메뉴 건너뛰기




Volumn 71, Issue 4, 2007, Pages 576-599

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; RUBISCO LIKE PROTEIN; SULFUR; UNCLASSIFIED DRUG;

EID: 37349069540     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.00015-07     Document Type: Review
Times cited : (292)

References (80)
  • 1
    • 18744382506 scopus 로고    scopus 로고
    • Prottest: Selection of best-fit models of protein evolution
    • Abascal, F., R. Zardoya, and D. Posada. 2005. Prottest: selection of best-fit models of protein evolution. Bioinformatics 21:2104-2105.
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 2
    • 0038681416 scopus 로고    scopus 로고
    • Diversity of ribulose-1,5-bisphosphate carboxylase/oxygenase large-subunit genes from groundwater and aquifer microorganisms
    • Alfreider, A., C. Vogt, D. Hoffmann, and W. Babel. 2003. Diversity of ribulose-1,5-bisphosphate carboxylase/oxygenase large-subunit genes from groundwater and aquifer microorganisms. Microb. Ecol. 45:317-328.
    • (2003) Microb. Ecol , vol.45 , pp. 317-328
    • Alfreider, A.1    Vogt, C.2    Hoffmann, D.3    Babel, W.4
  • 3
    • 0037304408 scopus 로고    scopus 로고
    • Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins
    • Anantharaman, V., L. Aravind, and E. V. Koonin. 2003. Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins. Curr. Opin. Chem. Biol. 7:12-20.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 12-20
    • Anantharaman, V.1    Aravind, L.2    Koonin, E.V.3
  • 4
    • 0030003964 scopus 로고    scopus 로고
    • Large structures at high resolution: The 1.6 Å crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate
    • Andersson, I. 1996. Large structures at high resolution: the 1.6 Å crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate. J. Mol. Biol. 259:160-174.
    • (1996) J. Mol. Biol , vol.259 , pp. 160-174
    • Andersson, I.1
  • 5
    • 0037561915 scopus 로고    scopus 로고
    • Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Andersson, I., and T. C. Taylor. 2003. Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase. Arch. Biochem. Biophys. 414:130-140.
    • (2003) Arch. Biochem. Biophys , vol.414 , pp. 130-140
    • Andersson, I.1    Taylor, T.C.2
  • 7
    • 20444419762 scopus 로고    scopus 로고
    • Was photosynthetic Rubisco recruited by acquisitive evolution from Rubisco-like proteins involved in sulfur metabolism?
    • Ashida, H., A. Danchin, and A. Yokota. 2005. Was photosynthetic Rubisco recruited by acquisitive evolution from Rubisco-like proteins involved in sulfur metabolism? Res. Microbiol. 156:611-618.
    • (2005) Res. Microbiol , vol.156 , pp. 611-618
    • Ashida, H.1    Danchin, A.2    Yokota, A.3
  • 8
    • 0141993683 scopus 로고    scopus 로고
    • A functional link between Rubisco-like protein of Bacillus and photosynthetic Rubisco
    • Ashida, H., Y. Saito, C. Kojima, K. Kobayashi, N. Ogasawara, and A. Yokota. 2003. A functional link between Rubisco-like protein of Bacillus and photosynthetic Rubisco. Science 302:286-290.
    • (2003) Science , vol.302 , pp. 286-290
    • Ashida, H.1    Saito, Y.2    Kojima, C.3    Kobayashi, K.4    Ogasawara, N.5    Yokota, A.6
  • 12
    • 37349044305 scopus 로고    scopus 로고
    • Sulfur oxidation in Chlorobium tepidum (syn. Chlorobaculum tepidum): Genetic and proteomic analyses
    • C. Dahl and C. G. Friedrich ed, in press. Springer, New York, NY
    • Chan, L. K., R. Morgan-Kiss, and T. E. Hanson. Sulfur oxidation in Chlorobium tepidum (syn. Chlorobaculum tepidum): genetic and proteomic analyses. In C. Dahl and C. G. Friedrich (ed.), Proceedings of the International Symposium on Microbial Sulfur Metabolism, in press. Springer, New York, NY.
