메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages 586-589

Late embryogenesis abundant proteins: Versatile players in the plant adaptation to water limiting environments

Author keywords

Drought stress; Hydrophilins; Intrinsically unstructured proteins; Late embryogenesis abundant proteins; Water deficit

Indexed keywords

LATE EMBRYOGENESIS ABUNDANT PROTEIN, PLANT; VEGETABLE PROTEIN;

EID: 79955610759     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.6.4.15042     Document Type: Article
Times cited : (99)

References (31)
  • 1
    • 0001587250 scopus 로고
    • Common amino acid sequence domains among the LEA proteins of higher plants
    • DOI: 10.1007/BF00036962
    • Dure L, Crouch M, Harada J, Ho THD, Mundy J, Quatrano RS, et al. Common amino acid sequence domains among the LEA proteins of higher plants. Plant Mol Biol 1989; 12:475-86 DOI: 10.1007/BF00036962.
    • (1989) Plant Mol Biol , vol.12 , pp. 475-486
    • Dure, L.1    Crouch, M.2    Harada, J.3    Ho, T.H.D.4    Mundy, J.5    Quatrano, R.S.6
  • 2
    • 0022379586 scopus 로고
    • Hydrodynamics and optical properties of the wheat Em protein
    • DOI:10.1139/o85-102
    • McCubin WD, Kay CM, Lane BG. Hydrodynamics and optical properties of the wheat Em protein. Can J Biochem Cell Biol 1985; 63:803-11 DOI:10.1139/o85-102.
    • (1985) Can J Biochem Cell Biol , vol.63 , pp. 803-811
    • McCubin, W.D.1    Kay, C.M.2    Lane, B.G.3
  • 3
    • 0034007384 scopus 로고    scopus 로고
    • Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit
    • PMID: 10681550; DOI: 10.1074/jbc.275.8.5668
    • Garay-Arroyo A, Colmenero-Flores JM, Garciarrubio A, Covarrubias AA. Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J Biol Chem 2000; 275:5668-74 PMID: 10681550; DOI: 10.1074/jbc.275.8.5668.
    • (2000) J Biol Chem , vol.275 , pp. 5668-5674
    • Garay-Arroyo, A.1    Colmenero-Flores, J.M.2    Garciarrubio, A.3    Covarrubias, A.A.4
  • 5
    • 42149115630 scopus 로고    scopus 로고
    • LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana
    • PMID: 18318901; DOI:10.1186/1471-2164-9-118
    • Hundertmark M, Hincha DK. LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 2008; 9:118-39 PMID: 18318901; DOI:10.1186/1471-2164-9-118.
    • (2008) BMC Genomics , vol.9 , pp. 118-139
    • Hundertmark, M.1    Hincha, D.K.2
  • 6
    • 57149119064 scopus 로고    scopus 로고
    • Late embryogenesis abundant proteins
    • DOI: 10.1016/S0065-2296(08)00404-7
    • Shih M, Hoekstra FA, Hsing YC. Late Embryogenesis Abundant Proteins. Advanc Bot Res 2008; 48:211-55 DOI: 10.1016/S0065-2296(08)00404-7.
    • (2008) Advanc Bot Res , vol.48 , pp. 211-255
    • Shih, M.1    Hoekstra, F.A.2    Hsing, Y.C.3
  • 7
    • 4143088129 scopus 로고    scopus 로고
    • Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae
    • PMID: 15302829; DOI:10.1128/EC.3.4.966-975.2004
    • Browne JA, Dolan KM, Tyson T, Goyal K, Tunnacliffe A, Burnell AM. Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae. Eukaryot Cell 2004; 3:966-75 PMID: 15302829; DOI:10.1128/EC.3.4.966-975.2004.
    • (2004) Eukaryot Cell , vol.3 , pp. 966-975
    • Browne, J.A.1    Dolan, K.M.2    Tyson, T.3    Goyal, K.4    Tunnacliffe, A.5    Burnell, A.M.6
  • 8
    • 77956706736 scopus 로고    scopus 로고
    • Functional analysis of the group 4 late embryogenesis abundant proteins reveals their relevance in the adaptive response during water deficit in Arabidopsis
    • PMID: 20668063; DOI: 10.1104/pp.110.158964
