메뉴 건너뛰기




Volumn 28, Issue 6, 2005, Pages 709-718

Hydrophilins from distant organisms can protect enzymatic activities from water limitation effects in vitro

Author keywords

Dehydrins; Enzyme protection; Hydrophilic proteins; Hydrophilins; LEA proteins; Protein stabilization; Water deficit

Indexed keywords

PROTEIN;

EID: 21244479722     PISSN: 01407791     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-3040.2005.01317.x     Document Type: Article
Times cited : (143)

References (50)
  • 1
    • 0030586740 scopus 로고    scopus 로고
    • Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state
    • Anchordoguy T.J. & Carpenter J.F. (1996) Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Archives of Biochemistry and Biophysics 332, 231-238.
    • (1996) Archives of Biochemistry and Biophysics , vol.332 , pp. 231-238
    • Anchordoguy, T.J.1    Carpenter, J.F.2
  • 2
    • 0000749615 scopus 로고
    • Sequence and characterization of 6 Lea proteins and their genes in cotton
    • Baker J., Steele C. & Dure L.I. (1988) Sequence and characterization of 6 Lea proteins and their genes in cotton. Plant Molecular Biology 11, 277-291.
    • (1988) Plant Molecular Biology , vol.11 , pp. 277-291
    • Baker, J.1    Steele, C.2    Dure, L.I.3
  • 3
    • 0028293240 scopus 로고
    • Characterization of the alpha-gamma and alpha-beta complex: Evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone
    • Boyle D. & Takemoto L. (1994) Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Experimental Eye Research 58, 9-16.
    • (1994) Experimental Eye Research , vol.58 , pp. 9-16
    • Boyle, D.1    Takemoto, L.2
  • 4
    • 0031081346 scopus 로고    scopus 로고
    • Plant responses to water deficit
    • Bray E.A. (1997) Plant responses to water deficit. Trends in Plant Science 2, 48-54.
    • (1997) Trends in Plant Science , vol.2 , pp. 48-54
    • Bray, E.A.1
  • 5
    • 21244443327 scopus 로고
    • Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization
    • Carpenter J.F., Prestrelski S.J. & Arakawa T. (1993) Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. Archives of Biochemistry and Biophysics 250, 505-512.
    • (1993) Archives of Biochemistry and Biophysics , vol.250 , pp. 505-512
    • Carpenter, J.F.1    Prestrelski, S.J.2    Arakawa, T.3
  • 6
    • 0028892852 scopus 로고
    • Enzyme thermostabilization by bovine serum albumin and other proteins: Evidence for hydrophobic interactions
    • Chang B.S. & Mahoney R.R. (1995) Enzyme thermostabilization by bovine serum albumin and other proteins: evidence for hydrophobic interactions. Biotechnology and Applied Biochemistry 22, 203-214.
    • (1995) Biotechnology and Applied Biochemistry , vol.22 , pp. 203-214
    • Chang, B.S.1    Mahoney, R.R.2
  • 7
    • 0031007034 scopus 로고    scopus 로고
    • Dehydrins: A commonalty in the response of plants to dehydration and low temperature
    • Close T.J. (1997) Dehydrins: a commonalty in the response of plants to dehydration and low temperature. Physiologia Plantarum 100, 291-296.
    • (1997) Physiologia Plantarum , vol.100 , pp. 291-296
    • Close, T.J.1
  • 8
    • 0031282618 scopus 로고    scopus 로고
    • Characterization of Phaseolus vulgaris cDNA clones responsive to water deficit: Identification of a novel late embryogenesis abundant-like protein
    • Colmenero-Flores J.M., Campos F., Garciarrubio A. & Covarrubias A.A. (1997) Characterization of Phaseolus vulgaris cDNA clones responsive to water deficit: identification of a novel late embryogenesis abundant-like protein. Plant Molecular Biology 35, 393-405.
