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Volumn 61, Issue 8, 2009, Pages 838-845

Molecular cold-adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes

Author keywords

Eukaryotic molecular microbiology; Life in the cold; Marine Antarctic protists; NMR protein structures

Indexed keywords

HISTIDINE; PHENYLALANINE; PHEROMONE; TRYPTOPHAN; TYROSINE;

EID: 70350734314     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.228     Document Type: Review
Times cited : (30)

References (39)
  • 1
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne, T., Gerday, C., and Feller, G. (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility, Biochim. Biophys. Acta 1543, 1-10.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 2
    • 23844458318 scopus 로고    scopus 로고
    • Increased flexibility as a strategy for cold adaptation
    • Olufsen, M., Smalas, A. O., Moe, E., and Brandsdal, B. O. (2005) Increased flexibility as a strategy for cold adaptation, J. Biol. Chem. 280, 18042-18048.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18042-18048
    • Olufsen, M.1    Smalas, A.O.2    Moe, E.3    Brandsdal, B.O.4
  • 3
    • 30144439453 scopus 로고    scopus 로고
    • Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family
    • Adekoya, O. A., Helland, R., Willassen, N. P., and Sylte, I. (2006) Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family, Proteins 62, 435-449.
    • (2006) Proteins , vol.62 , pp. 435-449
    • Adekoya, O.A.1    Helland, R.2    Willassen, N.P.3    Sylte, I.4
  • 4
    • 34548383957 scopus 로고    scopus 로고
    • Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasichemical approximation
    • Goldstein, R. A. (2007) Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: insights from the quasichemical approximation. Protein Sci. 16, 1887-1895.
    • (2007) Protein Sci. , vol.16 , pp. 1887-1895
    • Goldstein, R.A.1
  • 6
    • 77951076113 scopus 로고    scopus 로고
    • Psychrophiles and polar regions
    • Deming, J. W. (2006) Psychrophiles and polar regions. Nature Rev. Microbiol. 4, 301-309.
    • (2006) Nature Rev. Microbiol. , vol.4 , pp. 301-309
    • Deming, J.W.1
  • 7
    • 33846314770 scopus 로고    scopus 로고
    • Cold-loving microbes, plants, and animals-fundamental and applied aspects
    • Margesin, R., Neuner, G., and Storey, K. B. (2007) Cold-loving microbes, plants, and animals-fundamental and applied aspects. Naturwissenschaften 94, 77-99.
    • (2007) Naturwissenschaften , vol.94 , pp. 77-99
    • Margesin, R.1    Neuner, G.2    Storey, K.B.3
  • 8
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G. and Gerday, C. (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nature Rev. Microbiol. 1, 200-208.
    • (2003) Nature Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 12
    • 0034731469 scopus 로고    scopus 로고
    • Approaches for deciphering the structural basis of low temperature enzyme activity
    • Sheridan, P. P., Panasik, N., Coombs, J. M., and Brenchely, J. E. (2000) Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim. Biophys. Acta 1543, 417-433.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 417-433
    • Sheridan, P.P.1    Panasik, N.2    Coombs, J.M.3    Brenchely, J.E.4
  • 13
    • 41049100468 scopus 로고    scopus 로고
    • Pheromone evolution in the protozoan ciliate Euplotes: The ability to synthesize diffusible forms is ancestral and secondarily lost
    • Vallesi, A., Di Giuseppe, G., Dini, F., and Luporini, P. (2008) Pheromone evolution in the protozoan ciliate Euplotes: the ability to synthesize diffusible forms is ancestral and secondarily lost. Mol. Phylogenet. Evol. 47, 439-442.
    • (2008) Mol. Phylogenet. Evol. , vol.47 , pp. 439-442
    • Vallesi, A.1    Di Giuseppe, G.2    Dini, F.3    Luporini, P.4
  • 14
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russel, N. J. (2000) Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 4, 83-90.
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russel, N.J.1
  • 15
