메뉴 건너뛰기




Volumn 201, Issue 3, 1997, Pages 326-333

The 23-kDa light-stress-regulated heat-shock protein of Chenopodium rubrum L. is located in the mitochondria

Author keywords

Cell culture (plant); Chenopodium Heat shock protein (mitochondria); Mitochondrion Protein transport (in vitro)

Indexed keywords

DROSOPHILA PROTEIN; HEAT SHOCK PROTEIN; HSP23 PROTEIN, DROSOPHILA; MEMBRANE PROTEIN; VEGETABLE PROTEIN;

EID: 1842292085     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050074     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 0025796650 scopus 로고
    • Evidence for the localization of the nuclear-coded 22-kDa heat-shock protein in a subfraction of thylakoid membranes
    • Adamska I, Kloppstech K (1991) Evidence for the localization of the nuclear-coded 22-kDa heat-shock protein in a subfraction of thylakoid membranes. Eur J Biochem 198: 375-381
    • (1991) Eur J Biochem , vol.198 , pp. 375-381
    • Adamska, I.1    Kloppstech, K.2
  • 2
    • 0026262079 scopus 로고
    • Circadian oscillations of nuclear-encoded chloroplast proteins in pea (Pisum sativum)
    • Adamska I, Scheel B, Kloppstech K (1991) Circadian oscillations of nuclear-encoded chloroplast proteins in pea (Pisum sativum). Plant Mol Biol 17: 1055-1065
    • (1991) Plant Mol Biol , vol.17 , pp. 1055-1065
    • Adamska, I.1    Scheel, B.2    Kloppstech, K.3
  • 3
    • 0026603115 scopus 로고
    • Synthesis of the early light-inducible protein is controlled by blue light and related to light stress
    • Adamska I, Ohad I, Kloppstech K (1992) Synthesis of the early light-inducible protein is controlled by blue light and related to light stress. Proc Natl Acad Sci USA 89: 2610-2613
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2610-2613
    • Adamska, I.1    Ohad, I.2    Kloppstech, K.3
  • 4
    • 0016203040 scopus 로고
    • A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels
    • Bonner WM, Laskey RA (1974) A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem 64: 83-88
    • (1974) Eur J Biochem , vol.64 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 5
    • 0026610063 scopus 로고
    • 1 from potato: A protein with a presequence for targeting to the mitochondrial intermembrane space
    • 1 from potato: a protein with a presequence for targeting to the mitochondrial intermembrane space. Mol Gen Genet 231: 217-225
    • (1992) Mol Gen Genet , vol.231 , pp. 217-225
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 6
    • 0025764158 scopus 로고
    • Analysis of conserved domains identifies an unique structural feature of a chloroplast heat shock protein
    • Chen Q, Vierling E (1991) Analysis of conserved domains identifies an unique structural feature of a chloroplast heat shock protein. Mol Gen Genet 226: 425-431
    • (1991) Mol Gen Genet , vol.226 , pp. 425-431
    • Chen, Q.1    Vierling, E.2
  • 7
    • 0000155709 scopus 로고
    • Thermotolerance of isolated mitochondria associated with heat shock proteins
    • Chou M, Chen Y-M, Lin C-Y (1989) Thermotolerance of isolated mitochondria associated with heat shock proteins. Plant Physiol 89:617-621
    • (1989) Plant Physiol , vol.89 , pp. 617-621
    • Chou, M.1    Chen, Y.-M.2    Lin, C.-Y.3
  • 8
    • 0008690575 scopus 로고
    • Intracellular localization of heat shock proteins in maize
    • Cooper P, Ho THD (1987) Intracellular localization of heat shock proteins in maize. Plant Physiol 84: 1197-1203
    • (1987) Plant Physiol , vol.84 , pp. 1197-1203
    • Cooper, P.1    Ho, T.H.D.2
  • 9
    • 0028083341 scopus 로고
    • Accumulation of plastid HSP23 of Chenopodium rubrum is controlled post-translationally by light
    • Debel K, Knack G, Kloppstech K (1994) Accumulation of plastid HSP23 of Chenopodium rubrum is controlled post-translationally by light. Plant J 6: 79-85
    • (1994) Plant J , vol.6 , pp. 79-85
    • Debel, K.1    Knack, G.2    Kloppstech, K.3
  • 10
    • 0008820952 scopus 로고
    • Light stress: Its effect on the expression of small organellar heat-shock proteins. Clues as to their function?
    • Leigh RA, Blake-Kalff MMAM (eds) Salsomaggiore, Italy, 21-23 September 1995
