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Volumn 45, Issue 3, 2010, Pages 469-474

DcHsp17.7, a small heat shock protein from carrot, is upregulated under cold stress and enhances cold tolerance by functioning as a molecular chaperone

Author keywords

Cold stress; Daucus carota l.; Heat shock protein; Molecular chaperone; Oligomeric complex

Indexed keywords

DAUCUS CAROTA; ESCHERICHIA COLI;

EID: 77950450826     PISSN: 00185345     EISSN: None     Source Type: Journal    
DOI: 10.21273/hortsci.45.3.469     Document Type: Article
Times cited : (18)

References (20)
  • 1
    • 1542351305 scopus 로고    scopus 로고
    • Genotypic differences in the heat-shock response and thermotolerance in four potato cultivars
    • Ahn, Y.-J., K. Claussen, and J.L. Zimmerman. 2004. Genotypic differences in the heat-shock response and thermotolerance in four potato cultivars. Plant Sci. 166:901-911.
    • (2004) Plant Sci , vol.166 , pp. 901-911
    • Ahn, Y.-J.1    Claussen, K.2    Zimmerman, J.L.3
  • 2
    • 33645088178 scopus 로고    scopus 로고
    • Introduction of the carrot HSP17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro
    • Ahn, Y.-J. and J.L. Zimmerman. 2006. Introduction of the carrot HSP17.7 into potato (Solanum tuberosum L.) enhances cellular membrane stability and tuberization in vitro. Plant Cell Environ. 29:95-104.
    • (2006) Plant Cell Environ , vol.29 , pp. 95-104
    • Ahn, Y.-J.1    Zimmerman, J.L.2
  • 3
    • 0017184389 scopus 로고
    • Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0028448479 scopus 로고
    • Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: Localization and possible functional implications. Plant Mol
    • Coca, M.A., C. Almoguera, and J. Jordano. 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) Biol , vol.25 , pp. 479-492
    • Coca, M.A.1    Almoguera, C.2    Jordano, J.3
  • 5
    • 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., M. Kirschner, and L. Nover. 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
  • 6
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • Haslbeck, M., T. Franzmann, D. Weinfurtner, and J. Buchner. 2005. Some like it hot: The structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12:842-846.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 7
    • 67650433353 scopus 로고    scopus 로고
    • A cytosolic class I small heat shock protein, RcHSP17.8, of Rosa chinensis confers resistance to a variety of stresses to Escherichia coli, yeast and Arabidopsis thaliana
    • Jiang, C., J. Xu, H. Zhang, X. Zhang, J. Shi, M. Li, and F. Ming. 2009. A cytosolic class I small heat shock protein, RcHSP17.8, of Rosa chinensis confers resistance to a variety of stresses to Escherichia coli, yeast and Arabidopsis thaliana. Plant Cell Environ. 32:1046-1059.
    • (2009) Plant Cell Environ , vol.32 , pp. 1046-1059
    • Jiang, C.1    Xu, J.2    Zhang, H.3    Zhang, X.4    Shi, J.5    Li, M.6    Ming, F.7
  • 8
    • 0043133626 scopus 로고    scopus 로고
    • Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis
    • Kang, L.W., S.B. Gabelli, J.E. Cunningham, S.F. O'Handley, and L.M. Amzel. 2003. Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis. Structure 11:1015-1023.
    • (2003) Structure , vol.11 , pp. 1015-1023
    • Kang, L.W.1    Gabelli, S.B.2    Cunningham, J.E.3    O'Handley, S.F.4    Amzel, L.M.5
  • 9
    • 67650792991 scopus 로고    scopus 로고
    • Expression of a gene encoding the carrot HSP17.7 in Escherichia coli enhances cell viability and protein solubility under heat stress
    • Kim, H. and Y.-J. Ahn. 2009. Expression of a gene encoding the carrot HSP17.7 in Escherichia coli enhances cell viability and protein solubility under heat stress. HortScience 44:866-869.
    • (2009) HortScience , vol.44 , pp. 866-869
    • Kim, H.1    Ahn, Y.-J.2
  • 10
    • 0028949832 scopus 로고
    • Structural and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee, G.J., N. Pokala, and E. Vierling. 1995. Structural 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
  • 11
