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Volumn 55, Issue 6, 2009, Pages 568-573

Thermotolerance and HSP70 expression in the Mediterranean fruit fly Ceratitis capitata

Author keywords

Hsp70 expression; Medfly; Thermotolerance

Indexed keywords

HEAT SHOCK PROTEIN 70; INSECT PROTEIN;

EID: 67349250181     PISSN: 00221910     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinsphys.2009.02.002     Document Type: Article
Times cited : (50)

References (54)
  • 1
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., and Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Molecular Cell Biology 19 (1999) 4535-4545
    • (1999) Molecular Cell Biology , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 3
    • 39749083997 scopus 로고    scopus 로고
    • Inducible and constitutive heat shock gene expression responds to modification of Hsp70 copy number in Drosophila melanogaster but does not compensate for loss of thermotolerance in Hsp70 null flies
    • Bettencourt B.R., Hogan C.C., Nimali M., and Drohan B.W. Inducible and constitutive heat shock gene expression responds to modification of Hsp70 copy number in Drosophila melanogaster but does not compensate for loss of thermotolerance in Hsp70 null flies. BMC Biology 6 (2008) 5-15
    • (2008) BMC Biology , vol.6 , pp. 5-15
    • Bettencourt, B.R.1    Hogan, C.C.2    Nimali, M.3    Drohan, B.W.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0026645957 scopus 로고
    • The consequences of expressing hsp70 in Drosophila cells at normal temperatures
    • Feder J.H., Rossi J.M., Solomon J., Solomon N., and Lindquist S. The consequences of expressing hsp70 in Drosophila cells at normal temperatures. Genes Development 6 (1992) 1402-1413
    • (1992) Genes Development , vol.6 , pp. 1402-1413
    • Feder, J.H.1    Rossi, J.M.2    Solomon, J.3    Solomon, N.4    Lindquist, S.5
  • 8
    • 0030217968 scopus 로고    scopus 로고
    • Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster
    • Feder M.E., Cartaño N.V., Milos L., Krebs R.A., and Lindquist S.L. Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster. Journal of Experimental Biology 199 (1996) 1837-1844
    • (1996) Journal of Experimental Biology , vol.199 , pp. 1837-1844
    • Feder, M.E.1    Cartaño, N.V.2    Milos, L.3    Krebs, R.A.4    Lindquist, S.L.5
  • 9
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn G.C., Pohl J., Flocco M.T., and Rothman J.E. Peptide-binding specificity of the molecular chaperone BiP. Nature 353 (1991) 726-730
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 10
    • 0033452195 scopus 로고    scopus 로고
    • Patterns of puffing activity in the salivary gland polytene chromosomes of the Medfly Ceratitis capitata, during larval and prepupal development
    • Gariou-Papalexiou A., Chrysanthis G., Mintzas A.C., and Zacharopoulou A. Patterns of puffing activity in the salivary gland polytene chromosomes of the Medfly Ceratitis capitata, during larval and prepupal development. Genome 42 (1999) 919-929
    • (1999) Genome , vol.42 , pp. 919-929
    • Gariou-Papalexiou, A.1    Chrysanthis, G.2    Mintzas, A.C.3    Zacharopoulou, A.4
  • 11
    • 8344239759 scopus 로고    scopus 로고
    • Thermal death kinetics of egg and third instar Mediterranean fruit fly (Diptera: Tephritidae)
    • Gazit Y., Rossler Y., Wang S., Tang J., and Lurie S. Thermal death kinetics of egg and third instar Mediterranean fruit fly (Diptera: Tephritidae). Journal of Economic Entomology 97 (2004) 1540-1546
    • (2004) Journal of Economic Entomology , vol.97 , pp. 1540-1546
    • Gazit, Y.1    Rossler, Y.2    Wang, S.3    Tang, J.4    Lurie, S.5
  • 12
    • 33644749260 scopus 로고    scopus 로고
    • Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration
