708.
    • (2005) Protein Sci , vol.14 , pp. 1687-1708
    • Hennessy, F.1    Nicoll, W.S.2    Zimmermann, R.3    Cheetham, M.E.4    Blatch, G.L.5
  • 9
    • 80052436314 scopus 로고    scopus 로고
    • Nucleotide exchange factors for Hsp70 molecular chaperones. In: Blatch G.L., ed. Networking of Chaperones by Co-Chaperones. Austin: Landes Bioscience; New York: Springer Science + Business Media;
    • Brodsky JL, Bracher A. Nucleotide exchange factors for Hsp70 molecular chaperones. In: Blatch G.L., ed. Networking of Chaperones by Co-Chaperones. Austin: Landes Bioscience; New York: Springer Science + Business Media; 2007; 26-37.
    • (2007) , pp. 26-37
    • Brodsky, J.L.1    Bracher, A.2
  • 10
    • 34548232285 scopus 로고    scopus 로고
    • The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host
    • Botha M., Pesce E.-R., Blatch G.L. The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. Int J Biochem Cell Biol 2007, 39:1781-1803.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1781-1803
    • Botha, M.1    Pesce, E.-R.2    Blatch, G.L.3
  • 11
    • 33645059434 scopus 로고    scopus 로고
    • The evolution and diversity of kinetoplastid flagellates
    • Simpson A.G.B., Stevens J.R., Lukes J. The evolution and diversity of kinetoplastid flagellates. Trends Parasitol 2006, 22:168-174.
    • (2006) Trends Parasitol , vol.22 , pp. 168-174
    • Simpson, A.G.B.1    Stevens, J.R.2    Lukes, J.3
  • 13
    • 0021866913 scopus 로고
    • Heat shock genes: regulatory role for differentiation in parasitic protozoa
    • Van der Ploeg L.H.T., Giannini S.H., Cantor C.R. Heat shock genes: regulatory role for differentiation in parasitic protozoa. Science 1985, 228:1443-1446.
    • (1985) Science , vol.228 , pp. 1443-1446
    • Van der Ploeg, L.H.T.1    Giannini, S.H.2    Cantor, C.R.3
  • 14
    • 0028071199 scopus 로고
    • Molecular and Biochemical comparison of the 70-kDa heat shock proteins of Trypanosoma cruzi
    • Olson C.L., Nadeau K.C., Sullivan M.A., Winquist A.G., Donelson J.E., Walsh C.T., et al. Molecular and Biochemical comparison of the 70-kDa heat shock proteins of Trypanosoma cruzi. J Biol Chem 1994, 269:3868-3874.
    • (1994) J Biol Chem , vol.269 , pp. 3868-3874
    • Olson, C.L.1    Nadeau, K.C.2    Sullivan, M.A.3    Winquist, A.G.4    Donelson, J.E.5    Walsh, C.T.6
  • 15
    • 0029143254 scopus 로고
    • High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania
    • Brandau S., Dresel A., Clos J. High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania. Biochem J 1995, 318:225-232.
    • (1995) Biochem J , vol.318 , pp. 225-232
    • Brandau, S.1    Dresel, A.2    Clos, J.3
  • 17
    • 0141520538 scopus 로고    scopus 로고
    • Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani
    • Bente M., Harder S., Wiesgigl M., Haukeshoven J., Gelhaus C., Krause E., et al. Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani. Proteomics 2003, 3:1811-1829.
    • (2003) Proteomics , vol.3 , pp. 1811-1829
    • Bente, M.1    Harder, S.2    Wiesgigl, M.3    Haukeshoven, J.4    Gelhaus, C.5    Krause, E.6
  • 21
    • 33745725868 scopus 로고    scopus 로고
    • A combined proteomic and transcriptomic approach to the study of stage differentiation in Leishmania infantum
    • McNicoll F., Drummelsmith J., Muller M., Madore E., Boilard N., Oulette M., et al. A combined proteomic and transcriptomic approach to the study of stage differentiation in Leishmania infantum. Proteomics 2006, 6:3567-3581.
