메뉴 건너뛰기




Volumn 108, Issue , 2014, Pages 17-25

The crucial role of Φ- And K-segments in the in vitro functionality of Vitis vinifera dehydrin DHN1a

Author keywords

Alternative splicing; Antifungal activity; Cryoprotection; Dehydration protection; Dehydrin; Protein DNA interaction; Vitis vinifera

Indexed keywords

VITIS VINIFERA;

EID: 84911471976     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2014.10.006     Document Type: Article
Times cited : (36)

References (51)
  • 2
    • 0142103428 scopus 로고    scopus 로고
    • Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation
    • M.K. Alsheikh, B.J. Heyen, and S.K. Randall Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation J. Biol. Chem. 278 2003 40882 40889
    • (2003) J. Biol. Chem. , vol.278 , pp. 40882-40889
    • Alsheikh, M.K.1    Heyen, B.J.2    Randall, S.K.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 35248855455 scopus 로고    scopus 로고
    • Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana
    • F. Brini, M. Hanin, V. Lumbreras, I. Amara, H. Khoudi, A. Hassairi, M. Pagès, and K. Masmoudi Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana Plant Cell Rep. 26 2007 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
  • 6
    • 0032031617 scopus 로고    scopus 로고
    • Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens
    • L. Cavallarin, D. Andreu, and B. San Segundo Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens Mol. Plant - Microbe Interact. 11 1998 218 227
    • (1998) Mol. Plant - Microbe Interact. , vol.11 , pp. 218-227
    • Cavallarin, L.1    Andreu, D.2    San Segundo, B.3
  • 7
    • 0031007034 scopus 로고    scopus 로고
    • Dehydrins: A commonalty in the response of plants to dehydration and low temperature
    • T.J. Close Dehydrins: a commonalty in the response of plants to dehydration and low temperature Physiol. Plant. 100 1997 291 296
    • (1997) Physiol. Plant. , vol.100 , pp. 291-296
    • Close, T.J.1
  • 8
    • 0027674861 scopus 로고
    • A view of plant dehydrins using antibodies specific to the carboxy terminal peptide
    • T.J. Close, R.D. Fenton, and M. Francis A view of plant dehydrins using antibodies specific to the carboxy terminal peptide Plant Mol. Biol. 2 1993 279 286
    • (1993) Plant Mol. Biol. , vol.2 , pp. 279-286
    • Close, T.J.1    Fenton, R.D.2    Francis, M.3
  • 9
    • 84882879839 scopus 로고    scopus 로고
    • The K-segments of the wheat dehydrin DHN-5 are essential for the protection of lactate dehydrogenase and β-glucosidase activities in vitro
    • M. Drira, W. Saibi, F. Brini, A. Gargouri, K. Masmoudi, and M. Hanin The K-segments of the wheat dehydrin DHN-5 are essential for the protection of lactate dehydrogenase and β-glucosidase activities in vitro Mol. Biotechnol. 54 2013 643 650
    • (2013) Mol. Biotechnol. , vol.54 , pp. 643-650
    • Drira, M.1    Saibi, W.2    Brini, F.3    Gargouri, A.4    Masmoudi, K.5    Hanin, M.6
  • 12
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • K. Goyal, L.J. Walton, and A. Tunnacliffe LEA proteins prevent protein aggregation due to water stress Biochem. J. 388 2005 151 157
    • (2005) Biochem. J. , vol.388 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 13
    • 17444426801 scopus 로고    scopus 로고
    • Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying
    • J. Grelet, A. Benamar, E. Teyssier, M.-H. Avelange-Macherel, D. Grunwald, and D. Macherel Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying Plant Physiol. 137 2005 157 167
    • (2005) Plant Physiol. , vol.137 , pp. 157-167
    • Grelet, J.1    Benamar, A.2    Teyssier, E.3    Avelange-Macherel, M.-H.4    Grunwald, D.5    Macherel, D.6
  • 14
    • 80053607426 scopus 로고    scopus 로고
    • Plant dehydrins and stress tolerance: Versatile proteins for complex mechanisms
    • M. Hanin, F. Brini, C. Ebel, Y. Toda, Shin Takeda, and Masmoudi Plant dehydrins and stress tolerance: versatile proteins for complex mechanisms Plant Signal. Behav. 6 2011 1503 1509
    • (2011) Plant Signal. Behav. , vol.6 , pp. 1503-1509
    • Hanin, M.1    Brini, F.2    Ebel, C.3    Toda, Y.4    Takeda, S.5    Masmoudi6
  • 15
    • 0034781789 scopus 로고    scopus 로고
    • Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu
    • M. Hara, S. Terashima, and T. Kuboi Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu J. Plant Physiol. 158 2001 1333 1339
    • (2001) J. Plant Physiol. , vol.158 , pp. 1333-1339
