메뉴 건너뛰기




Volumn 34, Issue 4, 1998, Pages 655-660

RUBISCO adaptation to low temperatures: A comparative study in psychrophilic and mesophilic unicellular algae

Author keywords

Chlamydomonas; Chloromonas; Molecular adaptation to low temperatures; Psychrophilic algae; RUBISCO

Indexed keywords

CHLAMYDOMONAS REINHARDTII; CHLOROMONAS;

EID: 0031684804     PISSN: 00223646     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1529-8817.1998.340655.x     Document Type: Article
Times cited : (71)

References (34)
  • 2
    • 0027476253 scopus 로고
    • Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile Psychrobacter immobilis B10
    • Arpigny, J-L., Feller, G. & Gerday, C. 1993. Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile Psychrobacter immobilis B10. Biochem. Biophys. Acta 1171:331-3.
    • (1993) Biochem. Biophys. Acta , vol.1171 , pp. 331-333
    • Arpigny, J.-L.1    Feller, G.2    Gerday, C.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-54.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000170741 scopus 로고
    • Thermal instability of rihulose-1,5-bisphosphate carboxylase/oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii
    • Chen, Z., Hong, S. & Spreitzer, R. J. 1993. Thermal instability of rihulose-1,5-bisphosphate carboxylase/oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii. Plant Physiol. 101:1189-94.
    • (1993) Plant Physiol. , vol.101 , pp. 1189-1194
    • Chen, Z.1    Hong, S.2    Spreitzer, R.J.3
  • 6
    • 0026801565 scopus 로고
    • Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0 Åresolution
    • Curmi, P. M. G., Gascio, D., Sweet, R. M., Eisenberg, D. & Schreuder, H. 1992. Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0 Åresolution. J. Biol. Chem. 267:16980-9.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16980-16989
    • Curmi, P.M.G.1    Gascio, D.2    Sweet, R.M.3    Eisenberg, D.4    Schreuder, H.5
  • 7
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, characterization and sequence of the heat labile subtilisin from the antarctic psychrophile Bacillus TA41
    • Davail, S., Feller, G., Narinx, E. & Gerday, C. 1994. Cold adaptation of proteins. Purification, characterization and sequence of the heat labile subtilisin from the antarctic psychrophile Bacillus TA41. J. Biol. Chem. 269:17448-53.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 8
    • 0020376662 scopus 로고
    • Sequence of the chloroplast DNA region of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes
    • Dron, M., Rahire, M. & Rochaix, J-D. 1982. Sequence of the chloroplast DNA region of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes. J. Mol. Biol. 162:775-93.
    • (1982) J. Mol. Biol. , vol.162 , pp. 775-793
    • Dron, M.1    Rahire, M.2    Rochaix, J.-D.3
  • 9
    • 0031040836 scopus 로고    scopus 로고
    • Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and the inability of Rubisco activase to restore activity of heat-denatured Rubisco
    • Eckardt, N. A. & Portis, A. R. 1997. Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and the inability of Rubisco activase to restore activity of heat-denatured Rubisco. Plant Physiol. 113:243-8.
    • (1997) Plant Physiol. , vol.113 , pp. 243-248
    • Eckardt, N.A.1    Portis, A.R.2
  • 10
    • 0026673888 scopus 로고
    • Purification, characterization and nucleotide sequence of the thermo-labile α-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23
    • Feller, G., Lonhieune, T., Decroanne, C., Libioulle, C., van Beemen, J. & Gerday, C. 1992. Purification, characterization and nucleotide sequence of the thermo-labile α-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23. J. Biol. Chem. 267:5217-21.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhieune, T.2    Decroanne, C.3    Libioulle, C.4    Van Beemen, J.5    Gerday, C.6
  • 12
    • 0028289989 scopus 로고
    • Stability and structural analysis of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