    • (2006) Proteomics , vol.6 , pp. 3567-3581
    • McNicoll, F.1    Drummelsmith, J.2    Muller, M.3    Madore, E.4    Boilard, N.5    Oulette, M.6
  • 22
    • 31344479863 scopus 로고    scopus 로고
    • Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei
    • Jones A., Faldas A., Foucher A., Hunt E., Tait A., Wastling J.M., et al. Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei. Proteomics 2006, 6:259-267.
    • (2006) Proteomics , vol.6 , pp. 259-267
    • Jones, A.1    Faldas, A.2    Foucher, A.3    Hunt, E.4    Tait, A.5    Wastling, J.M.6
  • 23
    • 39049118320 scopus 로고    scopus 로고
    • Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei
    • Vertommen D., Van Roy J., Szikora J.P., Rider M.H., Michels P.A., Opperdoes F.R. Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei. Mol Biochem Parasitol 2008, 158:189-201.
    • (2008) Mol Biochem Parasitol , vol.158 , pp. 189-201
    • Vertommen, D.1    Van Roy, J.2    Szikora, J.P.3    Rider, M.H.4    Michels, P.A.5    Opperdoes, F.R.6
  • 24
    • 10844244086 scopus 로고    scopus 로고
    • Early evolution within kinetoplastids (euglenozoa), and the late emergence of trypanosomatids
    • Simpson G.B., Gill E.E., Callahan H.A., Litaker R.W., Roger A.J. Early evolution within kinetoplastids (euglenozoa), and the late emergence of trypanosomatids. Protist 2004, 155:407-422.
    • (2004) Protist , vol.155 , pp. 407-422
    • Simpson, G.B.1    Gill, E.E.2    Callahan, H.A.3    Litaker, R.W.4    Roger, A.J.5
  • 25
    • 34250351297 scopus 로고    scopus 로고
    • A postgenomic view of the heat shock proteins in kinetoplastids
    • Folgueira C., Requena J.M. A postgenomic view of the heat shock proteins in kinetoplastids. FEMS Microbiol Rev 2007, 31:359-377.
    • (2007) FEMS Microbiol Rev , vol.31 , pp. 359-377
    • Folgueira, C.1    Requena, J.M.2
  • 27
    • 0024393859 scopus 로고
    • A family of heat shock protein 70-related genes are expressed in the promastigotes of Leishmania major
    • Searle S., Campos A.J.R., Coulson R.M.R., Spithill T.W., Smith D.F. A family of heat shock protein 70-related genes are expressed in the promastigotes of Leishmania major. Nucleic Acids Res 1989, 17:5081-5095.
    • (1989) Nucleic Acids Res , vol.17 , pp. 5081-5095
    • Searle, S.1    Campos, A.J.R.2    Coulson, R.M.R.3    Spithill, T.W.4    Smith, D.F.5
  • 28
    • 0027337030 scopus 로고
    • Leishmania major: characterisation and expression of a cytoplasmic stress-related protein
    • Searle S., Smith D.F. Leishmania major: characterisation and expression of a cytoplasmic stress-related protein. Exp Parasitol 1993, 77:43-52.
    • (1993) Exp Parasitol , vol.77 , pp. 43-52
    • Searle, S.1    Smith, D.F.2
  • 29
    • 29344449706 scopus 로고    scopus 로고
    • Human and yeast Hsp110 chaperones exhibit functional differences
    • Raviol H., Bukau B., Mayer M.P. Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett 2006, 580:168-174.
    • (2006) FEBS Lett , vol.580 , pp. 168-174
    • Raviol, H.1    Bukau, B.2    Mayer, M.P.3
  • 30
  • 31
    • 0024347362 scopus 로고
    • Molecular cloning of mtp70, a mitochondrial member of the hsp70 family
    • Engman D.M., Kirchhoff L.V., Donelson J.E. Molecular cloning of mtp70, a mitochondrial member of the hsp70 family. Mol Cell Biol 1989, 9:5163-5168.
