메뉴 건너뛰기




Volumn 33, Issue 6, 2011, Pages 2103-2116

Biochemical characterization of the Arabidopsis KS-type dehydrin protein, whose gene expression is constitutively abundant rather than stress dependent

Author keywords

Arabidopsisthaliana; Dehydrin; Late embryogenesis abundant proteins; Metal binding

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 80054122556     PISSN: 01375881     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11738-011-0749-1     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 33749987806 scopus 로고    scopus 로고
    • Identification of plant cytoskeleton-interacting proteins by screening for actin stress fiber association in mammalian fibroblasts
    • Abu-Abied M, Golomb L, Belausov E, Huang S, Geiger B, Kam Z, Staiger CJ, Sadot E (2006) Identification of plant cytoskeleton-interacting proteins by screening for actin stress fiber association in mammalian fibroblasts. Plant J 48: 367-379.
    • (2006) Plant J , vol.48 , pp. 367-379
    • Abu-Abied, M.1    Golomb, L.2    Belausov, E.3    Huang, S.4    Geiger, B.5    Kam, Z.6    Staiger, C.J.7    Sadot, E.8
  • 2
    • 0142103428 scopus 로고    scopus 로고
    • Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation
    • Alsheikh MK, Heyen BJ, Randall SK (2003) Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation. J Biol Chem 278: 40882-40889.
    • (2003) J Biol Chem , vol.278 , pp. 40882-40889
    • Alsheikh, M.K.1    Heyen, B.J.2    Randall, S.K.3
  • 3
    • 33744495390 scopus 로고    scopus 로고
    • Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins
    • Alsheikh MK, Svensson JT, Randall SK (2005) Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins. Plant Cell Environ 28: 1114-1122.
    • (2005) Plant Cell Environ , vol.28 , pp. 1114-1122
    • Alsheikh, M.K.1    Svensson, J.T.2    Randall, S.K.3
  • 5
    • 0032819784 scopus 로고    scopus 로고
    • Characterization of an 80-kDa dehydrin-like protein in barley responsive to cold acclimation
    • Bravo LA, Close TJ, Corcuera LJ, Guy CL (1999) Characterization of an 80-kDa dehydrin-like protein in barley responsive to cold acclimation. Physiol Plant 106: 177-183.
    • (1999) Physiol Plant , vol.106 , pp. 177-183
    • Bravo, L.A.1    Close, T.J.2    Corcuera, L.J.3    Guy, C.L.4
  • 6
    • 35248855455 scopus 로고    scopus 로고
    • Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana
    • Brini F, Hanin M, Lumbreras V, Amara I, Khoudi H, Hassairi A, Pagès M, Masmoudi K (2007) Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana. Plant Cell Rep 26: 2017-2026.
    • (2007) Plant Cell Rep , vol.26 , pp. 2017-2026
    • Brini, F.1    Hanin, M.2    Lumbreras, V.3    Amara, I.4    Khoudi, H.5    Hassairi, A.6    Pagès, M.7    Masmoudi, K.8
  • 7
    • 0036380564 scopus 로고    scopus 로고
    • Wheat LEA genes, PMA80 and PMA1959 enhance dehydration tolerance of transgenic rice (Oryza sativa L.)
    • Cheng Z, Targolli J, Huang X, Wu R (2002) Wheat LEA genes, PMA80 and PMA1959 enhance dehydration tolerance of transgenic rice (Oryza sativa L.). Mol Breed 10: 71-82.
    • (2002) Mol Breed , vol.10 , pp. 71-82
    • Cheng, Z.1    Targolli, J.2    Huang, X.3    Wu, R.4
  • 8
    • 0030498675 scopus 로고    scopus 로고
    • Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins
    • Close TJ (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97: 795-803.
    • (1996) Physiol Plant , vol.97 , pp. 795-803
    • Close, T.J.1
  • 9
    • 0031770592 scopus 로고    scopus 로고
    • Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat
    • Danyluk J, Perron A, Houde M, Limin A, Fowler B, Benhamou N, Sarhan F (1998) Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat. Plant Cell 10: 623-638.