    • 0027203987 scopus 로고
    • Nuclear magnetic resonance solution structure of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi
    • Brown, L. R., Mronga, S., Bradshaw, R. A., Ortenzi, C., Luporini, P., and Wüthrich, K. (1993) Nuclear magnetic resonance solution structure of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi. J. Mol. Biol. 231, 800-816.
    • (1993) J. Mol. Biol. , vol.231 , pp. 800-816
    • Brown, L.R.1    Mronga, S.2    Bradshaw, R.A.3    Ortenzi, C.4    Luporini, P.5    Wüthrich, K.6
  • 17
    • 0028090090 scopus 로고
    • The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi
    • Ottiger, M., Szyperski, T., Luginbühl, P., Ortenzi, C., Luporini, P., Bradshaw, R. A., and Wüthrich, K. (1994) The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi. Protein Sci. 3, 1515-1526. (Pubitemid 24314470)
    • (1994) Protein Science , vol.3 , Issue.9 , pp. 1515-1526
    • Ottiger, M.1    Szyperski, T.2    Luginbuhl, P.3    Ortenzi, C.4    Luporini, P.5    Bradshaw, R.A.6    Wuthrich, K.7
  • 18
    • 0028030114 scopus 로고
    • Structure comparison of the NMR structures of the pheromones Er-1, Er-2, and Er-10 from Euplotes raikovi
    • Luginbühl, P., Ottiger, M., Mronga, S., and Wüthrich, K. (1994) Structure comparison of the NMR structures of the pheromones Er-1, Er-2, and Er-10 from Euplotes raikovi. Protein Sci. 3, 1537-1546.
    • (1994) Protein Sci. , vol.3 , pp. 1537-1546
    • Luginbühl, P.1    Ottiger, M.2    Mronga, S.3    Wüthrich, K.4
  • 19
    • 0030056640 scopus 로고    scopus 로고
    • The NMR solution structure of the pheromone Er-11 from the ciliated protozoan Euplotes raikovi
    • Luginbühl, P., Wu, J., Zerbe, O., Ortenzi, C., Luporini, P., and Wüthrich, K. (1996) The NMR solution structure of the pheromone Er-11 from the ciliated protozoan Euplotes raikovi, Protein Sci. 5, 1512-1522.
    • (1996) Protein Sci. , vol.5 , pp. 1512-1522
    • Luginbühl, P.1    Wu, J.2    Zerbe, O.3    Ortenzi, C.4    Luporini, P.5    Wüthrich, K.6
  • 21
    • 0035834466 scopus 로고    scopus 로고
    • NMR structure of the Euplotes raikovi pheromone Er-23 and identification of its five disulfide bonds
    • Zahn, R., Damberger, F., Ortenzi, C., Luporini, P., and Wüthrich, K. (2001) NMR structure of the Euplotes raikovi pheromone Er-23 and identification of its five disulfide bonds. J. Mol. Biol. 313, 923-931.
    • (2001) J. Mol. Biol. , vol.313 , pp. 923-931
    • Zahn, R.1    Damberger, F.2    Ortenzi, C.3    Luporini, P.4    Wüthrich, K.5
  • 23
    • 34547944216 scopus 로고    scopus 로고
    • Cold-adaptation in sea-waterborne signal proteins: Sequence and NMR structure of the pheromone En-6 from the Antarctic ciliate Euplotes nobilii
    • Pedrini, B., Placzek, W. J., Koculi, E., Alimenti, C., La Terza, A., Luporini, P., and Wüthrich, K. (2007) Cold-adaptation in sea-waterborne signal proteins: sequence and NMR structure of the pheromone En-6 from the Antarctic ciliate Euplotes nobilii. J. Mol. Biol. 372, 277-286.
    • (2007) J. Mol. Biol. , vol.372 , pp. 277-286
    • Pedrini, B.1    Placzek, W.J.2    Koculi, E.3    Alimenti, C.4    La Terza, A.5    Luporini, P.6    Wüthrich, K.7
  • 24
    • 0842335789 scopus 로고
    • Sex in ciliates
    • Jones J. G., ed.. Plenum Press, New York
    • Dini, F. and Nyberg, D. (1993) Sex in ciliates. In Advances in Microbial Ecology. (Jones J. G., ed.). 13, pp. 85-153, Plenum Press, New York.
    • (1993) Advances in Microbial Ecology , vol.13 , pp. 85-153
    • Dini, F.1    Nyberg, D.2
  • 25
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • Bae, E. and Phillips, G. N. (2004) Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J. Biol. Chem. 279, 28202-28208.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips, G.N.2
  • 26
    • 34047259479 scopus 로고    scopus 로고
    • Sequence and structural parameters enhancing adaptation of protein to low temperatures
    • Aahandideh, S., Abdolmaleki, P., Jahandideh, M., and Asadabadi, E. B. (2007) Sequence and structural parameters enhancing adaptation of protein to low temperatures. J. Theor. Biol. 246, 159-166.