    • Feller, G., Payan, F., Theys, F., Qian, M., Haser, R. & Gerday, C. 1994. Stability and structural analysis of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem. 222:441-7.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 441-447
    • Feller, G.1    Payan, F.2    Theys, F.3    Qian, M.4    Haser, R.5    Gerday, C.6
  • 13
    • 0028119032 scopus 로고
    • Phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase gene expression in response to elevated temperatures in C3 and C4 plants native to hot and temperate climates
    • Ghosh, S., Glick, B. R., Heikkila, J. J. & Dumbroff, E. B. 1994. Phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase gene expression in response to elevated temperatures in C3 and C4 plants native to hot and temperate climates. Plant Physiol. Biochem. 32:45-54.
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 45-54
    • Ghosh, S.1    Glick, B.R.2    Heikkila, J.J.3    Dumbroff, E.B.4
  • 14
    • 0023042758 scopus 로고
    • Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/ oxygenase in Chlamydomonas reinhardtii
    • Goldschmidt-Clermont, M. & Rahire, M. 1986. Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/ oxygenase in Chlamydomonas reinhardtii. J. Mol. Biol. 191:421-32.
    • (1986) J. Mol. Biol. , vol.191 , pp. 421-432
    • Goldschmidt-Clermont, M.1    Rahire, M.2
  • 15
    • 0028843014 scopus 로고
    • Rubisco synthesis, assembly, mechanism, and regulation
    • Gutteridge, S. & Gatenby, A. A. 1995. Rubisco synthesis, assembly, mechanism, and regulation. Plant Cell 7:809-19.
    • (1995) Plant Cell , vol.7 , pp. 809-819
    • Gutteridge, S.1    Gatenby, A.A.2
  • 16
    • 0842286227 scopus 로고
    • Cold acclimation and freezing stress tolerance: Role of protein metabolism
    • Guy, C. L. 1990. Cold acclimation and freezing stress tolerance: role of protein metabolism. Annu. Rev. Plant Physiol. Plant Mol. Biol. 41:187-223.
    • (1990) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.41 , pp. 187-223
    • Guy, C.L.1
  • 18
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Hartman, F. C. & Harpel, M. R. 1994. Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase. Annu. Rev. Biochem. 63:197-234.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 19
    • 0003905372 scopus 로고
    • Princeton University Press, Princeton, New Jersey
    • Hochachka, P. & Somero, G. N. 1984. In Biochemical Adaptation. Princeton University Press, Princeton, New Jersey, pp. 355-449.
    • (1984) Biochemical Adaptation , pp. 355-449
    • Hochachka, P.1    Somero, G.N.2
  • 20
    • 0030967199 scopus 로고    scopus 로고
    • Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase
    • Hong, S. & Spreitzer, R. J. 1997. Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase. J. Biol. Chem. 272:11114-7.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11114-11117
    • Hong, S.1    Spreitzer, R.J.2
  • 21
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose-1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution
    • Knight, S., Andersson, I. & Branden, C-I. 1990. Crystallographic analysis of ribulose-1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution. J. Mol. Biol. 215:113-60.
    • (1990) J. Mol. Biol. , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Branden, C.-I.3
  • 22
    • 0029739286 scopus 로고    scopus 로고
    • Effect of temperature on two enzymes from a psychrophilic Chloromonas (Chlorophyta)
    • Loppes, R., Devos, N., Willem, S., Barthelemy, P. & Matagne, R. F. 1996. Effect of temperature on two enzymes from a psychrophilic Chloromonas (Chlorophyta). J. Phycol. 32:276-8.
    • (1996) J. Phycol. , vol.32 , pp. 276-278
    • Loppes, R.1    Devos, N.2    Willem, S.3    Barthelemy, P.4    Matagne, R.F.5
  • 23
    • 0026608847 scopus 로고
    • Structure of a gene encoding heat shock protein HSP70 from the unicellular alga Chlamydomonas reinhardtii
    • Müller, F. W., Gabor, L. I. & Beck, C. F. 1992. Structure of a gene encoding heat shock protein HSP70 from the unicellular alga Chlamydomonas reinhardtii. Gene 111:165-73.
