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Volumn 120, Issue 2, 1999, Pages 521-528

Heterologous expression of a plant small heat-shock protein enhances Escherichia coli viability under heat and cold stress

Author keywords

[No Author keywords available]

Indexed keywords

AUTOLYSIS; COMPLEMENTARY DNA; CYTOSOL; GENE OVEREXPRESSION; HEAT SHOCK; HEAT SHOCK PROTEIN; HETEROLOGOUS PRODUCT; IMMUNOELECTRON MICROSCOPY; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; RECOMBINANT PROTEIN; SALT STRESS; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS; SURVIVAL;

EID: 0033150267     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.120.2.521     Document Type: Article
Times cited : (146)

References (40)
  • 1
    • 0026903505 scopus 로고
    • Developmental and environmental concurrent expression of sunflower dry-seed-stored low-molecular heat-shock protein and Lea mRNAs
    • Almoguera C, Jordano J (1992) Developmental and environmental concurrent expression of sunflower dry-seed-stored low-molecular heat-shock protein and Lea mRNAs. Plant Mol Biol 19: 781-792
    • (1992) Plant Mol Biol , vol.19 , pp. 781-792
    • Almoguera, C.1    Jordano, J.2
  • 2
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston RS, Viitanen PV, Vierling E (1996) Molecular chaperones and protein folding in plants. Plant Mol Biol 32: 191-222
    • (1996) Plant Mol Biol , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 3
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner J (1996) Supervising the fold: functional principles of molecular chaperones. FASEB J 10: 10-19
    • (1996) FASEB J , vol.10 , pp. 10-19
    • Buchner, J.1
  • 4
    • 0030829559 scopus 로고    scopus 로고
    • A plant small heat shock protein gene expressed during zygotic embryogenesis but noninducible by heat stress
    • Carrasco R, Almoguera C, Jordano J (1997) A plant small heat shock protein gene expressed during zygotic embryogenesis but noninducible by heat stress. J Biol Chem 272: 27470-27475
    • (1997) J Biol Chem , vol.272 , pp. 27470-27475
    • Carrasco, R.1    Almoguera, C.2    Jordano, J.3
  • 5
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang S, Puryear J, Cairney J (1993) A simple and efficient method for isolating RNA from pine trees. Plant Mol Biol Rep 11: 113-116
    • (1993) Plant Mol Biol Rep , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 6
    • 0028448479 scopus 로고
    • Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: Localization and possible functional implications
    • Coca MA, Almoguera C, Jordano J (1994) Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: localization and possible functional implications. Plant Mol Biol 25: 479-492
    • (1994) Plant Mol Biol , vol.25 , pp. 479-492
    • Coca, M.A.1    Almoguera, C.2    Jordano, J.3
  • 7
    • 3543024452 scopus 로고    scopus 로고
    • Purification and in vitro chaperone activity of a class I small heat-shock protein abundant in recalcitrant chestnut seeds
    • Collada C, Gomez L, Casado R, Aragoncillo C (1997) Purification and in vitro chaperone activity of a class I small heat-shock protein abundant in recalcitrant chestnut seeds. Plant Physiol 115: 71-77
    • (1997) Plant Physiol , vol.115 , pp. 71-77
    • Collada, C.1    Gomez, L.2    Casado, R.3    Aragoncillo, C.4
  • 8
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig EA, Gambill BD, Nelson RJ (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57: 402-414
    • (1993) Microbiol Rev , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 9
    • 0027947292 scopus 로고
    • Developmental control of small heat shock protein expression during pea seed maturation
    • DeRocher AE, Vierling E (1994) Developmental control of small heat shock protein expression during pea seed maturation. Plant J 5: 93-102
    • (1994) Plant J , vol.5 , pp. 93-102
    • Derocher, A.E.1    Vierling, E.2
  • 10
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Gräber S, Gaestel M, Buchner J (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 16: 221-229
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 11
    • 0031432208 scopus 로고    scopus 로고
    • Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo
    • Forreiter C, Kirschner M, Nover L (1997) Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo. Plant Cell 9: 2171-2181
    • (1997) Plant Cell , vol.9 , pp. 2171-2181
    • Forreiter, C.1    Kirschner, M.2    Nover, L.3
  • 13
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 14
    • 0000052340 scopus 로고
    • Expression of low molecular weight heat shock proteins under field conditions
    • Hernández LD, Vierling E (1993) Expression of low molecular weight heat shock proteins under field conditions. Plant Physiol 101: 1209-1216
    • (1993) Plant Physiol , vol.101 , pp. 1209-1216
    • Hernández, L.D.1    Vierling, E.2
  • 16
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz J (1992) α-Crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 89: 10449-10453
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 17
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K, Buchner J (1993) Small heat shock proteins are molecular chaperones. J Biol Chem 268: 1517-1520
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 18
    • 0028859629 scopus 로고
    • Characterization and physiological function of class I low-molecular-mass, heat-shock protein complex in soybean
    • Jinn TL, Chen YM, Lin CY (1995) Characterization and physiological function of class I low-molecular-mass, heat-shock protein complex in soybean. Plant Physiol 108: 693-701
    • (1995) Plant Physiol , vol.108 , pp. 693-701
    • Jinn, T.L.1    Chen, Y.M.2    Lin, C.Y.3
  • 19
    • 0001755774 scopus 로고
    • Stabilization of soluble proteins in vitro by heat shock proteins-enriched ammonium sulfate fraction from soybean seedlings
    • Jinn TL, Yeh YC, Chen YM, Lin CY (1989) Stabilization of soluble proteins in vitro by heat shock proteins-enriched ammonium sulfate fraction from soybean seedlings. Plant Cell Physiol 30: 463-469
    • (1989) Plant Cell Physiol , vol.30 , pp. 463-469
    • Jinn, T.L.1    Yeh, Y.C.2    Chen, Y.M.3    Lin, C.Y.4
  • 20
    • 0030942271 scopus 로고    scopus 로고
    • Molecular characterization of the gene encoding an 18-kDa small heat shock protein associated with the membrane of Leuconostoc oenos
    • Jobin MP, Delmas F, Garmyn D, Diviès D, Guzzo J (1997) Molecular characterization of the gene encoding an 18-kDa small heat shock protein associated with the membrane of Leuconostoc oenos. Appl Environ Microbiol 63: 609-614
    • (1997) Appl Environ Microbiol , vol.63 , pp. 609-614
    • Jobin, M.P.1    Delmas, F.2    Garmyn, D.3    Diviès, D.4    Guzzo, J.5
  • 21
    • 0032055785 scopus 로고    scopus 로고
    • Molecular cloning of a novel heat induced/chilling tolerance related cDNA in tomato fruit by use of mRNA differential display
    • Kadyrzhanova DK, Vlachonasios KE, Ververidis P, Dilley DR (1998) Molecular cloning of a novel heat induced/chilling tolerance related cDNA in tomato fruit by use of mRNA differential display. Plant Mol Biol 36: 885-895
    • (1998) Plant Mol Biol , vol.36 , pp. 885-895
    • Kadyrzhanova, D.K.1    Vlachonasios, K.E.2    Ververidis, P.3    Dilley, D.R.4
  • 22
    • 0030973119 scopus 로고    scopus 로고
    • Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures
    • Kandror O, Goldberg AL (1997) Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures. Proc Natl Acad Sci USA 94: 4978-4981
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4978-4981
    • Kandror, O.1    Goldberg, A.L.2
  • 23
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee GJ, Pokala N, Vierling E (1995) Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J Biol Chem 270: 10432-10438
    • (1995) J Biol Chem , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 24
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee GJ, Roseman AM, Saibil HR, Vierling E (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 16: 659-671
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 25
    • 0000340653 scopus 로고
    • Acquisition of low temperature tolerance in tomatoes by exposure to high temperature stress
    • Lurie S, Klein JD (1991) Acquisition of low temperature tolerance in tomatoes by exposure to high temperature stress. J Am Soc Hortic Sci 116: 1007-1012