    • Gong W.J., and Golic K.G. Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration. Genetics 172 (2006) 275-286
    • (2006) Genetics , vol.172 , pp. 275-286
    • Gong, W.J.1    Golic, K.G.2
  • 14
    • 3242733772 scopus 로고    scopus 로고
    • Heat shock proteins: to present or not, that is the question
    • Gullo C.A., and Teoh G. Heat shock proteins: to present or not, that is the question. Immunology Letter 94 (2004) 1-10
    • (2004) Immunology Letter , vol.94 , pp. 1-10
    • Gullo, C.A.1    Teoh, G.2
  • 16
    • 0001827780 scopus 로고
    • Pest status of fruit flies
    • Robinson A.S., and Hooper G.H. (Eds), Elsevier, Amsterdam
    • Harris E.J. Pest status of fruit flies. In: Robinson A.S., and Hooper G.H. (Eds). Fruit Flies: Their Biology, Natural Enemies and Control (1989), Elsevier, Amsterdam 73-81
    • (1989) Fruit Flies: Their Biology, Natural Enemies and Control , pp. 73-81
    • Harris, E.J.1
  • 17
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature 381 (1996) 571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 18
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 19
    • 0021917408 scopus 로고
    • Acquisition of the heat-shock response and thermotolerance during early development of Xenopus laevis
    • Heikkila J.J., Kloc M., Bury J., Schultz G.A., and Browder L.W. Acquisition of the heat-shock response and thermotolerance during early development of Xenopus laevis. Developmental Biology 107 (1985) 483-489
    • (1985) Developmental Biology , vol.107 , pp. 483-489
    • Heikkila, J.J.1    Kloc, M.2    Bury, J.3    Schultz, G.A.4    Browder, L.W.5
  • 20
    • 0015797002 scopus 로고
    • Preparation, molecular weight, base composition, and secondary structure of giant nuclear ribonucleic acid
    • Holmes D.S., and Bonner J. Preparation, molecular weight, base composition, and secondary structure of giant nuclear ribonucleic acid. Biochemistry 12 (1973) 2330-2338
    • (1973) Biochemistry , vol.12 , pp. 2330-2338
    • Holmes, D.S.1    Bonner, J.2
  • 21
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela M., Wissing D., Kokholm K., Kallunki T., and Egeblad M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO Journal 17 (1998) 6124-6134
    • (1998) EMBO Journal , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 22
    • 0026676855 scopus 로고
    • Heat shock proteins and thermotolerance in a cultured cell line from the Mediterranean fruit fly Ceratitis capitata.
    • Jang E.B. Heat shock proteins and thermotolerance in a cultured cell line from the Mediterranean fruit fly Ceratitis capitata. Archives of Insect Biochemistry Physiology 19 (1992) 93-103
    • (1992) Archives of Insect Biochemistry Physiology , vol.19 , pp. 93-103
    • Jang, E.B.1
  • 23
    • 0032748991 scopus 로고    scopus 로고
    • A comparison of Hsp70 expression and thermotolerance in adults and larvae of three Drosophila species
    • Krebs R.A. A comparison of Hsp70 expression and thermotolerance in adults and larvae of three Drosophila species. Cell Stress Chaperones 4 (1999) 243-249
    • (1999) Cell Stress Chaperones , vol.4 , pp. 243-249
    • Krebs, R.A.1
  • 24
    • 0030942057 scopus 로고    scopus 로고
    • Deleterious consequences of Hsp70 overexpression in Drosophila melanogaster larvae
    • Krebs R.A., and Feder M.E. Deleterious consequences of Hsp70 overexpression in Drosophila melanogaster larvae. Cell Stress Chaperones 2 (1997) 60-71
    • (1997) Cell Stress Chaperones , vol.2 , pp. 60-71
    • Krebs, R.A.1    Feder, M.E.2
  • 25
    • 0031194125 scopus 로고    scopus 로고
    • Tissue-specific variation in Hsp70 expression and thermal damage in Drosophila melanogaster larvae