    • (1997) Plant Molecular Biology , vol.35 , pp. 393-405
    • Colmenero-Flores, J.M.1    Campos, F.2    Garciarrubio, A.3    Covarrubias, A.A.4
  • 9
    • 0033134245 scopus 로고    scopus 로고
    • Pvlea18, a member of a new-late-embryogenesis-abundant protein family that accumulates during water stress and in the growing regions of well-irrigated been seedlings
    • Colmenero-Flores J., Moreno L., Smith C. & Covarrubias A.A. (1999) Pvlea18, a member of a new-late-embryogenesis-abundant protein family that accumulates during water stress and in the growing regions of well-irrigated been seedlings. Plant Physiology 120, 93-103.
    • (1999) Plant Physiology , vol.120 , pp. 93-103
    • Colmenero-Flores, J.1    Moreno, L.2    Smith, C.3    Covarrubias, A.A.4
  • 10
    • 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. The Plant Cell 10, 623-638.
    • (1998) The 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
  • 12
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong A., Prestrelski S., Allison S. & Carpenter J. (1995) Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. Journal of Pharmacological Science 84, 415-424.
    • (1995) Journal of Pharmacological Science , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.2    Allison, S.3    Carpenter, J.4
  • 13
    • 0002663990 scopus 로고
    • Plant responses to cellular dehydration during enviromental stress
    • eds T. Close & E. Bray, American Society of Plant Physiologists, Rockville, MD
    • Dure L.I. (1993) Plant responses to cellular dehydration during enviromental stress. In Plant Responses to Cellular Dehydration During Environmental Stress (eds T. Close & E. Bray), pp. 91-103. American Society of Plant Physiologists, Rockville, MD.
    • (1993) Plant Responses to Cellular Dehydration during Environmental Stress , pp. 91-103
    • Dure, L.I.1
  • 14
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • Fancy D. & Kodadek T. (1999) Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light. Proceedings of the National Academy of Sciences of the USA 96, 6020-6024.
    • (1999) Proceedings of the National Academy of Sciences of the USA , vol.96 , pp. 6020-6024
    • Fancy, D.1    Kodadek, T.2
  • 15
    • 0032530985 scopus 로고    scopus 로고
    • 1-Anilino-8-naphtalene sulfonate probes a gastric HK-ATPase potassium site whose access requires ionophores
    • Festy F., Lins L., Gallet X., Robert J.C. & Thomas-Soumarmon A. (1998) 1-anilino-8-naphtalene sulfonate probes a gastric HK-ATPase potassium site whose access requires ionophores. Journal of Membrane Biology 165, 153-160.
    • (1998) Journal of Membrane Biology , vol.165 , pp. 153-160
    • Festy, F.1    Lins, L.2    Gallet, X.3    Robert, J.C.4    Thomas-Soumarmon, A.5
  • 16
    • 0001078949 scopus 로고
    • Desiccation-tolerant flowering plants in Southern Africa
    • Gaff D. (1971) Desiccation-tolerant flowering plants in Southern Africa. Science 174, 1033-1034.
    • (1971) Science , vol.174 , pp. 1033-1034
    • Gaff, D.1
  • 20
    • 0029926862 scopus 로고    scopus 로고
    • A Lea class gene of tomato confers salt and freezing tolerance when expressed in Saccharomyces cerevisiae
    • Imai R., Chang L., Ohta A., Bray E. & Tagaki M. (1996) A Lea class gene of tomato confers salt and freezing tolerance when expressed in Saccharomyces cerevisiae. Gene 170, 243-248.
    • (1996) Gene , vol.170 , pp. 243-248
    • Imai, R.1    Chang, L.2    Ohta, A.3    Bray, E.4    Tagaki, M.5
  • 22
    • 0033539557 scopus 로고    scopus 로고
    • Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence
    • Ismail A.M., Hall A.E. & Close T.J. (1999) Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence. Proceedings of the National Academy of Sciences of the USA 96, 13566-13570.
