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Volumn 60, Issue , 2015, Pages 93-98

Trypanosoma brucei J protein 2 is a stress inducible and essential Hsp40

Author keywords

Hsp40; Molecular chaperone; RNA interference; Tbj2; Trypanosoma brucei

Indexed keywords

GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 40; HYBRID PROTEIN; MESSENGER RNA; PROTEIN DNAJ; TRYPANOSOMA BRUCEI J PROTEIN 2; UNCLASSIFIED DRUG; CHAPERONE; PROTOZOAL PROTEIN;

EID: 84921303510     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2014.12.016     Document Type: Article
Times cited : (9)

References (37)
  • 1
    • 11144327213 scopus 로고    scopus 로고
    • A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei
    • Alibu VP, Storm L, Haile S, Clayton C, Horn D. A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei. Mol Biochem Parasitol 2005;139:75-82.
    • (2005) Mol Biochem Parasitol , vol.139 , pp. 75-82
    • Alibu, V.P.1    Storm, L.2    Haile, S.3    Clayton, C.4    Horn, D.5
  • 2
    • 47949091926 scopus 로고    scopus 로고
    • Single-locus targeting constructs for reliable regulated RNAi and transgene expression in Trypanosoma brucei
    • Alsford S, Horn D. Single-locus targeting constructs for reliable regulated RNAi and transgene expression in Trypanosoma brucei. Mol Biochem Parasitol 2008;161:76-9.
    • (2008) Mol Biochem Parasitol , vol.161 , pp. 76-79
    • Alsford, S.1    Horn, D.2
  • 3
    • 27644517022 scopus 로고    scopus 로고
    • Tagging a T. brucei RRNA locus improves stable transfection efficiency and circumvents inducible expression position effects
    • Alsford S, Kawahara T, Glover L, Horn D. Tagging a T. brucei RRNA locus improves stable transfection efficiency and circumvents inducible expression position effects. Mol Biochem Parasitol 2005;144:142-8.
    • (2005) Mol Biochem Parasitol , vol.144 , pp. 142-148
    • Alsford, S.1    Kawahara, T.2    Glover, L.3    Horn, D.4
  • 4
    • 79955602637 scopus 로고    scopus 로고
    • High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome
    • Alsford S, Turner DJ, Obado SO, Sanchez-Flores A, Glover L, Berriman M, et al. High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome. Genome Res 2011;21:915-24.
    • (2011) Genome Res , vol.21 , pp. 915-924
    • Alsford, S.1    Turner, D.J.2    Obado, S.O.3    Sanchez-Flores, A.4    Glover, L.5    Berriman, M.6
  • 5
    • 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 ER, Blatch GL. The Hsp40 proteins of Plasmodium falciparum and other apicomplexa regulating chaperone power in the parasite and the host. Int J Biochem Cell Biol 2007;39:1781-803.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1781-1803
    • Botha, M.1    Pesce, E.R.2    Blatch, G.L.3
  • 6
    • 84897001801 scopus 로고    scopus 로고
    • Investigating the chaperone properties of a novel heat shock protein, Hsp70.C, from Trypanosoma brucei
    • Burger A, Ludewig MH, Boshoff A. Investigating the chaperone properties of a novel heat shock protein, Hsp70.c, from Trypanosoma brucei. J Parasitol Res 2014;2014,172582.
    • (2014) J Parasitol Res , vol.2014 , pp. 172582
    • Burger, A.1    Ludewig, M.H.2    Boshoff, A.3
  • 8
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham ME, Caplan AJ. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 1998;3:26-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 26-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 9
    • 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 AL, Ludewig MH, Blatch GL. 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;36:1585-98.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1585-1598
    • Edkins, A.L.1    Ludewig, M.H.2    Blatch, G.L.3
  • 11
    • 34250351297 scopus 로고    scopus 로고
    • A postgenomic view of the heat shock proteins in kinetoplastids
    • Folgueira C, Requena JM. A postgenomic view of the heat shock proteins in kinetoplastids. FEMS Microbiol Rev 2007;4:359-77.
    • (2007) FEMS Microbiol Rev , vol.4 , pp. 359-377