    • Proceedings of the International Symposium on Microbial Sulfur Metabolism
    • Chan, L.K.1    Morgan-Kiss, R.2    Hanson, T.E.3
  • 14
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: A fingerprint of proteins that physically interact
    • Dandekar, T., B. Snel, M. Huynen, and P. Bork. 1998. Conservation of gene order: a fingerprint of proteins that physically interact. Trends Biochem. Sci. 23:324-328.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 15
    • 0026559592 scopus 로고
    • The consistency of several phytogeny-inference methods under varying evolutionary rates
    • DeBry, R. W. 1992. The consistency of several phytogeny-inference methods under varying evolutionary rates. Mol. Biol. Evol. 9:537-551.
    • (1992) Mol. Biol. Evol , vol.9 , pp. 537-551
    • DeBry, R.W.1
  • 16
    • 0029897169 scopus 로고    scopus 로고
    • Rampant horizontal transfer and duplication of Rubisco genes in eubacteria and plastids
    • Delwiche, C. F., and J. D. Palmer. 1996. Rampant horizontal transfer and duplication of Rubisco genes in eubacteria and plastids. Mol. Biol. Evol. 13:873-882.
    • (1996) Mol. Biol. Evol , vol.13 , pp. 873-882
    • Delwiche, C.F.1    Palmer, J.D.2
  • 18
    • 0033603539 scopus 로고    scopus 로고
    • Phylogenetic classification and the universal tree
    • Doolittle, W. F. 1999. Phylogenetic classification and the universal tree. Science 284:2124-2129.
    • (1999) Science , vol.284 , pp. 2124-2129
    • Doolittle, W.F.1
  • 19
    • 2642524290 scopus 로고    scopus 로고
    • 2 assimilation, nitrogen fixation, hydrogen metabolism and energy generation
    • 2 assimilation, nitrogen fixation, hydrogen metabolism and energy generation. FEMS Microbiol. Rev. 28:353-376.
    • (2004) FEMS Microbiol. Rev , vol.28 , pp. 353-376
    • Dubbs, J.M.1    Tabita, F.R.2
  • 20
    • 0034685616 scopus 로고    scopus 로고
    • The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
    • Duff, A. P., T. J. Andrews, and P. M. Curmi. 2000. The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J. Mol. Biol. 298:903-916.
    • (2000) J. Mol. Biol , vol.298 , pp. 903-916
    • Duff, A.P.1    Andrews, T.J.2    Curmi, P.M.3
  • 21
    • 49249144575 scopus 로고
    • Most abundant protein in the world
    • Ellis, R. J. 1979. Most abundant protein in the world. Trends Biochem. Sci. 4:241-244.
    • (1979) Trends Biochem. Sci , vol.4 , pp. 241-244
    • Ellis, R.J.1
  • 22
    • 0035318376 scopus 로고    scopus 로고
    • Phylogenetic diversity of ribulose-1,5-bisphosphate carboxylase/oxygenase large-subunit genes from deep-sea microorganisms
    • Elsaied, H., and T. Naganuma. 2001. Phylogenetic diversity of ribulose-1,5-bisphosphate carboxylase/oxygenase large-subunit genes from deep-sea microorganisms. Appl. Environ. Microbiol. 67:1751-1765.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 1751-1765
    • Elsaied, H.1    Naganuma, T.2
  • 23
    • 33846137706 scopus 로고    scopus 로고
    • Composition of archaeal, bacterial, and eukaryal RuBisCO genotypes in three Western Pacific arc hydrothermal vent systems
    • Elsaied, H. E., H. Kimura, and T. Naganuma. 2007. Composition of archaeal, bacterial, and eukaryal RuBisCO genotypes in three Western Pacific arc hydrothermal vent systems. Extremophiles 11:191-202.
