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Volumn 8, Issue 1, 2016, Pages 45-52

Hydrophilins in the filamentous fungus Neosartorya fischeri (Aspergillus fischeri) have protective activity against several types of microbial water stress

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; LACTATE DEHYDROGENASE;

EID: 84958929700     PISSN: None     EISSN: 17582229     Source Type: Journal    
DOI: 10.1111/1758-2229.12349     Document Type: Article
Times cited : (12)

References (46)
  • 2
    • 0000092348 scopus 로고
    • Extraordinary heat-resistance of Talaromyces flavus and Neosartorya fischeri ascospores in fruit products
    • Beuchat, L.R. (1986) Extraordinary heat-resistance of Talaromyces flavus and Neosartorya fischeri ascospores in fruit products. J Food Sci 51: 1506-1510.
    • (1986) J Food Sci , vol.51 , pp. 1506-1510
    • Beuchat, L.R.1
  • 4
    • 0037034885 scopus 로고    scopus 로고
    • Anhydrobiosis - plant desiccation gene found in a nematode
    • Browne, J., Tunnacliffe, A., and Burnell, A. (2002) Anhydrobiosis - plant desiccation gene found in a nematode. Nature 416: 38.
    • (2002) Nature , vol.416 , pp. 38
    • Browne, J.1    Tunnacliffe, A.2    Burnell, A.3
  • 5
    • 84885625938 scopus 로고    scopus 로고
    • Group 1 LEA proteins, an ancestral plant protein group, are also present in other eukaryotes, and in the archeae and bacteria domains
    • Campos, F., Cuevas-Velazquez, C., Fares, M.A., Reyes, J.L., and Covarrubias, A.A. (2013) Group 1 LEA proteins, an ancestral plant protein group, are also present in other eukaryotes, and in the archeae and bacteria domains. Mol Genet Genomics 288: 503-517.
    • (2013) Mol Genet Genomics , vol.288 , pp. 503-517
    • Campos, F.1    Cuevas-Velazquez, C.2    Fares, M.A.3    Reyes, J.L.4    Covarrubias, A.A.5
  • 6
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong, A., Prestrelski, S.J., Allison, S.D., and Carpenter, J.F. (1995) Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J Pharm Sci 84: 415-424.
    • (1995) J Pharm Sci , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 7
    • 0002663990 scopus 로고
    • Rockville: American Society of Plant Physiologists.
    • Dure, L., III (1993a) Structural Motifs in LEA Proteins. Rockville: American Society of Plant Physiologists.
    • (1993) Structural Motifs in LEA Proteins
    • Dure, L.1
  • 8
    • 0027564435 scopus 로고
    • A repeating 11-mer amino acid motif and plant desiccation
    • Dure, L., III (1993b) A repeating 11-mer amino acid motif and plant desiccation. Plant J 3: 363-369.
    • (1993) Plant J , vol.3 , pp. 363-369
    • Dure, L.1
  • 9
    • 0019874708 scopus 로고
    • Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis
    • Dure, L., III, Greenway, S.C., and Galau, G.A. (1981) Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis. Biochemistry 20: 4162-4168.
    • (1981) Biochemistry , vol.20 , pp. 4162-4168
    • Dure, L.1    Greenway, S.C.2    Galau, G.A.3
  • 10
    • 0001587250 scopus 로고
    • Common amino acid sequence domains among the LEA proteins of higher plants
    • Dure, L., III, Crouch, M., Harada, J., Ho, T.-H., Mundy, J., Quatrano, R., etal. (1989) Common amino acid sequence domains among the LEA proteins of higher plants. Plant Mol Biol 12: 475-486.