    • (1989) Mol Cell Biol , vol.9 , pp. 5163-5168
    • Engman, D.M.1    Kirchhoff, L.V.2    Donelson, J.E.3
  • 32
    • 50249111475 scopus 로고    scopus 로고
    • Distinct mitochondrial Hsp70 homologues conserved in various Leishmania species suggest novel biological functions
    • Campos R.M., Nascimento M., Ferraz J.C., Pereira M.M.C., Rocha P.O., Thompson G.M., et al. Distinct mitochondrial Hsp70 homologues conserved in various Leishmania species suggest novel biological functions. Mol Biochem Parasitol 2008, 160:157-162.
    • (2008) Mol Biochem Parasitol , vol.160 , pp. 157-162
    • Campos, R.M.1    Nascimento, M.2    Ferraz, J.C.3    Pereira, M.M.C.4    Rocha, P.O.5    Thompson, G.M.6
  • 33
    • 38649089796 scopus 로고    scopus 로고
    • Trypanosoma brucei: differential requirement of membrane potential for import of proteins into mitochondria in two developmental stages
    • Williams S., Lipi S., Singha U.K., Chaudhuri M. Trypanosoma brucei: differential requirement of membrane potential for import of proteins into mitochondria in two developmental stages. Exp Parasitol 2008, 118:420-433.
    • (2008) Exp Parasitol , vol.118 , pp. 420-433
    • Williams, S.1    Lipi, S.2    Singha, U.K.3    Chaudhuri, M.4
  • 35
    • 0027275067 scopus 로고
    • Molecular cloning and cellular localization of a BiP homologue in Trypanosoma brucei
    • Bangs J.D., Uyetake L., Brickman M.J., Balber A.E., Boothroyd J.C. Molecular cloning and cellular localization of a BiP homologue in Trypanosoma brucei. J Cell Sci 1993, 105:1101-1113.
    • (1993) J Cell Sci , vol.105 , pp. 1101-1113
    • Bangs, J.D.1    Uyetake, L.2    Brickman, M.J.3    Balber, A.E.4    Boothroyd, J.C.5
  • 36
    • 0026583674 scopus 로고
    • Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe
    • Pidoux A., Armstrong J. Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe. EMBO J 1992, 11:1583-1591.
    • (1992) EMBO J , vol.11 , pp. 1583-1591
    • Pidoux, A.1    Armstrong, J.2
  • 37
    • 0029764290 scopus 로고    scopus 로고
    • A soluble secretory reporter system in Trypanosoma brucei
    • Bangs J.D., Brouch E.M., Ransom D.M., Roggy J.L. A soluble secretory reporter system in Trypanosoma brucei. J Biol Chem 1996, 31:18387-18393.
    • (1996) J Biol Chem , vol.31 , pp. 18387-18393
    • Bangs, J.D.1    Brouch, E.M.2    Ransom, D.M.3    Roggy, J.L.4
  • 38
    • 0028341242 scopus 로고
    • Molecular cloning and characterisation of the 78-kilodalton glucose-regulated protein of Trypanosoma cruzi
    • Tibbetts R.S., Kim I.Y., Olson C.L., Barthel L.M., Sullivan M.A., Winquist A.G., et al. Molecular cloning and characterisation of the 78-kilodalton glucose-regulated protein of Trypanosoma cruzi. Infect Immunol 1994, 62:2499-2507.
    • (1994) Infect Immunol , vol.62 , pp. 2499-2507
    • Tibbetts, R.S.1    Kim, I.Y.2    Olson, C.L.3    Barthel, L.M.4    Sullivan, M.A.5    Winquist, A.G.6
  • 41
    • 0035941210 scopus 로고    scopus 로고
    • A DnaJ-Like protein homologous to the yeast co-chaperone Sis1 (Tcj6p) is involved in initiation of translation in Trypanosoma cruzi
    • Salmon D., Montero-Lomeli M., Goldenberg S. A DnaJ-Like protein homologous to the yeast co-chaperone Sis1 (Tcj6p) is involved in initiation of translation in Trypanosoma cruzi. J Biol Chem 2001, 276:43970-43979.