    • Hara, M.1    Terashima, S.2    Kuboi, T.3
  • 16
    • 64149112683 scopus 로고    scopus 로고
    • DNA binding of citrus dehydrin promoted by zinc ion
    • M. Hara, Y. Shinoda, Y. Tanaka, and T. Kuboi DNA binding of citrus dehydrin promoted by zinc ion Plant Cell Environ. 32 2009 532 541
    • (2009) Plant Cell Environ. , vol.32 , pp. 532-541
    • Hara, M.1    Shinoda, Y.2    Tanaka, Y.3    Kuboi, T.4
  • 17
    • 0029379706 scopus 로고
    • Immunolocalization of freezing-tolerance associated proteins in cytoplasm and nucleoplasm of wheat crown tissues
    • M. Houde, C. Daniel, M. Lachapelle, F. Allard, S. Laliberté, and F. Sarhan Immunolocalization of freezing-tolerance associated proteins in cytoplasm and nucleoplasm of wheat crown tissues Plant J. 8 1995 583 593
    • (1995) Plant J. , vol.8 , pp. 583-593
    • Houde, M.1    Daniel, C.2    Lachapelle, M.3    Allard, F.4    Laliberté, S.5    Sarhan, F.6
  • 18
    • 78650799611 scopus 로고    scopus 로고
    • Cryoprotective mechanism of a small intrinsically disordered dehydrin protein
    • S. Hughes, and S.P. Graether Cryoprotective mechanism of a small intrinsically disordered dehydrin protein Protein Sci. 20 2011 42 50
    • (2011) Protein Sci. , vol.20 , pp. 42-50
    • Hughes, S.1    Graether, S.P.2
  • 20
    • 42149115630 scopus 로고    scopus 로고
    • LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana
    • M. Hundertmark, and D.K. Hincha LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana BMC Genomics 9 2008 118
    • (2008) BMC Genomics , vol.9 , pp. 118
    • Hundertmark, M.1    Hincha, D.K.2
  • 22
    • 67650175436 scopus 로고    scopus 로고
    • The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes
    • M.C. Koag, S. Wilkens, R.D. Fenton, J. Resnik, E. Vo, and T.J. Close The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes Plant Physiol. 150 2009 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
  • 24
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    • D. Kovacs, E. Kalmar, Z. Torok, and P. Tompa Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins Plant Physiol. 147 2008 381 390
    • (2008) Plant Physiol. , vol.147 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli 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
  • 26
    • 0026684471 scopus 로고
    • A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity
    • C. Lin, and M.F. Thomashow A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity Biochem. Biophys. Res. Commun. 183 1992 1103 1108
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 1103-1108
    • Lin, C.1    Thomashow, M.F.2
  • 28
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • R. Linding, R.B. Russell, V. Neduva, and T.J. Gibson GlobPlot: exploring protein sequences for globularity and disorder Nucleic Acids Res. 31 2003 3701 3708
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 29
    • 10844222539 scopus 로고    scopus 로고
    • Sequence patterns associated with disordered regions in proteins
    • S. Lise, and D.T. Jones Sequence patterns associated with disordered regions in proteins Proteins: Struct. Funct. Bioinf. 58 2005 144 150
    • (2005) Proteins: Struct. Funct. Bioinf. , vol.58 , pp. 144-150
    • Lise, S.1    Jones, D.T.2
  • 32
    • 34250683382 scopus 로고    scopus 로고
    • Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers
    • K. Nakayama, K. Okawa, T. Kakizaki, T. Honma, H. Itoh, and T. Inaba Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers Plant Physiol. 144 2007 513 523
    • (2007) Plant Physiol. , vol.144 , pp. 513-523
    • Nakayama, K.1    Okawa, K.2    Kakizaki, T.3    Honma, T.4    Itoh, H.5    Inaba, T.6
  • 33
    • 79955610759 scopus 로고    scopus 로고
    • Late embryogenesis abundant proteins: Versatile players in the plant adaptation to water limiting environments
    • Y. Olvera-Carrillo, J.L. Reyes, and A.A. Covarrubias Late embryogenesis abundant proteins: versatile players in the plant adaptation to water limiting environments Plant Signal. Behav. 6 2011 586 589
    • (2011) Plant Signal. Behav. , vol.6 , pp. 586-589
    • Olvera-Carrillo, Y.1    Reyes, J.L.2    Covarrubias, A.A.3
  • 34
    • 33847343883 scopus 로고    scopus 로고
    • Alternative splicing of pre-mRNAs of Arabidopsis serine/arginine-rich proteins: Regulation by hormones and stresses
    • S.G. Palusa, G.S. Ali, and A.S.N. Reddy Alternative splicing of pre-mRNAs of Arabidopsis serine/arginine-rich proteins: regulation by hormones and stresses Plant J. 49 2007 1091 1107