    • (1989) Plant Mol Biol , vol.12 , pp. 475-486
    • Dure, L.1    Crouch, M.2    Harada, J.3    Ho, T.-H.4    Mundy, J.5    Quatrano, R.6
  • 11
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J., and Wright, P.E. (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 0034007384 scopus 로고    scopus 로고
    • Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit
    • Garay-Arroyo, A., Colmenero-Flores, J.M., Garciarrubio, A., and Covarrubias, A.A. (2000) Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J Biol Chem 275: 5668-5674.
    • (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
  • 13
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • Goyal, K., Tisi, L., Basran, A., Browne, J., Burnell, A., Zurdo, J., and Tunnacliffe, A. (2003) Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J Biol Chem 278: 12977-12984.
    • (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    Tunnacliffe, A.7
  • 14
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • Goyal, K., Walton, L.J., and Tunnacliffe, A. (2005) LEA proteins prevent protein aggregation due to water stress. Biochem J 388: 151-157.
    • (2005) Biochem J , vol.388 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 15
    • 17444426801 scopus 로고    scopus 로고
    • Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying
    • Grelet, J., Benamar, A., Teyssier, E., Avelange-Macherel, M.H., Grunwald, D., and Macherel, D. (2005) Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying. Plant Physiol 137: 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
  • 16
    • 84864616661 scopus 로고    scopus 로고
    • NMR structure of hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast
    • Herbert, A.P., Riesen, M., Bloxam, L., Kosmidou, E., Wareing, B.M., Johnson, J.R., etal. (2012) NMR structure of hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast. PLoS ONE 7: e41975.
    • (2012) PLoS ONE , vol.7 , pp. e41975
    • Herbert, A.P.1    Riesen, M.2    Bloxam, L.3    Kosmidou, E.4    Wareing, B.M.5    Johnson, J.R.6
  • 18
    • 0029561270 scopus 로고
    • Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: identification of late embryogenesis abundant proteins
    • Honjoh, K., Yoshimoto, M., Joh, T., Kajiwara, T., Miyamoto, T., and Hatano, S. (1995) Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: identification of late embryogenesis abundant proteins. Plant Cell Physiol 36: 1421-1430.
    • (1995) Plant Cell Physiol , vol.36 , pp. 1421-1430
    • Honjoh, K.1    Yoshimoto, M.2    Joh, T.3    Kajiwara, T.4    Miyamoto, T.5    Hatano, S.6
  • 19
    • 67349221229 scopus 로고    scopus 로고
    • Possible roles of LEA proteins and sHSPs in seed protection: a short review
    • Kalemba, E., and Pukacka, S. (2007) Possible roles of LEA proteins and sHSPs in seed protection: a short review. Biol Lett 44: 3-16.
    • (2007) Biol Lett , vol.44 , pp. 3-16
    • Kalemba, E.1    Pukacka, S.2
  • 20
    • 0035936144 scopus 로고    scopus 로고
    • Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
    • Katinka, M.D., Duprat, S., Cornillot, E., Metenier, G., Thomarat, F., Prensier, G., etal. (2001) Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi. Nature 414: 450-453.
    • (2001) Nature , vol.414 , pp. 450-453
    • Katinka, M.D.1    Duprat, S.2    Cornillot, E.3    Metenier, G.4    Thomarat, F.5    Prensier, G.6
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 84876794343 scopus 로고    scopus 로고
    • Germination of conidia of Aspergillus niger is accompanied by major changes in RNA profiles
    • van Leeuwen, M.R., Krijgsheld, P., Bleichrodt, R., Menke, H., Stam, H., Stark, J., etal. (2013a) Germination of conidia of Aspergillus niger is accompanied by major changes in RNA profiles. Stud Mycol 74: 59-70.