    • (1999) Proceedings of the National Academy of Sciences of the USA , vol.96 , pp. 13566-13570
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 23
    • 0029379541 scopus 로고
    • Purification of a maize dehydrin protein expressed in Escherichia coli
    • Jepson S.G. & Close T.J. (1995) Purification of a maize dehydrin protein expressed in Escherichia coli. Protein Expression and Purification 6, 632-636.
    • (1995) Protein Expression and Purification , vol.6 , pp. 632-636
    • Jepson, S.G.1    Close, T.J.2
  • 24
    • 0028150137 scopus 로고
    • Purification and characterization of COR85-oligomeric complex from cold-acclimated spinach
    • Kazuoka T. & Oeda K. (1994) Purification and characterization of COR85-oligomeric complex from cold-acclimated spinach. Plant and Cell Physiology 35, 601-611.
    • (1994) Plant and Cell Physiology , vol.35 , pp. 601-611
    • Kazuoka, T.1    Oeda, K.2
  • 26
    • 0028388171 scopus 로고
    • Characterization of two cDNAs (ERD10 and ERD14) corresponding to genes that respond rapidly to dehydration stress in Arabidopsis thaliana
    • Kiyosue T., Yamaguchi-Shinozaki K. & Shinozaki K. (1994) Characterization of two cDNAs (ERD10 and ERD14) corresponding to genes that respond rapidly to dehydration stress in Arabidopsis thaliana. Plant and Cell Physiology 35, 225-231.
    • (1994) Plant and Cell Physiology , vol.35 , pp. 225-231
    • Kiyosue, T.1    Yamaguchi-Shinozaki, K.2    Shinozaki, K.3
  • 27
    • 0029442314 scopus 로고
    • Assaying porteins for molecular chaperone activity
    • Lee G.J. (1995) Assaying porteins for molecular chaperone activity. Methods in Cell Biology 50, 325-334.
    • (1995) Methods in Cell Biology , vol.50 , pp. 325-334
    • Lee, G.J.1
  • 28
    • 0032535663 scopus 로고    scopus 로고
    • Evidence for kinetic intermediate states during the refolding of GdnHCl-denatured MM-creatine kinase. Characterization of a trapped monomeric species
    • Leydier C., Clottes E., Couthon F., Marcillat O., Ebel C. & Vial C. (1998) Evidence for kinetic intermediate states during the refolding of GdnHCl-denatured MM-creatine kinase. Characterization of a trapped monomeric species. Biochemistry 37, 17579-17589.
    • (1998) Biochemistry , vol.37 , pp. 17579-17589
    • Leydier, C.1    Clottes, E.2    Couthon, F.3    Marcillat, O.4    Ebel, C.5    Vial, C.6
  • 29
    • 0026684471 scopus 로고
    • A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity
    • Lin C. & Thomashow M.F. (1992) A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity. Biochemistry and Biophysics Research Communications 183, 1103-1108.
    • (1992) Biochemistry and Biophysics Research Communications , vol.183 , pp. 1103-1108
    • Lin, C.1    Thomashow, M.F.2
  • 30
    • 0035907119 scopus 로고    scopus 로고
    • Osmotic perturbations induce differential movements in the core and periphery of proteins, membranes and micelles
    • Madhavarao C.N., Sauna Z.E., Srivastava A. & Sitaramam V. (2001) Osmotic perturbations induce differential movements in the core and periphery of proteins, membranes and micelles. Biophysical Chemistry 90, 233-248.
    • (2001) Biophysical Chemistry , vol.90 , pp. 233-248
    • Madhavarao, C.N.1    Sauna, Z.E.2    Srivastava, A.3    Sitaramam, V.4
  • 31
    • 0031660286 scopus 로고    scopus 로고
    • Stabilization of lactate dehydrogenase following freeze thawing and vacuum-drying in the presence of trehalose and borate
    • Miller D.P., Anderson R.E. & de Pablo T.J. (1998) Stabilization of lactate dehydrogenase following freeze thawing and vacuum-drying in the presence of trehalose and borate. Pharmacological Research 15, 1215-1221.