    • (2007) J. Theor. Biol. , vol.246 , pp. 159-166
    • Aahandideh, S.1    Abdolmaleki, P.2    Jahandideh, M.3    Asadabadi, E.B.4
  • 27
    • 0030220170 scopus 로고    scopus 로고
    • The role of protein-solvent interactions in protein unfolding
    • Schiffer, C. A. and Dotsch, V. (1996) The role of protein-solvent interactions in protein unfolding. Curr. Opin. Biotechnol. 7, 428-432.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 428-432
    • Schiffer, C.A.1    Dotsch, V.2
  • 29
    • 0037172796 scopus 로고    scopus 로고
    • Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study
    • DOI 10.1021/bi025523t
    • Chakravarty, S. and Varadarajan, R. (2002) Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study. Biochemistry 41, 8152-8161. (Pubitemid 34655184)
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 8152-8161
    • Chakravarty, S.1    Varadarajan, R.2
  • 30
    • 3042796482 scopus 로고    scopus 로고
    • Substitution of aspartic acid with glutamic acid increases the unfolding transition temperature of a protein
    • Lee, D. Y., Kim, K. A., Yu, Y. G., and Kim, K. S. (2004) Substitution of aspartic acid with glutamic acid increases the unfolding transition temperature of a protein. Biochem. Biophys. Res. Commun. 320, 900-906.
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 900-906
    • Lee, D.Y.1    Kim, K.A.2    Yu, Y.G.3    Kim, K.S.4
  • 31
    • 0028800215 scopus 로고
    • A cooperative model for ligand recognition and cell adhesion: Evidence from the molecular packing in the 1.6 A crystal structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi
    • Weiss, M. S., Anderson, D. H., Raffioni, S., Bradshaw, R. A., Ortenzi, C., Luporini, P., and Eisenberg, D. (1995) A cooperative model for ligand recognition and cell adhesion: evidence from the molecular packing in the 1.6 A crystal structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi. Proc. Natl. Acad. Sci. USA 92, 10172-10176.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10172-10176
    • Weiss, M.S.1    Anderson, D.H.2    Raffioni, S.3    Bradshaw, R.A.4    Ortenzi, C.5    Luporini, P.6    Eisenberg, D.7
  • 32
    • 22444435626 scopus 로고    scopus 로고
    • Autocrine, mitogenic pheromone receptor loop of the ciliate Euplotes raikovi: Pheromone-induced receptor internalization
    • DOI 10.1128/EC.4.7.1221-1227.2005
    • Vallesi, A., Ballarini, P., Di Pretoro, B., Alimenti, C., Miceli, C., and Luporini, P. (2005) The autocrine, mitogenic pheromone-receptor loop of the ciliate Euplotes raikovi: pheromone-induced receptor internalization. Eukaryot. Cell 4, 1221-1227. (Pubitemid 41004135)
    • (2005) Eukaryotic Cell , vol.4 , Issue.7 , pp. 1221-1227
    • Vallesi, A.1    Ballarini, P.2    Di Pretoro, B.3    Alimenti, C.4    Miceli, C.5    Luporini, P.6
  • 33
    • 34547680284 scopus 로고    scopus 로고
    • Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability
    • Fedoy, A. E., Yang, N., Martinez, A., Leiros, H. K. S., and Steen, I. H. (2007) Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability. J. Mol. Biol. 372, 130-149.
    • (2007) J. Mol. Biol. , vol.372 , pp. 130-149
    • Fedoy, A.E.1    Yang, N.2    Martinez, A.3    Leiros, H.K.S.4    Steen, I.H.5
  • 35
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley, S. K. and Petsko, G. A. (1985) Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229, 23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 36
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan, N. and Vishveshwara, S. (2000) Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng. 13, 753-761.
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 37
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan, N. and Vishveshwara, S. (2000) Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng. 13, 753-761.
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2


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