    • (2013) Stud Mycol , vol.74 , pp. 59-70
    • van Leeuwen, M.R.1    Krijgsheld, P.2    Bleichrodt, R.3    Menke, H.4    Stam, H.5    Stark, J.6
  • 25
    • 0028838470 scopus 로고
    • Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying
    • Leslie, S.B., Israeli, E., Lighthart, B., Crowe, J.H., and Crowe, L.M. (1995) Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying. Appl Environ Microbiol 61: 3592-3597.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3592-3597
    • Leslie, S.B.1    Israeli, E.2    Lighthart, B.3    Crowe, J.H.4    Crowe, L.M.5
  • 26
    • 67449106986 scopus 로고    scopus 로고
    • Occurrence of mitochondria-targeted Late Embryogenesis Abundant (LEA) gene in animals increases organelle resistance to water stress
    • Menze, M.A., Boswell, L., Toner, M., and Hand, S.C. (2009) Occurrence of mitochondria-targeted Late Embryogenesis Abundant (LEA) gene in animals increases organelle resistance to water stress. J Biol Chem 284: 10714-10719.
    • (2009) J Biol Chem , vol.284 , pp. 10714-10719
    • Menze, M.A.1    Boswell, L.2    Toner, M.3    Hand, S.C.4
  • 27
    • 1242292279 scopus 로고    scopus 로고
    • LEA (late embryonic abundant)-like protein Hsp 12 (heat-shock protein 12) is present in the cell wall and enhances the barotolerance of the yeast Saccharomyces cerevisiae
    • Motshwene, P., Karreman, R., Kgari, G., Brandt, W., and Lindsey, G. (2004) LEA (late embryonic abundant)-like protein Hsp 12 (heat-shock protein 12) is present in the cell wall and enhances the barotolerance of the yeast Saccharomyces cerevisiae. Biochem J 377: 769-774.
    • (2004) Biochem J , vol.377 , pp. 769-774
    • Motshwene, P.1    Karreman, R.2    Kgari, G.3    Brandt, W.4    Lindsey, G.5
  • 28
    • 33745655415 scopus 로고    scopus 로고
    • Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments
    • Mouillon, J.M., Gustafsson, P., and Harryson, P. (2006) Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments. Plant Physiol 141: 638-650.
    • (2006) Plant Physiol , vol.141 , pp. 638-650
    • Mouillon, J.M.1    Gustafsson, P.2    Harryson, P.3
  • 29
    • 67650739079 scopus 로고    scopus 로고
    • Small heat-shock protein Hsp12 contributes to yeast tolerance to freezing stress
    • Pacheco, A., Pereira, C., Almeida, M.J., and Sousa, M.J. (2009) Small heat-shock protein Hsp12 contributes to yeast tolerance to freezing stress. Microbiol-Sgm 155: 2021-2028.
    • (2009) Microbiol-Sgm , vol.155 , pp. 2021-2028
    • Pacheco, A.1    Pereira, C.2    Almeida, M.J.3    Sousa, M.J.4
  • 30
    • 79955802057 scopus 로고    scopus 로고
    • Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes
    • Popova, A.V., Hundertmark, M., Seckler, R., and Hincha, D.K. (2011) Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes. Biochim Biophys Acta 1808: 1879-1887.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1879-1887
    • Popova, A.V.1    Hundertmark, M.2    Seckler, R.3    Hincha, D.K.4
  • 31
    • 0025071981 scopus 로고
    • HSP12, a new small heat-shock gene of Saccharomyces cerevisiae: analysis of structure, regulation and function
    • Praekelt, U.M., and Meacock, P.A. (1990) HSP12, a new small heat-shock gene of Saccharomyces cerevisiae: analysis of structure, regulation and function. Mol Gen Genet 223: 97-106.
    • (1990) Mol Gen Genet , vol.223 , pp. 97-106
    • Praekelt, U.M.1    Meacock, P.A.2
  • 32
    • 24044515001 scopus 로고    scopus 로고
    • FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded
    • Prilusky, J., Felder, C.E., Zeev-Ben-Mordehai, T., Rydberg, E.H., Man, O., Beckmann, J.S., etal. (2005) FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21: 3435-3438.