    • Olvera-Carrillo Y, Campos F, Reyes JL, Garciarrubio A, Covarrubias AA. Functional analysis of the group 4 late embryogenesis abundant proteins reveals their relevance in the adaptive response during water deficit in Arabidopsis. Plant Physiol 2010; 154:373-90 PMID: 20668063; DOI: 10.1104/pp.110.158964.
    • (2010) Plant Physiol , vol.154 , pp. 373-390
    • Olvera-Carrillo, Y.1    Campos, F.2    Reyes, J.L.3    Garciarrubio, A.4    Covarrubias, A.A.5
  • 9
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • PMID: 12569097; DOI: 10.1074/jbc. M212007200
    • Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, et al. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J Biol Chem 2003; 278:12977-84 PMID: 12569097; DOI: 10.1074/jbc. M212007200.
    • (2003) J Biol Chem , vol.278 , pp. 12977-12984
    • Goyal, K.1    Tisi, L.2    Basran, A.3    Browne, J.4    Burnell, A.5    Zurdo, J.6
  • 10
    • 67650175436 scopus 로고    scopus 로고
    • The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes
    • PMID: 19439573; DOI: 10.1104/pp.109.136697
    • Koag MC, Wilkens S, Fenton RD, Resnik J, Vo E, Close TJ. The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes. Plant Physiol 2009; 150:1503-14 PMID: 19439573; DOI: 10.1104/pp.109.136697.
    • (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
  • 11
    • 21244479722 scopus 로고    scopus 로고
    • Hydrophilins from distant organisms can protect enzymatic activities from water limitation effects in vitro
    • DOI: 10.1111/j.1365-3040.2005.01317.x
    • Reyes JL, Rodrigo MJ, Colmenero-Flores JM, Gil JV, Salamini F, Bartels D, et al. Hydrophilins from distant organisms can protect enzymatic activities from water limitation effects in vitro. Plant Cell Environ 2005; 28:709-18 DOI: 10.1111/j.1365-3040.2005.01317.x.
    • (2005) Plant Cell Environ , vol.28 , pp. 709-718
    • Reyes, J.L.1    Rodrigo, M.J.2    Colmenero-Flores, J.M.3    Gil, J.V.4    Salamini, F.5    Bartels, D.6
  • 12
    • 55949122703 scopus 로고    scopus 로고
    • Functional dissection of hydrophilins during in vitro freeze protection
    • PMID: 18761701; DOI:10.1111/j.1365-3040.2008.01879.x
    • Reyes JL, Campos F, Wei H, Arora R, Yang Y, Karlson DT. Functional dissection of hydrophilins during in vitro freeze protection. Plant Cell Environ 2008; 31:1781-90 PMID: 18761701; DOI:10.1111/j.1365-3040.2008.01879.x.
    • (2008) Plant Cell Environ , vol.31 , pp. 1781-1790
    • Reyes, J.L.1    Campos, F.2    Wei, H.3    Arora, R.4    Yang, Y.5    Karlson, D.T.6
  • 13
    • 77954949426 scopus 로고    scopus 로고
    • The multifuncionality of dehydrins: An overview
    • PMID:20139737
    • Hara M. The multifuncionality of dehydrins: an overview. Plant Signal Behav 2010; 5:1-6 PMID:20139737.
    • (2010) Plant Signal Behav , vol.5 , pp. 1-6
    • Hara, M.1
  • 14
    • 77950597578 scopus 로고    scopus 로고
    • Intrinsically disordered chaperones in plants and animals
    • PMID: 20453919; DOI:10.1139/O09-163
    • Tompa P, Kovacs D. Intrinsically disordered chaperones in plants and animals. Biochem Cell Biol 2010; 88:167-74 PMID: 20453919; DOI:10.1139/O09-163.
    • (2010) Biochem Cell Biol , vol.88 , pp. 167-174
    • Tompa, P.1    Kovacs, D.2
  • 15
    • 0026684471 scopus 로고
    • A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity
    • PMID: 1567390
    • Lin C, Thomashow MF. A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity. Biochem Biophys Res Commun 1992;183:1103-8 PMID: 1567390.
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 1103-1108
    • Lin, C.1    Thomashow, M.F.2
  • 16
    • 0034781789 scopus 로고    scopus 로고
    • Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu
    • DOI:10.1078/0176-1617-00600