    • (1998) Pharmacological Research , vol.15 , pp. 1215-1221
    • Miller, D.P.1    Anderson, R.E.2    De Pablo, T.J.3
  • 32
    • 0029050236 scopus 로고
    • A genomic locus in Saccharomyces cerevisiae with four genes up-regulated by osmotic stress
    • Miralles V.J. & Serrano R. (1995) A genomic locus in Saccharomyces cerevisiae with four genes up-regulated by osmotic stress. Molecular Microbiology 17, 653-662.
    • (1995) Molecular Microbiology , vol.17 , pp. 653-662
    • Miralles, V.J.1    Serrano, R.2
  • 33
    • 0032147202 scopus 로고    scopus 로고
    • Role of water in plasticity of proteins: The crystal structures of lysozyme at very low levels of hydration
    • Nagendra H.G., Sukumar N. & Vijayan M. (1998) Role of water in plasticity of proteins: the crystal structures of lysozyme at very low levels of hydration. Proteins: Structure, Function and Genetics 32, 229-240.
    • (1998) Proteins: Structure, Function and Genetics , vol.32 , pp. 229-240
    • Nagendra, H.G.1    Sukumar, N.2    Vijayan, M.3
  • 34
    • 0001027860 scopus 로고
    • Characterization of five abscisic acid-responsive cDNA clones isolated from the desiccation tolerant plant Craterostigma plantagineum and their relationship to other water-stress genes
    • Piatkowski D., Schneider K., Salamini F. & Bartels D. (1990) Characterization of five abscisic acid-responsive cDNA clones isolated from the desiccation tolerant plant Craterostigma plantagineum and their relationship to other water-stress genes. Plant Physiology 94, 1682-1688.
    • (1990) Plant Physiology , vol.94 , pp. 1682-1688
    • Piatkowski, D.1    Schneider, K.2    Salamini, F.3    Bartels, D.4
  • 36
    • 0030028764 scopus 로고    scopus 로고
    • Glycerol decreases the volume and compressibility of protein interior
    • Priev A., Almagor A., Yedgar S. & Gavish B. (1996) Glycerol decreases the volume and compressibility of protein interior. Biochemistry 35, 2061-2066.
    • (1996) Biochemistry , vol.35 , pp. 2061-2066
    • Priev, A.1    Almagor, A.2    Yedgar, S.3    Gavish, B.4
  • 38
    • 0032701931 scopus 로고    scopus 로고
    • Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): Production, localization and potential role in rescuing enzyme function during dehydration
    • Rinne P.L.H., Kaikuranta P.L.M., van der Plas L.H.W. & van der School C. (1999) Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): production, localization and potential role in rescuing enzyme function during dehydration. Planta 209, 377-388.
    • (1999) Planta , vol.209 , pp. 377-388
    • Rinne, P.L.H.1    Kaikuranta, P.L.M.2    Van Der Plas, L.H.W.3    Van Der School, C.4
  • 39
    • 0001621369 scopus 로고
    • Desiccation leads to rapid accumulation of both cytoplasmic an chloroplastic proteins in the resurrection plant Craterostigma plantagineum Hochst
    • Schneider K., Wells B., Schmelzer E., Salamini F. & Bartels D. (1993) Desiccation leads to rapid accumulation of both cytoplasmic an chloroplastic proteins in the resurrection plant Craterostigma plantagineum Hochst. Planta 189, 120-131.
    • (1993) Planta , vol.189 , pp. 120-131
    • Schneider, K.1    Wells, B.2    Schmelzer, E.3    Salamini, F.4    Bartels, D.5
  • 41
    • 0036006031 scopus 로고    scopus 로고
    • Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean
    • Soulages J.L., Kim K., Walters C. & Cushman J.C. (2002) Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean. Plant Physiology 128, 822-832.