    • Folgueira, C.1    Requena, J.M.2
  • 12
    • 57649137959 scopus 로고    scopus 로고
    • Role of protein translocation pathways across the endoplasmic reticulum in Trypanosoma brucei
    • Goldshmidt 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;283:32085-98.
    • (2008) J Biol Chem , vol.283 , pp. 32085-32098
    • Goldshmidt, H.1    Sheiner, L.2    Bütikofer, P.3    Roditi, I.4    Uliel, S.5    Günzel, M.6
  • 13
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 2009;16:574-81.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 14
    • 22344447035 scopus 로고    scopus 로고
    • Not all J domains are created equal: Implication for the specificity of Hsp40-Hsp70 interactions
    • Hennessy F, Nicoll WS, Zimmermann R, Cheetham ME, Blatch GL. Not all J domains are created equal: implication for the specificity of Hsp40-Hsp70 interactions. Protein Sci 2005;14:1697-709.
    • (2005) Protein Sci , vol.14 , pp. 1697-1709
    • Hennessy, F.1    Nicoll, W.S.2    Zimmermann, R.3    Cheetham, M.E.4    Blatch, G.L.5
  • 15
    • 0028009258 scopus 로고
    • Axenic culture of African trypanosome bloodstream forms
    • Hirumi H, Hirumi K. Axenic culture of African trypanosome bloodstream forms. Parasitol Today 1994;10:80-4.
    • (1994) Parasitol Today , vol.10 , pp. 80-84
    • Hirumi, H.1    Hirumi, K.2
  • 16
    • 0024948840 scopus 로고
    • Continuous cultivation of Trypanosoma brucei bloodstream forms in a medium containing a low concentration of serum-protein without feeder cell layers
    • Hirumi H, Hirumi K. Continuous cultivation of Trypanosoma brucei bloodstream forms in a medium containing a low concentration of serum-protein without feeder cell layers. J Parasitol 1989;75:985-9.
    • (1989) J Parasitol , vol.75 , pp. 985-989
    • Hirumi, H.1    Hirumi, K.2
  • 17
    • 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 JM, et al. Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei. Proteomics 2006;6:259-67.
    • (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
  • 18
    • 77954947810 scopus 로고    scopus 로고
    • The Hsp70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA. The Hsp70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 2010;11:579-92.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 21
    • 0037995501 scopus 로고    scopus 로고
    • Structure and energetics of an allele-specific interaction between dnaJ and dnaK: Correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK
    • Landry SJ. Structure and energetics of an allele-specific interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. Biochemistry 2003;42:4926-36.
    • (2003) Biochemistry , vol.42 , pp. 4926-4936
    • Landry, S.J.1
  • 23
    • 70449524433 scopus 로고    scopus 로고
    • Overproduction, purification and characterisation of Tbj1, a novel Type III Hsp40 from Trypanosoma brucei, the African sleeping sickness parasite
    • Louw CA, Ludewig MH, Blatch GL. Overproduction, purification and characterisation of Tbj1, a novel Type III Hsp40 from Trypanosoma brucei, the African sleeping sickness parasite. Protein Expr Purif 2010b;69:168-77.
    • (2010) Protein Expr Purif , vol.69 , pp. 168-177
    • Louw, C.A.1    Ludewig, M.H.2    Blatch, G.L.3
  • 24
    • 77958456516 scopus 로고    scopus 로고
    • The Hsp70 chaperones of the Tritryps are characterised by unusual features and novel members
    • Louw CA, Ludewig MH, Mayer J, Blatch GL. The Hsp70 chaperones of the Tritryps are characterised by unusual features and novel members. Parasitol Int 2010a;59:497-505.
    • (2010) Parasitol Int , vol.59 , pp. 497-505
    • Louw, C.A.1    Ludewig, M.H.2    Mayer, J.3    Blatch, G.L.4
  • 25
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005;62:670-84.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 26
    • 0037466382 scopus 로고    scopus 로고
    • RNAit: An automated web-based tool for the selection of RNAi targets in Trypanosoma brucei
    • Redmond S, Vadivelu J, Field MC. RNAit: an automated web-based tool for the selection of RNAi targets in Trypanosoma brucei. Mol Biochem Parasitol 2003;128:115-8.
