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Volumn 40, Issue 12, 2008, Pages 2914-2926

The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns

Author keywords

DnaJ; Heat shock proteins; Malaria; Plasmodium

Indexed keywords

HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN DNAJ; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 51249122014     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.06.011     Document Type: Article
Times cited : (51)

References (38)
  • 1
    • 0037040201 scopus 로고    scopus 로고
    • Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum
    • Banumathy G., Singh V., and Tatu U. Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum. The Journal of Biological Chemistry 277 (2002) 3902-3912
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 3902-3912
    • Banumathy, G.1    Singh, V.2    Tatu, U.3
  • 2
    • 0038381514 scopus 로고    scopus 로고
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes
    • Banumathy G., Singh V., Pavithra S.R., and Tatu U. Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. The Journal of Biological Chemistry 278 (2003) 18336-18345
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 18336-18345
    • Banumathy, G.1    Singh, V.2    Pavithra, S.R.3    Tatu, U.4
  • 3
    • 0027961010 scopus 로고
    • Enhanced expression of Plasmodium falciparum heat shock protein PFHSP70-I at higher temperatures and parasite survival
    • Biswas S., and Sharma Y.D. Enhanced expression of Plasmodium falciparum heat shock protein PFHSP70-I at higher temperatures and parasite survival. FEMS Microbiology Letters 124 (1994) 425-429
    • (1994) FEMS Microbiology Letters , vol.124 , pp. 425-429
    • Biswas, S.1    Sharma, Y.D.2
  • 4
    • 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., and Blatch G.L. The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. The International Journal of Biochemistry & Cell Biology 39 (2007) 1781-1803
    • (2007) The International Journal of Biochemistry & Cell Biology , vol.39 , pp. 1781-1803
    • Botha, M.1    Pesce, E.-R.2    Blatch, G.L.3
  • 5
    • 0032583105 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum exports the ATP-binding cassette protein PFGCN20 to membrane structures in the host red blood cell
    • Bozdech Z., VanWye J., Haldar K., and Schurr E. The human malaria parasite Plasmodium falciparum exports the ATP-binding cassette protein PFGCN20 to membrane structures in the host red blood cell. Molecular and Biochemical Parasitology 97 (1998) 81-95
    • (1998) Molecular and Biochemical Parasitology , vol.97 , pp. 81-95
    • Bozdech, Z.1    VanWye, J.2    Haldar, K.3    Schurr, E.4
  • 7
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
    • Cheetham M.E., and Caplan A.J. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress and Chaperones 3 (1998) 28-36
    • (1998) Cell Stress and Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 8
    • 0030929209 scopus 로고    scopus 로고
    • Structure-function analyses of Ssc1p, Mdj1p and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coli
    • Deloche O., Kelley W.L., and Georgopoulos C. Structure-function analyses of Ssc1p, Mdj1p and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coli. Journal of Bacteriology 179 (1997) 6066-6075
    • (1997) Journal of Bacteriology , vol.179 , pp. 6066-6075
    • Deloche, O.1    Kelley, W.L.2    Georgopoulos, C.3
  • 10
    • 0035896599 scopus 로고    scopus 로고
    • Dj1A is a third DnaK co-chaperone of Escherichia coli, and Dj1A-mediated induction of colanic acid capsule requires Dj1A-DnaK interaction
    • Genevaux P., Wawrzynów A., Zylicz M., Georgopoulos C., and Kelley W.L. Dj1A is a third DnaK co-chaperone of Escherichia coli, and Dj1A-mediated induction of colanic acid capsule requires Dj1A-DnaK interaction. The Journal of Biological Chemistry 276 (2001) 7906-7912
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 7906-7912
    • Genevaux, P.1    Wawrzynów, A.2    Zylicz, M.3    Georgopoulos, C.4    Kelley, W.L.5
  • 12
    • 0031792787 scopus 로고    scopus 로고
    • Inhibition of glutathione-dependent degradation of heme by chloroquine and amodiaquine as a possible basis for their antimalarial mode of action