    • (1998) Plant Cell , vol.10 , pp. 623-638
    • Danyluk, J.1    Perron, A.2    Houde, M.3    Limin, A.4    Fowler, B.5    Benhamou, N.6    Sarhan, F.7
  • 10
    • 28144461633 scopus 로고    scopus 로고
    • Maize Rabl7 overexpression in Arabidopsis plants promotes osmotic stress tolerance
    • Figueras M, Pujal J, Saleh A, Save R, Pagès M, Goday A (2004) Maize Rabl7 overexpression in Arabidopsis plants promotes osmotic stress tolerance. Ann Appl Biol 144: 251-257.
    • (2004) Ann Appl Biol , vol.144 , pp. 251-257
    • Figueras, M.1    Pujal, J.2    Saleh, A.3    Save, R.4    Pagès, M.5    Goday, A.6
  • 11
    • 0028675650 scopus 로고
    • Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants
    • Godoy JA, Lunar R, Torres-Schumann S, Moreno J, Rodrigo RM, Pintor-Toro JA (1994) Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants. Plant Mol Biol 26: 1921-1934.
    • (1994) Plant Mol Biol , vol.26 , pp. 1921-1934
    • Godoy, J.A.1    Lunar, R.2    Torres-Schumann, S.3    Moreno, J.4    Rodrigo, R.M.5    Pintor-Toro, J.A.6
  • 12
    • 77954949426 scopus 로고    scopus 로고
    • The multifunctionality of dehydrins: an overview
    • Hara M (2010) The multifunctionality of dehydrins: an overview. Plant Signal Behav 5: 503-508.
    • (2010) Plant Signal Behav , vol.5 , pp. 503-508
    • Hara, M.1
  • 13
    • 0038758836 scopus 로고    scopus 로고
    • Enhancement of cold tolerance and inhibition of lipid peroxidation by citrus dehydrin in transgenic tobacco
    • Hara M, Terashima S, Fukaya T, Kuboi T (2003) Enhancement of cold tolerance and inhibition of lipid peroxidation by citrus dehydrin in transgenic tobacco. Planta 217: 290-298.
    • (2003) Planta , vol.217 , pp. 290-298
    • Hara, M.1    Terashima, S.2    Fukaya, T.3    Kuboi, T.4
  • 14
    • 24944438537 scopus 로고    scopus 로고
    • Metal binding by citrus dehydrin with histidine-rich domains
    • Hara M, Fujinaga M, Kuboi T (2005) Metal binding by citrus dehydrin with histidine-rich domains. J Exp Bot 56: 2695-2703.
    • (2005) J Exp Bot , vol.56 , pp. 2695-2703
    • Hara, M.1    Fujinaga, M.2    Kuboi, T.3
  • 15
    • 64149112683 scopus 로고    scopus 로고
    • DNA binding of citrus dehydrin promoted by zinc ion
    • Hara M, Shinoda Y, Tanaka Y, Kuboi T (2009) DNA binding of citrus dehydrin promoted by zinc ion. Plant Cell Environ 32: 532-541.
    • (2009) Plant Cell Environ , vol.32 , pp. 532-541
    • Hara, M.1    Shinoda, Y.2    Tanaka, Y.3    Kuboi, T.4
  • 16
    • 0036802435 scopus 로고    scopus 로고
    • The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation
    • Heyen BJ, Alsheikh MK, Smith EA, Torvik CF, Seals DF, Randall SK (2002) The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation. Plant Physiol 130: 675-687.
    • (2002) Plant Physiol , vol.130 , pp. 675-687
    • Heyen, B.J.1    Alsheikh, M.K.2    Smith, E.A.3    Torvik, C.F.4    Seals, D.F.5    Randall, S.K.6
  • 17
    • 77950418344 scopus 로고    scopus 로고
    • Research on plant abiotic stress responses in the post-genome era: past, present and future
    • Hirayama T, Shinozaki K (2010) Research on plant abiotic stress responses in the post-genome era: past, present and future. Plant J 61: 1041-1052.