    • Debel K, Eberhard D, Kloppstech K (1995) Light stress: its effect on the expression of small organellar heat-shock proteins. Clues as to their function? In: Leigh RA, Blake-Kalff MMAM (eds) Proceedings of the second STRESSNET conference, Salsomaggiore, Italy, 21-23 September 1995, pp 29-34
    • (1995) Proceedings of the Second STRESSNET Conference , pp. 29-34
    • Debel, K.1    Eberhard, D.2    Kloppstech, K.3
  • 11
    • 77957088304 scopus 로고
    • Isolation of plant mitochondria: General principles and criteria of integrity
    • Douce R, Bourguignon J, Brouquisse R, Neuburger M (1987) Isolation of plant mitochondria: general principles and criteria of integrity. Methods Enzymol 148: 403-409
    • (1987) Methods Enzymol , vol.148 , pp. 403-409
    • Douce, R.1    Bourguignon, J.2    Brouquisse, R.3    Neuburger, M.4
  • 12
    • 77954849936 scopus 로고
    • Photoautotrophic growth and photosynthesis in cell suspension cultures of Chenopodium rubrum
    • Hüsemann W, Barz W (1977) Photoautotrophic growth and photosynthesis in cell suspension cultures of Chenopodium rubrum. Physiol Plant 40: 77-81
    • (1977) Physiol Plant , vol.40 , pp. 77-81
    • Hüsemann, W.1    Barz, W.2
  • 13
    • 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
  • 15
    • 0001480444 scopus 로고
    • Synthesis, transport and localisation of a nuclear coded 22-kDa heatshock protein in chloroplast membranes of peas and Chlamydomanas reinhardii
    • Kloppstech K, Meyer G, Schuster G (1985) Synthesis, transport and localisation of a nuclear coded 22-kDa heatshock protein in chloroplast membranes of peas and Chlamydomanas reinhardii. EMBO J 4: 1901-1909
    • (1985) EMBO J , vol.4 , pp. 1901-1909
    • Kloppstech, K.1    Meyer, G.2    Schuster, G.3
  • 16
    • 0024967185 scopus 로고
    • cDNA sequence of a heat-inducible protein of Chenopodium rubrum sharing little homology with other heat-shock proteins
    • Knack G, Kloppstech K (1989) cDNA sequence of a heat-inducible protein of Chenopodium rubrum sharing little homology with other heat-shock proteins. Nucleic Acids Res 17: 5380
    • (1989) Nucleic Acids Res , vol.17 , pp. 5380
    • Knack, G.1    Kloppstech, K.2
  • 17
    • 0011650103 scopus 로고
    • The heat shock response in a photoautotrophic cell culture of Chenopodium rubrum: The effects of temperature and light
    • Knack G, Kloppstech K (1992) The heat shock response in a photoautotrophic cell culture of Chenopodium rubrum: the effects of temperature and light. J Plant Physiol 140: 489-493
    • (1992) J Plant Physiol , vol.140 , pp. 489-493
    • Knack, G.1    Kloppstech, K.2
  • 18
    • 0026464992 scopus 로고
    • Low molecular mass heat-shock proteins of a light-resistant photoautotrophic cell culture
    • Knack G, Liu Z, Kloppstech K (1992) Low molecular mass heat-shock proteins of a light-resistant photoautotrophic cell culture. Eur J Cell Biol 59: 166-175
    • (1992) Eur J Cell Biol , vol.59 , pp. 166-175
    • Knack, G.1    Liu, Z.2    Kloppstech, K.3
  • 19
    • 1842359289 scopus 로고
    • Heat shock proteins in plants: An approach to understanding the function of plastid heatshock proteins
    • Barber J (ed) Elsevier Science Publishers B V, Amsterdam
    • Kruse E, Kloppstech K (1992) Heat shock proteins in plants: an approach to understanding the function of plastid heatshock proteins. In: Barber J (ed) Topics in photosynthesis, vol 1. Elsevier Science Publishers B V, Amsterdam, pp 409-442
    • (1992) Topics in Photosynthesis , vol.1 , pp. 409-442
    • Kruse, E.1    Kloppstech, K.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0030039706 scopus 로고    scopus 로고
    • Molecular characterization of cDNA encoding low molecular-weight heatshock proteins of soybean
    • LaFayette PR, Nagao RT, O'Grady K, Vierling E, Key JL (1996) Molecular characterization of cDNA encoding low molecular-weight heatshock proteins of soybean. Plant Mol Biol 30: 159-169
    • (1996) Plant Mol Biol , vol.30 , pp. 159-169
    • LaFayette, P.R.1    Nagao, R.T.2    O'Grady, K.3    Vierling, E.4    Key, J.L.5