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1    Felder, C.E.2    Zeev-Ben-Mordehai, T.3    Rydberg, E.H.4    Man, O.5    Beckmann, J.S.6
  • 33
    • 0033967755 scopus 로고    scopus 로고
    • The LEA-like protein HSP12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress
    • Sales, K., Brandt, W., Rumbak, E., and Lindsey, G. (2000) The LEA-like protein HSP12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. Biochim Biophys Acta Biomembr 1463: 267-278.
    • (2000) Biochim Biophys Acta Biomembr , vol.1463 , pp. 267-278
    • Sales, K.1    Brandt, W.2    Rumbak, E.3    Lindsey, G.4
  • 34
    • 0033199922 scopus 로고    scopus 로고
    • Roles of sugar alcohols in osmotic stress adaptation. Replacement of glycerol by mannitol and sorbitol in yeast
    • Shen, B., Hohmann, S., Jensen, R.G., and Bohnert, H.J. (1999) Roles of sugar alcohols in osmotic stress adaptation. Replacement of glycerol by mannitol and sorbitol in yeast. Plant Physiol 121: 45-52.
    • (1999) Plant Physiol , vol.121 , pp. 45-52
    • Shen, B.1    Hohmann, S.2    Jensen, R.G.3    Bohnert, H.J.4
  • 35
    • 76749151971 scopus 로고    scopus 로고
    • Desiccation-induced structuralization and glass formation of group 3 late embryogenesis abundant protein model peptides
    • Shimizu, T., Kanamori, Y., Furuki, T., Kikawada, T., Okuda, T., and Takahashi, T. (2010) Desiccation-induced structuralization and glass formation of group 3 late embryogenesis abundant protein model peptides. Biochemistry 49: 1093-1104.
    • (2010) Biochemistry , vol.49 , pp. 1093-1104
    • Shimizu, T.1    Kanamori, Y.2    Furuki, T.3    Kikawada, T.4    Okuda, T.5    Takahashi, T.6
  • 36
    • 0026741970 scopus 로고
    • Expression of con genes along the three sporulation pathways of Neurospora crassa
    • Springer, M.L., and Yanofsky, C. (1992) Expression of con genes along the three sporulation pathways of Neurospora crassa. Genes Dev 6: 1052-1057.
    • (1992) Genes Dev , vol.6 , pp. 1052-1057
    • Springer, M.L.1    Yanofsky, C.2
  • 37
    • 2942755628 scopus 로고    scopus 로고
    • Isolation of a new member of group 3 late embryogenesis abundant protein gene from a halotolerant green alga by a functional expression screening with cyanobacterial cells
    • Tanaka, S., Ikeda, K., and Miyasaka, H. (2004) Isolation of a new member of group 3 late embryogenesis abundant protein gene from a halotolerant green alga by a functional expression screening with cyanobacterial cells. FEMS Microbiol Lett 236: 41-45.
    • (2004) FEMS Microbiol Lett , vol.236 , pp. 41-45
    • Tanaka, S.1    Ikeda, K.2    Miyasaka, H.3
  • 38
    • 34347397758 scopus 로고    scopus 로고
    • Structure and function of a mitochondrial late embryogenesis abundant protein are revealed by desiccation
    • Tolleter, D., Jaquinod, M., Mangavel, C., Passirani, C., Saulnier, P., Manon, S., etal. (2007) Structure and function of a mitochondrial late embryogenesis abundant protein are revealed by desiccation. Plant Cell 19: 1580-1589.
    • (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
  • 39
    • 77955652628 scopus 로고    scopus 로고
    • A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state
    • Tolleter, D., Hincha, D.K., and Macherel, D. (2010) A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state. Biochim Biophys Acta 1798: 1926-1933.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1926-1933
    • Tolleter, D.1    Hincha, D.K.2    Macherel, D.3
  • 40
    • 0034669882 scopus 로고    scopus 로고
    • Why are 'natively unfolded' proteins unstructured under physiologic conditions?