    • (2010) Plant J , vol.61 , pp. 1041-1052
    • Hirayama, T.1    Shinozaki, K.2
  • 18
    • 13444310781 scopus 로고    scopus 로고
    • Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves
    • Houde M, Dallaire S, N'Dong D, Sarhan F (2004) Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves. Plant Biotechnol J 2: 381-387.
    • (2004) Plant Biotechnol J , vol.2 , pp. 381-387
    • Houde, M.1    Dallaire, S.2    N'Dong, D.3    Sarhan, F.4
  • 19
    • 42149115630 scopus 로고    scopus 로고
    • LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana
    • Hundertmark M, Hincha DK (2008) LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 9: 118.
    • (2008) BMC Genomics , vol.9 , pp. 118
    • Hundertmark, M.1    Hincha, D.K.2
  • 20
    • 0033539557 scopus 로고    scopus 로고
    • Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence
    • Ismail AM, Hall AE, Close TJ (1999) Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence. Proc Natl Acad Sci USA 96: 13566-13570.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13566-13570
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 21
    • 10644286555 scopus 로고    scopus 로고
    • β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein
    • Jiang X, Wang Y (2004) β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein. Biochemistry 43: 15567-15576.
    • (2004) Biochemistry , vol.43 , pp. 15567-15576
    • Jiang, X.1    Wang, Y.2
  • 22
    • 67650175436 scopus 로고    scopus 로고
    • The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes
    • Koag MC, Wilkens S, Fenton RD, Resnik J, Vo E, Close TJ (2009) The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes. Plant Physiol 150: 1503-1514.
    • (2009) Plant Physiol , vol.150 , pp. 1503-1514
    • Koag, M.C.1    Wilkens, S.2    Fenton, R.D.3    Resnik, J.4    Vo, E.5    Close, T.J.6
  • 23
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    • Kovacs D, Kalmar E, Torok Z, Tompa P (2008) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol 147: 381-390.
    • (2008) Plant Physiol , vol.147 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 24
    • 0037067730 scopus 로고    scopus 로고
    • A metal-binding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L
    • Krüger C, Berkowitz O, Stephan UW, Hell R (2002) A metal-binding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L. J Biol Chem 277: 25062-25069.
    • (2002) J Biol Chem , vol.277 , pp. 25062-25069
    • Krüger, C.1    Berkowitz, O.2    Stephan, U.W.3    Hell, R.4
  • 25
    • 0035084328 scopus 로고    scopus 로고
    • Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana
    • Nylander M, Svensson J, Palva ET, Welin BV (2001) Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana. Plant Mol Biol 45: 263-279.
    • (2001) Plant Mol Biol , vol.45 , pp. 263-279
    • Nylander, M.1    Svensson, J.2    Palva, E.T.3    Welin, B.V.4
  • 27
    • 16544387856 scopus 로고    scopus 로고
    • Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis
    • Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET (2004) Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis. Plant Mol Biol 54: 743-753.
    • (2004) Plant Mol Biol , vol.54 , pp. 743-753
    • Puhakainen, T.1    Hess, M.W.2    Mäkelä, P.3    Svensson, J.4    Heino, P.5    Palva, E.T.6
  • 29
    • 33748489098 scopus 로고    scopus 로고
    • Desiccation of the resurrection plant Craterostigma plantagineum induces dynamic changes in protein phosphorylation
    • Röhrig H, Schmidt J, Colby T, Bräutigam A, Hufnagel P, Böhm N, Bartels D (2006) Desiccation of the resurrection plant Craterostigma plantagineum induces dynamic changes in protein phosphorylation. Plant Cell Environ 29: 1606-1615.
    • (2006) Plant Cell Environ , vol.29 , pp. 1606-1615
    • Röhrig, H.1    Schmidt, J.2    Colby, T.3    Bräutigam, A.4    Hufnagel, P.5    Böhm, N.6    Bartels, D.7
  • 30
    • 33847140438 scopus 로고    scopus 로고
    • Plant dehydrins: tissue location, structure and function
    • Rorat T (2006) Plant dehydrins: tissue location, structure and function. Cell Mol Biol Lett 11: 536-556.