  • 22
    • 0028002821 scopus 로고
    • A low molecular mass heat-shock protein is localized to higher plant mitochondria
    • Lenne C, Douce R (1994) A low molecular mass heat-shock protein is localized to higher plant mitochondria. Plant Physiol 105: 1255-1261
    • (1994) Plant Physiol , vol.105 , pp. 1255-1261
    • Lenne, C.1    Douce, R.2
  • 23
    • 0028822440 scopus 로고
    • Sequence and expression of the mRNA encoding HSP22 the mitochondrial small heat-shock protein in pea leaves
    • Lenne C, Block MA, Garin J, Douce R (1995) Sequence and expression of the mRNA encoding HSP22 the mitochondrial small heat-shock protein in pea leaves. Biochem J 311: 805-813
    • (1995) Biochem J , vol.311 , pp. 805-813
    • Lenne, C.1    Block, M.A.2    Garin, J.3    Douce, R.4
  • 25
    • 0015240315 scopus 로고
    • Molecular weight determination of protein-dodecylsulfate complexes by electrophoresis in a discontinuous buffer system
    • Neville DM (1971) Molecular weight determination of protein-dodecylsulfate complexes by electrophoresis in a discontinuous buffer system. J Biol Chem 246: 6328-6334
    • (1971) J Biol Chem , vol.246 , pp. 6328-6334
    • Neville, D.M.1
  • 26
    • 0029793563 scopus 로고    scopus 로고
    • The expression of mRNA for light stress proteins in barley: Inverse relationship of mRNA levels of individual genes within the leaf gradient
    • Pötter E, Beator J, Kloppstech K (1996) The expression of mRNA for light stress proteins in barley: inverse relationship of mRNA levels of individual genes within the leaf gradient. Planta 199: 314-320
    • (1996) Planta , vol.199 , pp. 314-320
    • Pötter, E.1    Beator, J.2    Kloppstech, K.3
  • 27
    • 0002003584 scopus 로고
    • Evidence for protection by heat-shock proteins against photoinhibition during heat-shock
    • Schuster G, Even D, Kloppstech K, Ohad I (1988) Evidence for protection by heat-shock proteins against photoinhibition during heat-shock. EMBO J 7: 1-6
    • (1988) EMBO J , vol.7 , pp. 1-6
    • Schuster, G.1    Even, D.2    Kloppstech, K.3    Ohad, I.4
  • 28
    • 0026686662 scopus 로고
    • Immunogold labelling of the cytoplasmic estradiol receptor in resting porcine endometrium
    • Sierralta WD, Thole HH (1992) Immunogold labelling of the cytoplasmic estradiol receptor in resting porcine endometrium. Cell Tiss Res 270: 1-6
    • (1992) Cell Tiss Res , vol.270 , pp. 1-6
    • Sierralta, W.D.1    Thole, H.H.2
  • 29
    • 0001575537 scopus 로고
    • Proteins associated with the adaptation of cultured tobacco cells to NaCl
    • Singh NK, Handa AK, Hasegawa PM, Bressan RA (1985) Proteins associated with the adaptation of cultured tobacco cells to NaCl. Plant Physiol 79: 126-137
    • (1985) Plant Physiol , vol.79 , pp. 126-137
    • Singh, N.K.1    Handa, A.K.2    Hasegawa, P.M.3    Bressan, R.A.4
  • 30
    • 0014444144 scopus 로고
    • A low viscosity resin-embedding medium for electron microscopy
    • Spurr AR (1969) A low viscosity resin-embedding medium for electron microscopy. J Ultrastruct Res 26: 31-43
    • (1969) J Ultrastruct Res , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 31
    • 0027137815 scopus 로고
    • The protective effect of heat-shock proteins against photoinhibition under heat shock in barley (Hordeum vulgare)
    • Stapel D, Kruse E, Kloppstech K (1993) The protective effect of heat-shock proteins against photoinhibition under heat shock in barley (Hordeum vulgare). J Photochem Photobiol B: Biol 21: 211-218
    • (1993) J Photochem Photobiol B: Biol , vol.21 , pp. 211-218
    • Stapel, D.1    Kruse, E.2    Kloppstech, K.3
  • 33
    • 84995108088 scopus 로고
    • Photorespiration is more effective than the Mehler reaction in protecting the photosynthetic apparatus against photoinhibition
    • Wu J, Neimanis S, Heber U (1991) Photorespiration is more effective than the Mehler reaction in protecting the photosynthetic apparatus against photoinhibition. Bot Acta 104: 283-291
    • (1991) Bot Acta , vol.104 , pp. 283-291
    • Wu, J.1    Neimanis, S.2    Heber, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.