    • (2007) Extremophiles , vol.11 , pp. 191-202
    • Elsaied, H.E.1    Kimura, H.2    Naganuma, T.3
  • 24
    • 0033523989 scopus 로고    scopus 로고
    • Protein interaction maps for complete genomes based on gene fusion events
    • Enright, A. J., I. Iliopoulos, N. C. Kyrpides, and C. A. Ouzounis. 1999. Protein interaction maps for complete genomes based on gene fusion events. Nature 402:86-90.
    • (1999) Nature , vol.402 , pp. 86-90
    • Enright, A.J.1    Iliopoulos, I.2    Kyrpides, N.C.3    Ouzounis, C.A.4
  • 25
    • 0033582465 scopus 로고    scopus 로고
    • Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1
    • Ezaki, S., N. Maeda, T. Kishimoto, H. Atomi, and T. Imanaka. 1999. Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1. J. Biol. Chem. 274:5078-5082.
    • (1999) J. Biol. Chem , vol.274 , pp. 5078-5082
    • Ezaki, S.1    Maeda, N.2    Kishimoto, T.3    Atomi, H.4    Imanaka, T.5
  • 26
    • 4544272017 scopus 로고    scopus 로고
    • Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea
    • Finn, M. W., and F. R. Tabita. 2004. Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea. J. Bacteriol. 186:6360-6366.
    • (2004) J. Bacteriol , vol.186 , pp. 6360-6366
    • Finn, M.W.1    Tabita, F.R.2
  • 27
    • 0038643328 scopus 로고    scopus 로고
    • Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea
    • Finn, M. W., and F. R. Tabita. 2003. Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea. J. Bacteriol. 185:3049-3059.
    • (2003) J. Bacteriol , vol.185 , pp. 3049-3059
    • Finn, M.W.1    Tabita, F.R.2
  • 29
    • 0017620115 scopus 로고
    • Different molecular forms of D-ribulose-1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides
    • Gibson, J. L., and F. R. Tabita. 1977. Different molecular forms of D-ribulose-1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides. J. Biol. Chem. 252:943-949.
    • (1977) J. Biol. Chem , vol.252 , pp. 943-949
    • Gibson, J.L.1    Tabita, F.R.2
  • 30
    • 0347506350 scopus 로고    scopus 로고
    • Insights into the stress response and sulfur metabolism revealed by proteome analysis of a Chlorobium tepidum mutant lacking the Rubisco-like protein
    • Hanson, T. E., and F. R. Tabita. 2003. Insights into the stress response and sulfur metabolism revealed by proteome analysis of a Chlorobium tepidum mutant lacking the Rubisco-like protein. Photosynth. Res. 78:231-248.
    • (2003) Photosynth. Res , vol.78 , pp. 231-248
    • Hanson, T.E.1    Tabita, F.R.2
  • 31
    • 0035836695 scopus 로고    scopus 로고
    • A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress
    • Hanson, T. E., and F. R. Tabita. 2001. A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress. Proc. Natl. Acad. Sci. USA 98:4397-4402.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4397-4402
    • Hanson, T.E.1    Tabita, F.R.2
  • 32
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Hartman, F. C., and M. R. Harpel. 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
  • 33
    • 34047237283 scopus 로고    scopus 로고
    • Mechanistic diversity in the RuBisCO superfamily: The "enolase" in the methionine salvage pathway in Geobacillus kaustophilus
    • Imker, H. J., A. A. Fedorov, E. V. Fedorov, S. C. Almo, and J. A. Gerlt. 2007. Mechanistic diversity in the RuBisCO superfamily: the "enolase" in the methionine salvage pathway in Geobacillus kaustophilus. Biochemistry 46:4077-4089.