    • Ginsburg H., Famin O., Zhang J., and Krugliak M. Inhibition of glutathione-dependent degradation of heme by chloroquine and amodiaquine as a possible basis for their antimalarial mode of action. Biochemical Pharmacology 56 (1998) 1305-1313
    • (1998) Biochemical Pharmacology , vol.56 , pp. 1305-1313
    • Ginsburg, H.1    Famin, O.2    Zhang, J.3    Krugliak, M.4
  • 13
    • 4644243721 scopus 로고    scopus 로고
    • Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium tumefaciens identifies amino acid residues critical to its in vivo function
    • Hennessy F., Boshoff A., and Blatch G.L. Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium tumefaciens identifies amino acid residues critical to its in vivo function. The International Journal of Biochemistry & Cell Biology 37 (2005) 177-191
    • (2005) The International Journal of Biochemistry & Cell Biology , vol.37 , pp. 177-191
    • Hennessy, F.1    Boshoff, A.2    Blatch, G.L.3
  • 14
  • 15
    • 0026714937 scopus 로고
    • Effect of heat-shock on Plasmodium falciparum viability, growth and expression of the heat-shock protein 'PFHSP70-I' gene
    • Joshi B., Biswas S., and Sharma Y.D. Effect of heat-shock on Plasmodium falciparum viability, growth and expression of the heat-shock protein 'PFHSP70-I' gene. Federation of European Biochemical Societies Letters 312 (1992) 91-94
    • (1992) Federation of European Biochemical Societies Letters , vol.312 , pp. 91-94
    • Joshi, B.1    Biswas, S.2    Sharma, Y.D.3
  • 16
    • 0030935256 scopus 로고    scopus 로고
    • The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J domain of the Escherichia coli DnaJ molecular chaperone
    • Kelley W.L., and Georgopoulos C. The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J domain of the Escherichia coli DnaJ molecular chaperone. Proceedings of the National Academy of Sciences, United States of America 94 (1997) 3679-3684
    • (1997) Proceedings of the National Academy of Sciences, United States of America , vol.94 , pp. 3679-3684
    • Kelley, W.L.1    Georgopoulos, C.2
  • 17
    • 20444405371 scopus 로고    scopus 로고
    • Proteome analysis of separated male and female gametocytes reveals novel sex-specific Plasmodium biology
    • Khan S.M., Franke-Fayard B., Mair G.R., Lasonder E., Janse C.J., Mann M., et al. Proteome analysis of separated male and female gametocytes reveals novel sex-specific Plasmodium biology. Cell 121 (2005) 675-687
    • (2005) Cell , vol.121 , pp. 675-687
    • Khan, S.M.1    Franke-Fayard, B.2    Mair, G.R.3    Lasonder, E.4    Janse, C.J.5    Mann, M.6
  • 18
    • 0347122968 scopus 로고    scopus 로고
    • Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
    • Klemba M., Beatty W., Gluzman I., and Goldberg D.E. Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum. The Journal of Cell Biology 164 (2004) 47-56
    • (2004) The Journal of Cell Biology , vol.164 , pp. 47-56
    • Klemba, M.1    Beatty, W.2    Gluzman, I.3    Goldberg, D.E.4
  • 19
    • 0025743647 scopus 로고
    • Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family
    • Kumar N., Koski G., Harada M., Aikawa M., and Zheng H. Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family. Molecular and Biochemical Parasitology 48 (1991) 47-58
    • (1991) Molecular and Biochemical Parasitology , vol.48 , pp. 47-58
    • Kumar, N.1    Koski, G.2    Harada, M.3    Aikawa, M.4    Zheng, H.5
  • 22
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti M., Good R.T., Rug M., Knuepfer E., and Cowman A.F. Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science 306 (2004) 1930-1933
    • (2004) Science , vol.306 , pp. 1930-1933
    • Marti, M.1    Good, R.T.2    Rug, M.3    Knuepfer, E.4    Cowman, A.F.5
  • 23
    • 0033020519 scopus 로고    scopus 로고
    • Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy
    • Mayer M.P., Laufen T., Paal K., McCarty J.S., and Bukau B. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. Journal of Molecular Biology 289 (1999) 1131-1144
    • (1999) Journal of Molecular Biology , vol.289 , pp. 1131-1144
    • Mayer, M.P.1    Laufen, T.2    Paal, K.3    McCarty, J.S.4    Bukau, B.5
  • 24
    • 0042527130 scopus 로고    scopus 로고
    • Heat shock protein 70 stimulation of the deoxyribonucleic acid base excision repair enzyme polymerase β