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a foldingcompetent state
    • Lee, G.J., A.M. Roseman, H.R. Saibil, and E. Vierling. 1997. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a foldingcompetent 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
  • 12
    • 1942533519 scopus 로고    scopus 로고
    • Protein cryoprotective activity of a cytosolic small heat shock protein that accumulates constitutively in chestnut stems and is up-regulated by low and high temperatures
    • Lopez-Matas, M.-A., P. Nunez, A. Soto, I. Allona, R. Casado, C. Collada, M.-A. Guevara, C. Aragoncillo, and L. Gomez. 2004. Protein cryoprotective activity of a cytosolic small heat shock protein that accumulates constitutively in chestnut stems and is up-regulated by low and high temperatures. Plant Physiol. 134:1708-1717.
    • (2004) Plant Physiol , vol.134 , pp. 1708-1717
    • Lopez-Matas, M.-A.1    Nunez, P.2    Soto, A.3    Allona, I.4    Casado, R.5    Collada, C.6    Guevara, M.-A.7    Aragoncillo, C.8    Gomez, L.9
  • 13
    • 33745451171 scopus 로고    scopus 로고
    • Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes
    • Ma, C., M. Haslbeck, L. Babujee, O. Jahn, and S. Reumann. 2006. Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes. Plant Physiol. 141:47-60.
    • (2006) Plant Physiol , vol.141 , pp. 47-60
    • Ma, C.1    Haslbeck, M.2    Babujee, L.3    Jahn, O.4    Reumann, S.5
  • 14
    • 0032697142 scopus 로고    scopus 로고
    • Modified expression of a carrot small heat shock protein gene, hsp17.7, results in increased or decreased thermotolerance
    • Malik, M.K., J.P. Slovin, C.H. Hwang, and J.L. Zimmerman. 1999. Modified expression of a carrot small heat shock protein gene, hsp17.7, results in increased or decreased thermotolerance. Plant J. 20:89-99.
    • (1999) Plant J , vol.20 , pp. 89-99
    • Malik, M.K.1    Slovin, J.P.2    Hwang, C.H.3    Zimmerman, J.L.4
  • 16
    • 0033150267 scopus 로고    scopus 로고
    • Heterologous expression of a plant small heat-shock protein enhances Escherichia coli viability under heat and cold stress
    • Soto, A., I. Allona, C. Collada, M.-A. Guevara, R. Casado, E. Rodriguez-Cerezo, C. Aragoncillo, and L. Gomez. 1999. Heterologous expression of a plant small heat-shock protein enhances Escherichia coli viability under heat and cold stress. Plant Physiol. 120:521-528.
    • (1999) Plant Physiol , vol.120 , pp. 521-528
    • Soto, A.1    Allona, I.2    Collada, C.3    Guevara, M.-A.4    Casado, R.5    Rodriguez-Cerezo, E.6    Aragoncillo, C.7    Gomez, L.8
  • 17
    • 0037136230 scopus 로고    scopus 로고
    • Small heat shock proteins and stress tolerance in plants
    • Sun, W., M. van Montagu, and N. Verbruggen. 2002. Small heat shock proteins and stress tolerance in plants. Biochim. Biophys. Acta 1577:1-9.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 1-9
    • Sun, W.1    van Montagu, M.2    Verbruggen, N.3
  • 18
    • 0033498862 scopus 로고    scopus 로고
    • Plant cold acclimation: Freezing tolerance genes and regulatory mechanisms. Annu
    • Thomashow, M.F. 1999. Plant cold acclimation: Freezing tolerance genes and regulatory mechanisms. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50:571-599.
    • (1999) Rev. Plant Physiol. Plant Mol. Biol , vol.50 , pp. 571-599
    • Thomashow, M.F.1
  • 19
    • 17044385046 scopus 로고    scopus 로고
    • Recent advances in engineering plant tolerance to abiotic stress: Achievements and limitations
    • Vinocur, B. and A. Altman. 2005. Recent advances in engineering plant tolerance to abiotic stress: Achievements and limitations. Curr. Opin. Biotechnol. 16:123-132.
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 123-132
    • Vinocur, B.1    Altman, A.2
  • 20
    • 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, C.H., P.F. Chang, K.W. Yeh, W.C. Lin, Y.M. Chen, and C.Y. Lin. 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, C.H.1    Chang, P.F.2    Yeh, K.W.3    Lin, W.C.4    Chen, Y.M.5    Lin, C.Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.