    • (2001) J Biol Chem , vol.276 , pp. 43970-43979
    • Salmon, D.1    Montero-Lomeli, M.2    Goldenberg, S.3
  • 42
    • 2442513446 scopus 로고    scopus 로고
    • A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40
    • Edkins A.L., Ludewig M.H., Blatch G.L. A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40. Int J Biochem Cell Biol 2004, 36:1585-1598.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1585-1598
    • Edkins, A.L.1    Ludewig, M.H.2    Blatch, G.L.3
  • 43
    • 70449524433 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of Tbj1, a novel type III Hsp40 from Trypanosoma brucei, the African Sleeping Sickness parasite
    • Louw C.A., Ludewig M.H., Blatch G.L. Overexpression, purification and characterization of Tbj1, a novel type III Hsp40 from Trypanosoma brucei, the African Sleeping Sickness parasite. Protein Expr Purif 2010, 69:168-177.
    • (2010) Protein Expr Purif , vol.69 , pp. 168-177
    • Louw, C.A.1    Ludewig, M.H.2    Blatch, G.L.3
  • 44
    • 57649137959 scopus 로고    scopus 로고
    • Role of protein translocation pathways across the endoplasmic reticulum in Trypanosoma brucei
    • Goldschmidt H., Sheiner L., Bütikofer P., Roditi I., Uliel S., Günzel M., et al. Role of protein translocation pathways across the endoplasmic reticulum in Trypanosoma brucei. J Biol Chem 2008, 283:32085-32098.
    • (2008) J Biol Chem , vol.283 , pp. 32085-32098
    • Goldschmidt, H.1    Sheiner, L.2    Bütikofer, P.3    Roditi, I.4    Uliel, S.5    Günzel, M.6
  • 45
    • 62549112594 scopus 로고    scopus 로고
    • A novel twist to protein secretion in eukaryotes
    • Zimmermann R., Blatch G.L. A novel twist to protein secretion in eukaryotes. Trends Parasitol 2009, 25:147-150.
    • (2009) Trends Parasitol , vol.25 , pp. 147-150
    • Zimmermann, R.1    Blatch, G.L.2
  • 46
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • Jiang J., Prasad K., Lafer E., Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell 2005, 20:513-524.
    • (2005) Mol Cell , vol.20 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.3    Sousa, R.4
  • 48
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT Version 5: improvement in accuracy of multiple sequence alignment
    • Katoh K., Kuma K., Toh H., Miyata T. MAFFT Version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res 2005, 33:511-518.
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 49
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 50
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • Cupp-Vickery J.R., Peterson J.C., Ta D.T., Vickery L.E. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J Mol Biol 2004, 342:1265-1278.
    • (2004) J Mol Biol , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 51
    • 0029937037 scopus 로고    scopus 로고
    • A structural analysis of substrate binding by the molecular chaperone DnaK
    • Zhu X., Zhao X., Burkholder W.F., Gragerov A., Ogata C.M., Gottesman M., et al. A structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996, 272:1606-1614.
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1    Zhao, X.2    Burkholder, W.F.3    Gragerov, A.4    Ogata, C.M.5    Gottesman, M.6
  • 52
    • 38149099329 scopus 로고    scopus 로고
    • Characterisation of the plasma membrane subproteome of bloodstream form Trypanosoma brucei
    • Bridges D.J., Pitt A.R., Hanrahan O., Brennan K., Voorheis H.P., Herzyk P., et al. Characterisation of the plasma membrane subproteome of bloodstream form Trypanosoma brucei. Proteomics 2008, 8:83-99.
    • (2008) Proteomics , vol.8 , pp. 83-99
    • Bridges, D.J.1    Pitt, A.R.2    Hanrahan, O.3    Brennan, K.4    Voorheis, H.P.5    Herzyk, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.