    • (1991) J Am Soc Hortic Sci , vol.116 , pp. 1007-1012
    • Lurie, S.1    Klein, J.D.2
  • 27
    • 0028813168 scopus 로고
    • Immersion of cucumber fruit in heated water alters chilling-induced physiological changes
    • McCollum TG, Doostdar H, Mayer RT, McDonald RE (1995) Immersion of cucumber fruit in heated water alters chilling-induced physiological changes. Postharv Biol Technol 6: 55-64
    • (1995) Postharv Biol Technol , vol.6 , pp. 55-64
    • McCollum, T.G.1    Doostdar, H.2    Mayer, R.T.3    McDonald, R.E.4
  • 28
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat-shock protein human αB crystallin
    • Muchowski PJ, Clark JI (1998) ATP-enhanced molecular chaperone functions of the small heat-shock protein human αB crystallin. Proc Natl Acad Sci USA 95: 1004-1009
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 29
    • 0001199057 scopus 로고    scopus 로고
    • Heat-shock response in heat-tolerant and non-tolerant variants of Agrostis palustris Huds
    • Park SY, Shijavi R, Krans JV, Luthe DS (1996) Heat-shock response in heat-tolerant and non-tolerant variants of Agrostis palustris Huds. Plant Physiol 111: 515-524
    • (1996) Plant Physiol , vol.111 , pp. 515-524
    • Park, S.Y.1    Shijavi, R.2    Krans, J.V.3    Luthe, D.S.4
  • 30
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27: 437-496
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 32
    • 0032090396 scopus 로고    scopus 로고
    • Expression of small heat-shock proteins at low temperatures. A possible role in protecting against chilling injuries
    • Sabehat A, Lurie S, Weiss D (1998) Expression of small heat-shock proteins at low temperatures. A possible role in protecting against chilling injuries. Plant Physiol 117: 651-658
    • (1998) Plant Physiol , vol.117 , pp. 651-658
    • Sabehat, A.1    Lurie, S.2    Weiss, D.3
  • 33
    • 0030088062 scopus 로고    scopus 로고
    • The correlation between heat-shock protein accumulation and persistence and chilling tolerance in tomato fruit
    • Sabehat A, Weiss D, Lurie S (1996) The correlation between heat-shock protein accumulation and persistence and chilling tolerance in tomato fruit. Plant Physiol 110: 531-537
    • (1996) Plant Physiol , vol.110 , pp. 531-537
    • Sabehat, A.1    Weiss, D.2    Lurie, S.3
  • 34
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez Y, Lindquist S (1990) HSP104 required for induced thermotolerance. Science 248: 1112-1115
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.2
  • 36
    • 0030903748 scopus 로고    scopus 로고
    • Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
    • Török Z, Horváth I, Goloubinoff P, Kovács E, Glatz A, Balogh G, Vígh L (1997) Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc Natl Acad Sci USA 94: 2192-2197
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2192-2197
    • Török, Z.1    Horváth, I.2    Goloubinoff, P.3    Kovács, E.4    Glatz, A.5    Balogh, G.6    Vígh, L.7
  • 38
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters ER, Lee GJ, Vierling E (1996) Evolution, structure and function of the small heat shock proteins in plants. J Exp Bot 47: 325-338
    • (1996) J Exp Bot , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 39
    • 0030886055 scopus 로고    scopus 로고
    • Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance
    • Yeh CH, Chang PL, Yeh KW, Lin WC, Chen YM, Lin CY (1997) Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc Natl Acad Sci USA 94: 10967-10972
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10967-10972
    • Yeh, Ch.1    Chang, P.L.2    Yeh, K.W.3    Lin, W.C.4    Chen, Y.M.5    Lin, C.Y.6
  • 40
    • 0028836210 scopus 로고
    • Tissue-specific localization of heat-stress proteins during embryo development
    • zur Nieden U, Neumann D, Bucka A, Nover L (1995) Tissue-specific localization of heat-stress proteins during embryo development. Planta 196: 530-538
    • (1995) Planta , vol.196 , pp. 530-538
    • Zur Nieden, U.1    Neumann, D.2    Bucka, A.3    Nover, L.4


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