    • Hara M, Terashima S, Kuboi T. Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu. J Plant Physiol 2001; 58:1333-9 DOI:10.1078/0176-1617-00600.
    • (2001) J Plant Physiol , vol.58 , pp. 1333-1339
    • Hara, M.1    Terashima, S.2    Kuboi, T.3
  • 17
    • 34250683382 scopus 로고    scopus 로고
    • Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers
    • PMID: 17384167; DOI:10.1104/pp.106.094581
    • Nakayama K, Okawa K, Kakizaki T, Honma T, Itoh H, Inaba T. Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers. Plant Physiol 2007; 144:513-23 PMID: 17384167; DOI:10.1104/pp.106.094581.
    • (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
  • 18
    • 17444426801 scopus 로고    scopus 로고
    • Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying
    • PMID: 15618423; DOI: 10.1104/pp.104.052480
    • Grelet J, Benamar A, Teyssier E, Avelange-Macherel MH, Grunwald D, Macherel D. Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying. Plant Physiol 2005; 137:157-67. PMID: 15618423; DOI: 10.1104/pp.104.052480.
    • (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
  • 19
    • 0033134023 scopus 로고    scopus 로고
    • Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea
    • PMID: 10318701
    • Ismail AM, Hall AE, Close TJ. Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea. Plant Physiol 1999; 120:237-44. PMID: 10318701.
    • (1999) Plant Physiol , vol.120 , pp. 237-244
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 20
    • 0036006031 scopus 로고    scopus 로고
    • Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean
    • PMID: 11891239; DOI: 10.1104/pp.010521
    • Soulages JL, Kim K, Walters C, Cushman JC. Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean. Plant Physiol 2002; 128:822-32 PMID: 11891239; DOI: 10.1104/pp.010521.
    • (2002) Plant Physiol , vol.128 , pp. 822-832
    • Soulages, J.L.1    Kim, K.2    Walters, C.3    Cushman, J.C.4
  • 21
    • 17844363270 scopus 로고    scopus 로고
    • Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16
    • PMID: 15803408; DOI: 10.1007/s11103-004-4680-3
    • Shih MD, Lin SD, Hsieh JS, Tsou CH, Chow TY, Lin TP, et al. Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16. Plant Mol Biol 2004; 56:689-703 PMID: 15803408; DOI: 10.1007/s11103-004-4680-3.
    • (2004) Plant Mol Biol , vol.56 , pp. 689-703
    • Shih, M.D.1    Lin, S.D.2    Hsieh, J.S.3    Tsou, C.H.4    Chow, T.Y.5    Lin, T.P.6
  • 22
    • 34249986057 scopus 로고    scopus 로고
    • A predicted N-terminal helical domain of a Group 1 LEA protein is required for protection of enzyme activity from drying
    • PMID: 17544288; DOI:10.1016/j.plaphy.2007.03.027
    • Gilles GJ, Hines KM, Manfre AJ, Marcotte WR Jr. A predicted N-terminal helical domain of a Group 1 LEA protein is required for protection of enzyme activity from drying. Plant Physiol Biochem 2007; 45:389-99 PMID: 17544288; DOI:10.1016/j.plaphy.2007.03.027.
    • (2007) Plant Physiol Biochem , vol.45 , pp. 389-399
    • Gilles, G.J.1    Hines, K.M.2    Manfre, A.J.3    Marcotte Jr., W.R.4
  • 23
    • 34347397758 scopus 로고    scopus 로고
    • Structure and function of a mitochondrial late embryogenesis abundant protein are revealed by desiccation
    • PMID: 17526751; DOI: 10.1105/tpc.107.050104
    • Tolleter D, Jaquinod M, Mangavel C, Passirani C, Saulnier P, Manon S, et al. Structure and function of a mitochondrial late embryogenesis abundant protein are revealed by desiccation. Plant Cell 2007; 19:1580-9. PMID: 17526751; DOI: 10.1105/tpc.107.050104.
    • (2007) Plant Cell , vol.19 , pp. 1580-1589