    • (1992) Gene , vol.111 , pp. 165-173
    • Müller, F.W.1    Gabor, L.I.2    Beck, C.F.3
  • 24
    • 0000528384 scopus 로고
    • Structure determination and refinement of ribulose-1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301
    • Newman, J., Branden, C-I. & Jones, A. 1993. Structure determination and refinement of ribulose-1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301. Acta Crystallogr. D49:548-60.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 548-560
    • Newman, J.1    Branden, C.-I.2    Jones, A.3
  • 25
    • 0024987366 scopus 로고
    • The purification and preliminary x-ray diffraction studies of recombinant Synechococcus ribulose-1,5-bisphosphate carboxylase/oxygenase from Escherichia coli
    • Newman, J. & Gutteridge, S. 1990. The purification and preliminary x-ray diffraction studies of recombinant Synechococcus ribulose-1,5-bisphosphate carboxylase/oxygenase from Escherichia coli. J. Biol. Chem. 265:15154-9.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15154-15159
    • Newman, J.1    Gutteridge, S.2
  • 26
    • 0025781599 scopus 로고
    • An intra-dimeric crosslink of large subunits of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase is formed by oxidation of cysteine 247
    • Ranty, B., Lorimer, G. & Gutteridge, S. 1991. An intra-dimeric crosslink of large subunits of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase is formed by oxidation of cysteine 247. Eur. J. Biochem. 200:353-8.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 353-358
    • Ranty, B.1    Lorimer, G.2    Gutteridge, S.3
  • 27
    • 0018880548 scopus 로고
    • Restriction fragments from Chlamydomonas chloroplast DNA
    • Rochaix, J-D. 1978. Restriction fragments from Chlamydomonas chloroplast DNA. Methods Enzymol. 65:785-95.
    • (1978) Methods Enzymol. , vol.65 , pp. 785-795
    • Rochaix, J.-D.1
  • 28
    • 0001734325 scopus 로고
    • Physiology and molecular biology of psychrophilic microorganisms
    • Herbert, R. A. & Sharp, R. J. [Eds.] Chapman and Hall, New York
    • Russell, N. J. 1992. Physiology and molecular biology of psychrophilic microorganisms. In Herbert, R. A. & Sharp, R. J. [Eds.] Molecular Biology and Biotechnology of Extremophiles. Chapman and Hall, New York, pp. 203-4.
    • (1992) Molecular Biology and Biotechnology of Extremophiles , pp. 203-204
    • Russell, N.J.1
  • 30
    • 0017070348 scopus 로고
    • Temperature: A 'shaping force' in protein evolution
    • Somero, G. N. & Low, P. S. 1976. Temperature: a 'shaping force' in protein evolution. Biochem. Soc. Symp. 41:32-42.
    • (1976) Biochem. Soc. Symp. , vol.41 , pp. 32-42
    • Somero, G.N.1    Low, P.S.2
  • 32
    • 0018976083 scopus 로고
    • Non-mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity
    • Spreitzer, R. J. & Mets, L. J. 1980. Non-mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity. Nature 285:114-5.
    • (1980) Nature , vol.285 , pp. 114-115
    • Spreitzer, R.J.1    Mets, L.J.2
  • 33
    • 0000266632 scopus 로고
    • 2 and mercurials on the circular dichroism, thermal stability and light scattering of ribulose-1,5-bisphosphate carboxylase from alfalfa, spinach and tobacco
    • 2 and mercurials on the circular dichroism, thermal stability and light scattering of ribulose-1,5-bisphosphate carboxylase from alfalfa, spinach and tobacco. Plant Physiol. 68:808-13.
    • (1981) Plant Physiol. , vol.68 , pp. 808-813
    • Tomimatsu, Y.1    Donovan, J.W.2
  • 34
    • 85051612826 scopus 로고
    • Plant genome organisation and its relationship to classical plant genetics
    • Hall, T. C. & Davies, J. W. [Eds.] CRC Press, Boca Raton, Florida
    • Walbot, V. & Goldberg, R. 1978. Plant genome organisation and its relationship to classical plant genetics. In Hall, T. C. & Davies, J. W. [Eds.] Nucleic Acids in Plants. CRC Press, Boca Raton, Florida, pp. 3-40.
    • (1978) Nucleic Acids in Plants , pp. 3-40
    • Walbot, V.1    Goldberg, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.