    • (2002) Plant Physiology , vol.128 , pp. 822-832
    • Soulages, J.L.1    Kim, K.2    Walters, C.3    Cushman, J.C.4
  • 42
    • 0346034535 scopus 로고    scopus 로고
    • Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (1-proline) -type II structure
    • Soulages J.L., Kim K., Arrese E.L., Walters C. & Cushman J.C. (2003) Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (1-proline) -type II structure. Plant Physiology 131, 963-975.
    • (2003) Plant Physiology , vol.131 , pp. 963-975
    • Soulages, J.L.1    Kim, K.2    Arrese, E.L.3    Walters, C.4    Cushman, J.C.5
  • 43
    • 0027085843 scopus 로고
    • Spectrofluorimetric study of the binding of 1-anilinonaphthalene-8- sulfonate to bovine serum albumin
    • Suarez-Varela A., Sandez-Macho M.I. & Minones J. (1992) Spectrofluorimetric study of the binding of 1-anilinonaphthalene-8-sulfonate to bovine serum albumin. Journal of Pharmacological Sciences 81, 842ñ, 844.
    • (1992) Journal of Pharmacological Sciences , vol.81 , pp. 842
    • Suarez-Varela, A.1    Sandez-Macho, M.I.2    Minones, J.3
  • 44
    • 0033059242 scopus 로고    scopus 로고
    • The wheat LEA protein Em functions as an osmoprotective molecule in Saccharomyces cerevisiae
    • Swire-Clark G.A. & MarcotteW.R. Jr (1999) The wheat LEA protein Em functions as an osmoprotective molecule in Saccharomyces cerevisiae. Plant Molecular Biology 39, 117-128.
    • (1999) Plant Molecular Biology , vol.39 , pp. 117-128
    • Swire-Clark, G.A.1    Marcotte Jr., W.R.2
  • 46
    • 0028518754 scopus 로고
    • Characterization and differential expression of dhn/lea/rab-like genes during cold acclimation and drought stress in Arabidopsis thaliana
    • Welin B.V., Olsson A., Nylander M. & Palva E. T. (1994) Characterization and differential expression of dhn/lea/rab-like genes during cold acclimation and drought stress in Arabidopsis thaliana. Plant Molecular Biology 26, 131-144.
    • (1994) Plant Molecular Biology , vol.26 , pp. 131-144
    • Welin, B.V.1    Olsson, A.2    Nylander, M.3    Palva, E.T.4
  • 48
    • 0030021536 scopus 로고    scopus 로고
    • Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice
    • Xu D., Duan X., Wang B., Hong B., Ho T.-D. & Wu R. (1996) Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice. Plant Physiology 110, 249-257.
    • (1996) Plant Physiology , vol.110 , pp. 249-257
    • Xu, D.1    Duan, X.2    Wang, B.3    Hong, B.4    Ho, T.-D.5    Wu, R.6
  • 49
    • 0035844224 scopus 로고    scopus 로고
    • Transcript expression in Saccharomyces cerevisiae at high salinity
    • Yale J. & Bohnert H.J. (2001) Transcript expression in Saccharomyces cerevisiae at high salinity. Journal of Biological Chemistry 276, 15996-16007.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 15996-16007
    • Yale, J.1    Bohnert, H.J.2
  • 50
    • 0034090734 scopus 로고    scopus 로고
    • Expression of plant group 2 and group 3 lea genes in Sacharomyces cerevisiae revealed functional divergence among LEA proteins
    • Zhang L., Ohta A., Takagi M. & Imai R. (2000) Expression of plant group 2 and group 3 lea genes in Sacharomyces cerevisiae revealed functional divergence among LEA proteins. Journal of Biochemistry 127, 611-616.
    • (2000) Journal of Biochemistry , vol.127 , pp. 611-616
    • Zhang, L.1    Ohta, A.2    Takagi, M.3    Imai, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.