    • Uversky, V.N., Gillespie, J.R., and Fink, A.L. (2000) Why are 'natively unfolded' proteins unstructured under physiologic conditions? Proteins 41: 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 41
    • 1642545243 scopus 로고    scopus 로고
    • Artemin is an RNA-binding protein with high thermal stability and potential RNA chaperone activity
    • Warner, A.H., Brunet, R.T., MacRae, T.H., and Clegg, J.S. (2004) Artemin is an RNA-binding protein with high thermal stability and potential RNA chaperone activity. Arch Biochem Biophys 424: 189-200.
    • (2004) Arch Biochem Biophys , vol.424 , pp. 189-200
    • Warner, A.H.1    Brunet, R.T.2    MacRae, T.H.3    Clegg, J.S.4
  • 42
    • 77956006894 scopus 로고    scopus 로고
    • Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function
    • Welker, S., Rudolph, B., Frenzel, E., Hagn, F., Liebisch, G., and Schmitz, G. (2010) Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol Cell 39: 507-520.
    • (2010) Mol Cell , vol.39 , pp. 507-520
    • Welker, S.1    Rudolph, B.2    Frenzel, E.3    Hagn, F.4    Liebisch, G.5    Schmitz, G.6
  • 43
    • 0027366309 scopus 로고
    • Structural characterization and expression analysis of the Neurospora conidiation gene CON-6
    • White, B.T., and Yanofsky, C. (1993) Structural characterization and expression analysis of the Neurospora conidiation gene CON-6. Dev Biol 160: 254-264.
    • (1993) Dev Biol , vol.160 , pp. 254-264
    • White, B.T.1    Yanofsky, C.2
  • 44
    • 0035847037 scopus 로고    scopus 로고
    • Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro
    • Wolkers, W.F., McCready, S., Brandt, W.F., Lindsey, G.G., and Hoekstra, F.A. (2001) Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro. Biochim Biophys Acta 1544: 196-206.
    • (2001) Biochim Biophys Acta , vol.1544 , pp. 196-206
    • Wolkers, W.F.1    McCready, S.2    Brandt, W.F.3    Lindsey, G.G.4    Hoekstra, F.A.5
  • 45
    • 84923788583 scopus 로고    scopus 로고
    • Functionality and prevalence of trehalose-based oligosaccharides as novel compatible solutes in ascospores of Neosartorya fischeri (Aspergillus fischeri) and other fungi
    • Wyatt, T.T., van Leeuwen, M.R., Golovina, E.A., Hoekstra, F.A., Kuenstner, E.J., Palumbo, E.A., etal. (2015a) Functionality and prevalence of trehalose-based oligosaccharides as novel compatible solutes in ascospores of Neosartorya fischeri (Aspergillus fischeri) and other fungi. Environ Microbiol 17: 395-411.
    • (2015) Environ Microbiol , vol.17 , pp. 395-411
    • Wyatt, T.T.1    van Leeuwen, M.R.2    Golovina, E.A.3    Hoekstra, F.A.4    Kuenstner, E.J.5    Palumbo, E.A.6
  • 46
    • 84929120667 scopus 로고    scopus 로고
    • Novel trehalose-based oligosaccharides from extreme stress-tolerant ascospores of Neosartorya fischeri (Aspergillus fischeri)
    • Wyatt, T.T., Gerwig, G.J., Kamerling, J.P., Wösten, H.A.B., and Dijksterhuis, J. (2015b) Novel trehalose-based oligosaccharides from extreme stress-tolerant ascospores of Neosartorya fischeri (Aspergillus fischeri). Carbohydr Res 411: 49-55.
    • (2015) Carbohydr Res , vol.411 , pp. 49-55
    • Wyatt, T.T.1    Gerwig, G.J.2    Kamerling, J.P.3    Wösten, H.A.B.4    Dijksterhuis, J.5


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