    • Tolleter, D.1    Jaquinod, M.2    Mangavel, C.3    Passirani, C.4    Saulnier, P.5    Manon, S.6
  • 24
    • 0033134245 scopus 로고    scopus 로고
    • Pvlea-18, a member of a new lateembryogenesis abundant protein family that accumulates during water stress and in the growing regions of well irrigated bean seedlings
    • PMID: 10318687
    • Colmenero-Flores JM, Moreno LP, Smith C, Covarrubias AA. Pvlea-18, a member of a new lateembryogenesis abundant protein family that accumulates during water stress and in the growing regions of well irrigated bean seedlings. Plant Physiol 1999; 120:93-104 PMID: 10318687.
    • (1999) Plant Physiol , vol.120 , pp. 93-104
    • Colmenero-Flores, J.M.1    Moreno, L.P.2    Smith, C.3    Covarrubias, A.A.4
  • 25
    • 39049191101 scopus 로고    scopus 로고
    • Differential expression of dehydrin in flower buds of two Japanese apricot cultivars requiring different chilling requirements for bud break
    • PMID:17169895; DOI: 10.1093/treephys/26.12.1559
    • Yamane H, Kashiwa Y, Kakehi E, Yonemori K, Mori H, Hayashi K, et al. Differential expression of dehydrin in flower buds of two Japanese apricot cultivars requiring different chilling requirements for bud break. Tree Physiol 2006; 26:1559-63 PMID:17169895; DOI: 10.1093/treephys/26.12.1559.
    • (2006) Tree Physiol , vol.26 , pp. 1559-1563
    • Yamane, H.1    Kashiwa, Y.2    Kakehi, E.3    Yonemori, K.4    Mori, H.5    Hayashi, K.6
  • 27
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • PMID: 15738986
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005; 6:197-208 PMID: 15738986.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 28
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • PMID: 18054235; DOI:10.1016/j.tibs.2007.10.003
    • Tompa P, Fuxreiter M. Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 2008; 33:2-8 PMID: 18054235; DOI:10.1016/j.tibs.2007.10.003.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 29
    • 1842473094 scopus 로고    scopus 로고
    • P27 binds cyclin-CDK complexes through a sequential mechanism involving indinginduced protein folding
    • PMID: 15024385
    • Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, et al. p27 binds cyclin-CDK complexes through a sequential mechanism involving indinginduced protein folding. Nat Struct Mol Biol 2004; 11:358-64 PMID: 15024385.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 358-364
    • Lacy, E.R.1    Filippov, I.2    Lewis, W.S.3    Otieno, S.4    Xiao, L.5    Weiss, S.6
  • 30
    • 34247279793 scopus 로고    scopus 로고
    • Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stressregulated plant-specific protein, from unfolded to folded state
    • PMID: 17189335; DOI: 10.1104/pp.106.092965
    • Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, et al. Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stressregulated plant-specific protein, from unfolded to folded state. Plant Physiol 2007; 143:617-28 PMID: 17189335; DOI: 10.1104/pp.106.092965.
    • (2007) Plant Physiol , vol.143 , pp. 617-628
    • Goldgur, Y.1    Rom, S.2    Ghirlando, R.3    Shkolnik, D.4    Shadrin, N.5    Konrad, Z.6
  • 31
    • 77949356529 scopus 로고    scopus 로고
    • Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry
    • PMID: 20071374; DOI: 10.1093/pcp/pcq005
    • Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. Plant Cell Physiol 2010; 51:395-407 PMID: 20071374; DOI: 10.1093/pcp/pcq005.
    • (2010) Plant Cell Physiol , vol.51 , pp. 395-407
    • Shih, M.D.1    Hsieh, T.Y.2    Lin, T.P.3    Hsing, Y.I.4    Hoekstra, F.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.