    • Krebs R.A., and Feder M.E. Tissue-specific variation in Hsp70 expression and thermal damage in Drosophila melanogaster larvae. Journal of Experimental Biology 200 (1997) 2007-2015
    • (1997) Journal of Experimental Biology , vol.200 , pp. 2007-2015
    • Krebs, R.A.1    Feder, M.E.2
  • 26
    • 0032212173 scopus 로고    scopus 로고
    • Hsp70 and larval thermotolerance in Drosophila melanogater: how much is enough and when is more too much?
    • Krebs R.A., and Feder M.E. Hsp70 and larval thermotolerance in Drosophila melanogater: how much is enough and when is more too much?. Journal Insect Physiology 44 (1998) 1091-1101
    • (1998) Journal Insect Physiology , vol.44 , pp. 1091-1101
    • Krebs, R.A.1    Feder, M.E.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0029549553 scopus 로고
    • Gene transfer into the Medfly, Ceratitis capitata, using a Drosophila hydei transposable element
    • Loukeris T.G., Livadaras I., Arca B., Zabalou S., and Savakis C. Gene transfer into the Medfly, Ceratitis capitata, using a Drosophila hydei transposable element. Science 270 (1995) 2002-2007
    • (1995) Science , vol.270 , pp. 2002-2007
    • Loukeris, T.G.1    Livadaras, I.2    Arca, B.3    Zabalou, S.4    Savakis, C.5
  • 31
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: a link between the chaperone and proteasome systems
    • McDonough H., and Patterson C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8 (2003) 303-308
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 32
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., and Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Molecular Life Science 62 (2005) 670-684
    • (2005) Cell Molecular Life Science , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 34
    • 0020713524 scopus 로고
    • Translation of the mRNA encoding for the major haemolymph proteins of Ceratitis capitata in cell free system: comparison of the translatable mRNA levels to the respective biosynthetic levels of the proteins in the fat body during development
    • Mintzas A.C., Chrysanthis G., Christodoulou C., and Marmaras V.J. Translation of the mRNA encoding for the major haemolymph proteins of Ceratitis capitata in cell free system: comparison of the translatable mRNA levels to the respective biosynthetic levels of the proteins in the fat body during development. Developmental Biology 95 (1983) 492-496
    • (1983) Developmental Biology , vol.95 , pp. 492-496
    • Mintzas, A.C.1    Chrysanthis, G.2    Christodoulou, C.3    Marmaras, V.J.4
  • 35
    • 0021233951 scopus 로고
    • Altered expression of heat shock proteins in embryonal carcinoma and mouse early embryonic cells
    • Morange M., Diu A., Bensaude O., and Babinet C. Altered expression of heat shock proteins in embryonal carcinoma and mouse early embryonic cells. Molecular Cell Biology 4 (1984) 730-735
    • (1984) Molecular Cell Biology , vol.4 , pp. 730-735
    • Morange, M.1    Diu, A.2    Bensaude, O.3    Babinet, C.4
  • 36
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annual Review of Biochemistry 66 (1997) 863-917
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 863-917
    • Neupert, W.1
  • 37
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins
    • Nollen E.A., and Morimoto R.I. Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. Journal of Cell Science 115 (2002) 2809-2816
    • (2002) Journal of Cell Science , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 41
    • 0027427986 scopus 로고
    • DnaK, DnaJ GrpE form a cellular chaperone machinery caable of repairing heat-induced protein damage
    • Schroder H., Langer T., Hartl F.U., and Bukau B. DnaK, DnaJ GrpE form a cellular chaperone machinery caable of repairing heat-induced protein damage. EMBO Journal 12 (1993) 4137-4144