    • (2003) Mol Biochem Parasitol , vol.128 , pp. 115-118
    • Redmond, S.1    Vadivelu, J.2    Field, M.C.3
  • 27
    • 0031438790 scopus 로고    scopus 로고
    • Cell density triggers slender to stumpy differentiation of Trypanosoma brucei bloodstream forms in culture
    • Reuner B, Vasella E, Yutzy B, Boshart M. Cell density triggers slender to stumpy differentiation of Trypanosoma brucei bloodstream forms in culture. Mol Biochem Parasitol 1997;90:269-80.
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 269-280
    • Reuner, B.1    Vasella, E.2    Yutzy, B.3    Boshart, M.4
  • 28
    • 0035941210 scopus 로고    scopus 로고
    • 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 SA. DnaJ-like protein homologous to the yeast co-chaperone Sis1 (TcJ6p) is involved in initiation of translation in Trypanosoma cruzi. J Biol Chem 2001;276:43970-9.
    • (2001) J Biol Chem , vol.276 , pp. 43970-43979
    • Salmon, D.1    Montero-Lomeli, M.2    Goldenberg, S.A.3
  • 29
    • 79952172924 scopus 로고    scopus 로고
    • Intracellular protozoan parasites of humans: The role of molecular chaperones in development and pathogenesis
    • Shonhai A, Przyborski JM, Maier AG, Blatch GL. Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis. Protein Pept Lett 2011;18:143-57.
    • (2011) Protein Pept Lett , vol.18 , pp. 143-157
    • Shonhai, A.1    Przyborski, J.M.2    Maier, A.G.3    Blatch, G.L.4
  • 30
    • 33645059434 scopus 로고    scopus 로고
    • The evolution and diversity of kinetoplastid flagellates
    • Simpson AGB, Stevens JR, Lukes J. The evolution and diversity of kinetoplastid flagellates. Trends Parasitol 2006;22:168-74.
    • (2006) Trends Parasitol , vol.22 , pp. 168-174
    • Simpson, A.G.B.1    Stevens, J.R.2    Lukes, J.3
  • 32
    • 84896516202 scopus 로고    scopus 로고
    • Transcellular chaperone signalling: An organismal strategy for integrated cell stress response
    • van Oosten-Hawle P, Morimoto R. Transcellular chaperone signalling: an organismal strategy for integrated cell stress response. J Exp Biol 2014;217:129-36.
    • (2014) J Exp Biol , vol.217 , pp. 129-136
    • Van Oosten-Hawle, P.1    Morimoto, R.2
  • 33
    • 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 JP, Rider MH, Michels PA, Opperdoes FR. 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
  • 34
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly and translocation
    • Walsh P, Bursać D, Law YC, Cyr D, Lithgow T. The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 2004;5:567-71.
    • (2004) EMBO Rep , vol.5 , pp. 567-571
    • Walsh, P.1    Bursać, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 35
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible system for the conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei
    • Wirtz E, Leal S, Ochatt C, Cross GA. A tightly regulated inducible system for the conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei. Mol Biochem Parasitol 1999;99:89-101.
    • (1999) Mol Biochem Parasitol , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4
  • 36
    • 0030696101 scopus 로고    scopus 로고
    • Differentiation of African trypanosomes is controlled by a density sensing mechanism which signals cell cycle arrest via the cAMP pathway
    • Vasella E, Reuner B, Yutzy B, Boshart M. Differentiation of African trypanosomes is controlled by a density sensing mechanism which signals cell cycle arrest via the cAMP pathway. J Cell Sci 1997;110:2661-71.
    • (1997) J Cell Sci , vol.110 , pp. 2661-2671
    • Vasella, E.1    Reuner, B.2    Yutzy, B.3    Boshart, M.4
  • 37
    • 62549112594 scopus 로고    scopus 로고
    • A novel twist to protein secretion in eukaryotes
    • Zimmermann R, Blatch GL. A novel twist to protein secretion in eukaryotes. Trends Parasitol 2009;25:147-50.
    • (2009) Trends Parasitol , vol.25 , pp. 147-150
    • Zimmermann, R.1    Blatch, G.L.2


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