    • Mendez F., Kozin E., and Bases R. Heat shock protein 70 stimulation of the deoxyribonucleic acid base excision repair enzyme polymerase β. Cell Stress and Chaperones 8 (2003) 153-161
    • (2003) Cell Stress and Chaperones , vol.8 , pp. 153-161
    • Mendez, F.1    Kozin, E.2    Bases, R.3
  • 27
    • 33645090922 scopus 로고    scopus 로고
    • Proteases and chaperones are the most abundant proteins in the parasitophorous vacuole of Plasmodium falciparum-infected erythrocytes
    • Nyalwidhe J., and Lingelbach K. Proteases and chaperones are the most abundant proteins in the parasitophorous vacuole of Plasmodium falciparum-infected erythrocytes. Proteomics 6 (2006) 1563-1573
    • (2006) Proteomics , vol.6 , pp. 1563-1573
    • Nyalwidhe, J.1    Lingelbach, K.2
  • 29
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • Rüdiger S., Schneider-Mergener J., and Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. The European Molecular Biology Organisation Journal 20 (2001) 1042-1050
    • (2001) The European Molecular Biology Organisation Journal , vol.20 , pp. 1042-1050
    • Rüdiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 31
    • 20744437430 scopus 로고    scopus 로고
    • The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity
    • Shi Y.Y., Hong X.G., and Wang C.C. The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity. The Journal of Biological Chemistry 280 (2005) 22761-22768
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 22761-22768
    • Shi, Y.Y.1    Hong, X.G.2    Wang, C.C.3
  • 32
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai J., and Douglas M.G. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. The Journal of Biological Chemistry 271 (1996) 9347-9354
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 33
    • 0029001571 scopus 로고
    • GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the elF-2 alpha kinase GCN2 in amino acid starved cells
    • Vazquez de Aldana C.R., Marton M.J., and Hinnebusch A.G. GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the elF-2 alpha kinase GCN2 in amino acid starved cells. The European Molecular Biology Organisation Journal 14 (1995) 3184-3199
    • (1995) The European Molecular Biology Organisation Journal , vol.14 , pp. 3184-3199
    • Vazquez de Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 34
    • 16244400417 scopus 로고    scopus 로고
    • Proteomic analysis identifies novel proteins of the Maurer's Clefts, a secretory compartment delivering Plasmodium falciparum proteins to the surface of its host cell
    • Vincensini L., Richert S., Blisnick T., Van Dorsselaer A., Leize-Wagner E., Rabilloud T., et al. Proteomic analysis identifies novel proteins of the Maurer's Clefts, a secretory compartment delivering Plasmodium falciparum proteins to the surface of its host cell. Molecular and Cellular Proteomics 4 (2005) 582-593
    • (2005) Molecular and Cellular Proteomics , vol.4 , pp. 582-593
    • Vincensini, L.1    Richert, S.2    Blisnick, T.3    Van Dorsselaer, A.4    Leize-Wagner, E.5    Rabilloud, T.6
  • 36
    • 0030871598 scopus 로고    scopus 로고
    • Cloning and characterization of heat shock protein DnaJ homologues from Plasmodium falciparum and comparison with ring infected erythrocyte surface antigen
    • Watanabe J. Cloning and characterization of heat shock protein DnaJ homologues from Plasmodium falciparum and comparison with ring infected erythrocyte surface antigen. Molecular and Biochemical Parasitology 88 (1997) 253-258
    • (1997) Molecular and Biochemical Parasitology , vol.88 , pp. 253-258
    • Watanabe, J.1
  • 37
    • 0038523841 scopus 로고    scopus 로고
    • The J domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70
    • Wittung-Stafshede P., Guidry J., Horne B.E., and Landry S.J. The J domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Biochemistry 42 (2003) 4937-4944
    • (2003) Biochemistry , vol.42 , pp. 4937-4944
    • Wittung-Stafshede, P.1    Guidry, J.2    Horne, B.E.3    Landry, S.J.4
  • 38
    • 0032694248 scopus 로고    scopus 로고
    • The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1
    • Yan W., and Craig E.A. The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Molecular and Cellular Biology 19 (1999) 7751-7758
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 7751-7758
    • Yan, W.1    Craig, E.A.2


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