    • (1993) EMBO Journal , vol.12 , pp. 4137-4144
    • Schroder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 42
    • 0024988094 scopus 로고
    • The E. coli dnaK gene product, the Hsp70 homog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
    • Skowyra D., Georgopoulos C., and Zylicz M. The E. coli dnaK gene product, the Hsp70 homog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62 (1990) 939-944
    • (1990) Cell , vol.62 , pp. 939-944
    • Skowyra, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 43
    • 0025787706 scopus 로고
    • Changes in hsp70 alter thermotolerance and heat-shock regulation in Drosophila
    • Solomon J.M., Rossi J.M., Golic K., McGarry T., and Lindquist S. Changes in hsp70 alter thermotolerance and heat-shock regulation in Drosophila. The New Biologist 3 (1991) 1106-1120
    • (1991) The New Biologist , vol.3 , pp. 1106-1120
    • Solomon, J.M.1    Rossi, J.M.2    Golic, K.3    McGarry, T.4    Lindquist, S.5
  • 45
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S., Reed J.C., and Homma S. Heat-shock proteins as regulators of apoptosis. Oncogene 22 (2003) 9041-9047
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 46
    • 0032007938 scopus 로고    scopus 로고
    • A member of the hsp70 gene family from the Mediterranean fruit fly Ceratitis capitata
    • Thanaphum S., and Haymer D.S. A member of the hsp70 gene family from the Mediterranean fruit fly Ceratitis capitata. Insect Molecular Biology 7 (1998) 63-72
    • (1998) Insect Molecular Biology , vol.7 , pp. 63-72
    • Thanaphum, S.1    Haymer, D.S.2
  • 47
    • 33845608851 scopus 로고    scopus 로고
    • cDNA cloning, heat shock regulation and developmental expression of the hsp83 gene in the Mediterranean fruit fly Ceratitis capitata
    • Theodoraki M.A., and Mintzas A.C. cDNA cloning, heat shock regulation and developmental expression of the hsp83 gene in the Mediterranean fruit fly Ceratitis capitata. Insect Molecular Biology 15 (2006) 839-852
    • (2006) Insect Molecular Biology , vol.15 , pp. 839-852
    • Theodoraki, M.A.1    Mintzas, A.C.2
  • 49
    • 0020667551 scopus 로고
    • Is the major Drosophila heat shock protein present in cells that have not been heat shocked?
    • Velazquez J.M., Sonoda S., Bugaisky G., and Lindquist S. Is the major Drosophila heat shock protein present in cells that have not been heat shocked?. Journal Cell Biology 96 (1983) 286-290
    • (1983) Journal Cell Biology , vol.96 , pp. 286-290
    • Velazquez, J.M.1    Sonoda, S.2    Bugaisky, G.3    Lindquist, S.4
  • 51
    • 0032445640 scopus 로고    scopus 로고
    • Developmentally regulated nuclear transport of transcription factors in Drosophila embryos enable the heat shock response
    • Wang Z., and Lindquist S. Developmentally regulated nuclear transport of transcription factors in Drosophila embryos enable the heat shock response. Development 125 (1998) 4841-4850
    • (1998) Development , vol.125 , pp. 4841-4850
    • Wang, Z.1    Lindquist, S.2
  • 52
    • 0027144416 scopus 로고
    • A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism
    • Welte M.A., Tetrault J.M., Dellavalle R.P., and Lindquist S.L. A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism. Current Biology 3 (1993) 842-853
    • (1993) Current Biology , vol.3 , pp. 842-853
    • Welte, M.A.1    Tetrault, J.M.2    Dellavalle, R.P.3    Lindquist, S.L.4
  • 53
    • 0025323552 scopus 로고
    • Polytene chromosome maps in the medfly Ceratitis capitata
    • Zacharopoulou A. Polytene chromosome maps in the medfly Ceratitis capitata. Genome 33 (1990) 184-197
    • (1990) Genome , vol.33 , pp. 184-197
    • Zacharopoulou, A.1


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