    • (2006) Cell Mol Biol Lett , vol.11 , pp. 536-556
    • Rorat, T.1
  • 31
    • 1642378630 scopus 로고    scopus 로고
    • Expression of KS-type dehydrins is primarily regulated by factors related to organ type and leaf developmental stage during vegetative growth
    • Rorat T, Grygorowicz WJ, Irzykowski W, Rey P (2004) Expression of KS-type dehydrins is primarily regulated by factors related to organ type and leaf developmental stage during vegetative growth. Planta 218: 878-885.
    • (2004) Planta , vol.218 , pp. 878-885
    • Rorat, T.1    Grygorowicz, W.J.2    Irzykowski, W.3    Rey, P.4
  • 32
    • 77952742620 scopus 로고    scopus 로고
    • More from less: plant growth under limited water
    • Skirycz A, Inzé D (2010) More from less: plant growth under limited water. Curr Opin Biotechnol 21: 197-203.
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 197-203
    • Skirycz, A.1    Inzé, D.2
  • 33
    • 0033769133 scopus 로고    scopus 로고
    • Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography
    • Svensson J, Palva ET, Welin B (2000) Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. Protein Expr Purif 20: 169-178.
    • (2000) Protein Expr Purif , vol.20 , pp. 169-178
    • Svensson, J.1    Palva, E.T.2    Welin, B.3
  • 34
    • 77957062426 scopus 로고    scopus 로고
    • Dehydrins
    • K. B. Storey and J. M. Storey (Eds.), Elsevier: Signaling and cell adaptation
    • Svensson J, Ismail AM, Palva ET, Close TJ (2002) Dehydrins. In: Storey KB, Storey JM (eds) Sensing. Signaling and cell adaptation, Elsevier, pp 155-171.
    • (2002) Sensing , pp. 155-171
    • Svensson, J.1    Ismail, A.M.2    Palva, E.T.3    Close, T.J.4
  • 36
    • 33748510154 scopus 로고    scopus 로고
    • Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects
    • Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G, Tompa K (2006) Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophys J 91: 2243-2249.
    • (2006) Biophys J , vol.91 , pp. 2243-2249
    • Tompa, P.1    Bánki, P.2    Bokor, M.3    Kamasa, P.4    Kovács, D.5    Lasanda, G.6    Tompa, K.7
  • 37
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • Tunnacliffe A, Wise MJ (2007) The continuing conundrum of the LEA proteins. Naturwissenschaften 94: 791-812.
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 38
    • 0347613015 scopus 로고    scopus 로고
    • Current and prospective applications of metal ion-protein binding
    • Ueda EKM, Gout PW, Morganti L (2003) Current and prospective applications of metal ion-protein binding. J Chromatogr A 988: 1-23.
    • (2003) J Chromatogr A , vol.988 , pp. 1-23
    • Ueda, E.K.M.1    Gout, P.W.2    Morganti, L.3
  • 39
    • 0033047676 scopus 로고    scopus 로고
    • Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach (Prunus persica)
    • Wisniewski M, Webb R, Balsamo R, Close TJ, Yu XM, Griffith M (1999) Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach (Prunus persica). Physiol Plant 105: 600-608.
    • (1999) Physiol Plant , vol.105 , pp. 600-608
    • Wisniewski, M.1    Webb, R.2    Balsamo, R.3    Close, T.J.4    Yu, X.M.5    Griffith, M.6
  • 40
    • 33748255935 scopus 로고    scopus 로고
    • Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings
    • Yin Z, Rorat T, Szabala BM, Ziólkowska A, Malepszy S (2006) Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings. Plant Sci 170: 1164-1172.
    • (2006) Plant Sci , vol.170 , pp. 1164-1172
    • Yin, Z.1    Rorat, T.2    Szabala, B.M.3    Ziólkowska, A.4    Malepszy, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.