    • (2007) Plant J. , vol.49 , pp. 1091-1107
    • Palusa, S.G.1    Ali, G.S.2    Reddy, A.S.N.3
  • 35
    • 84903896074 scopus 로고    scopus 로고
    • Grape contains 4 ICE genes whose expression includes alternative polyadenylation, leading to transcripts encoding at least 7 different ICE proteins
    • M.A. Rahman, M.A. Moody, and A. Nassuth Grape contains 4 ICE genes whose expression includes alternative polyadenylation, leading to transcripts encoding at least 7 different ICE proteins Environ. Exp. Bot. 106 2014 70 78
    • (2014) Environ. Exp. Bot. , vol.106 , pp. 70-78
    • Rahman, M.A.1    Moody, M.A.2    Nassuth, A.3
  • 38
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • P. Romero, Z. Obradovic, and A.K. Dunker Natively disordered proteins: functions and predictions Appl. Bioinf. 3 2004 105 113
    • (2004) Appl. Bioinf. , vol.3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 41
    • 1842587761 scopus 로고    scopus 로고
    • Dehydrin from citrus, which confers in vitro dehydration and freezing protection activity, is constitutive and highly expressed in the flavedo of fruit but responsive to cold and water stress in leaves
    • M.T. Sanchez-Ballesta, M.J. Rodrigo, M.T. LaFuente, A. Granell, and L. Zacarias Dehydrin from citrus, which confers in vitro dehydration and freezing protection activity, is constitutive and highly expressed in the flavedo of fruit but responsive to cold and water stress in leaves J. Agric. Food Chem. 52 2004 1950 1957
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1950-1957
    • Sanchez-Ballesta, M.T.1    Rodrigo, M.J.2    Lafuente, M.T.3    Granell, A.4    Zacarias, L.5
  • 42
    • 84878360308 scopus 로고    scopus 로고
    • Alternative splicing of transcription factors in plant responses to low temperature stress: Mechanisms and functions
    • P.J. Seo, M.-J. Park, and C.-M. Park Alternative splicing of transcription factors in plant responses to low temperature stress: mechanisms and functions Planta 237 2013 1415 1424
    • (2013) Planta , vol.237 , pp. 1415-1424
    • Seo, P.J.1    Park, M.-J.2    Park, C.-M.3
  • 44
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 45
    • 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
    • P. Tompa, P. Bánki, M. Bokor, P. Kamasa, D. Kovács, G. Lasanda, and K. Tompa Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects Biophys. J. 91 2006 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
  • 46
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • A. Tunnacliffe, and M.J. Wise The continuing conundrum of the LEA proteins Naturwissenschaften 94 2007 791 812
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 47
    • 0033047676 scopus 로고    scopus 로고
    • Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: A dehydrin from peach (Prunus persica)
    • M. Wisniewski, R. Webb, R. Balsamo, T.J. Close, X.M. Yu, and M. Griffith Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach (Prunus persica) Physiol. Plant. 105 1999 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
  • 48
    • 33747387556 scopus 로고    scopus 로고
    • Stress- and development-induced expression of spliced and unspliced transcripts from two highly similar dehydrin 1 genes in V. Riparia and V. Vinifera
    • H. Xiao, and A. Nassuth Stress- and development-induced expression of spliced and unspliced transcripts from two highly similar dehydrin 1 genes in V. riparia and V. vinifera Plant Cell Rep. 25 2006 968 977
    • (2006) Plant Cell Rep. , vol.25 , pp. 968-977
    • Xiao, H.1    Nassuth, A.2
  • 50
    • 84864810475 scopus 로고    scopus 로고
    • Identification of the dehydrin gene family from grapevine species and analysis of their responsiveness to various forms of abiotic and biotic stress
    • Y. Yang, M. He, Z. Zhu, S. Li, Y. Xu, C. Zhang, S.D. Singer, and Y. Wang Identification of the dehydrin gene family from grapevine species and analysis of their responsiveness to various forms of abiotic and biotic stress BMC Plant Biol. 12 2012 140
    • (2012) BMC Plant Biol. , vol.12 , pp. 140
    • Yang, Y.1    He, M.2    Zhu, Z.3    Li, S.4    Xu, Y.5    Zhang, C.6    Singer, S.D.7    Wang, Y.8
  • 51
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang, Z.R., Thomson, R., McNeil, P., Esnouf, R.M., 2005. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21, 33693376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.