    • (2007) Biochemistry , vol.46 , pp. 4077-4089
    • Imker, H.J.1    Fedorov, A.A.2    Fedorov, E.V.3    Almo, S.C.4    Gerlt, J.A.5
  • 34
    • 33746645973 scopus 로고    scopus 로고
    • Gene diversity and organization in rbcL-containing genome fragments from uncultivated Synechococcus in the Gulf of Mexico
    • John, D. E., B. Wawrik, F. Tabita, and J. H. Paul. 2006. Gene diversity and organization in rbcL-containing genome fragments from uncultivated Synechococcus in the Gulf of Mexico. Mar. Ecol. Prog. Ser. 316:23-33.
    • (2006) Mar. Ecol. Prog. Ser , vol.316 , pp. 23-33
    • John, D.E.1    Wawrik, B.2    Tabita, F.3    Paul, J.H.4
  • 35
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution. Subunit interactions and active site
    • Knight, S., I. Andersson, and C. I. Branden. 1990. Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution. Subunit interactions and active site. J. Mol. Biol. 215:113-160.
    • (1990) J. Mol. Biol , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Branden, C.I.3
  • 36
    • 0033537899 scopus 로고    scopus 로고
    • Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts
    • Kopp, J., S. Kopriva, K. H. Suss, and G. E. Schulz. 1999. Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts. J. Mol. Biol. 287:761-771.
    • (1999) J. Mol. Biol , vol.287 , pp. 761-771
    • Kopp, J.1    Kopriva, S.2    Suss, K.H.3    Schulz, G.E.4
  • 38
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar, S., K. Tamura, and M. Nei. 2004. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5:150-163.
    • (2004) Brief. Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 39
    • 18944389308 scopus 로고    scopus 로고
    • Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum
    • Li, H., M. R. Sawaya, F. R. Tabita, and D. Eisenberg. 2005. Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum. Structure 13:779-789.
    • (2005) Structure , vol.13 , pp. 779-789
    • Li, H.1    Sawaya, M.R.2    Tabita, F.R.3    Eisenberg, D.4
  • 40
    • 0027943051 scopus 로고
    • Transcription control of ribulose bisphosphate carboxylase/oxygenase activase and adjacent genes in Anabaena species
    • Li, L. A., and F. R. Tabita. 1994. Transcription control of ribulose bisphosphate carboxylase/oxygenase activase and adjacent genes in Anabaena species. J. Bacteriol. 176:6697-6706.
    • (1994) J. Bacteriol , vol.176 , pp. 6697-6706
    • Li, L.A.1    Tabita, F.R.2
  • 43
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte, E. M., M. Pellegrini, H. L. Ng, D. W. Rice, T. O. Yeates, and D. Eisenberg. 1999. Detecting protein function and protein-protein interactions from genome sequences. Science 285:751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 44
    • 0028977898 scopus 로고
    • A nuclear-encoded form II RuBisCO in dinoflagellates
    • Morse, D., P. Salois, P. Markovic, and J. W. Hastings. 1995. A nuclear-encoded form II RuBisCO in dinoflagellates. Science 268:1622- 1624.
    • (1995) Science , vol.268 , pp. 1622-1624
    • Morse, D.1    Salois, P.2    Markovic, P.3    Hastings, J.W.4
  • 45
    • 0036202171 scopus 로고    scopus 로고
    • Prediction of gene function in methylthioadenosine recycling from regulatory signals
    • Murphy, B. A., F. J. Grundy, and T. M. Henkin. 2002. Prediction of gene function in methylthioadenosine recycling from regulatory signals. J. Bacteriol. 184:2314-2318.
    • (2002) J. Bacteriol , vol.184 , pp. 2314-2318
    • Murphy, B.A.1    Grundy, F.J.2    Henkin, T.M.3
  • 46
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano, N., C. A. Orengo, and J. M. Thornton. 2002. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 321:741-765.
    • (2002) J. Mol. Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 47
    • 2942608404 scopus 로고    scopus 로고
    • Analysis of facultative lithotroph distribution and diversity on volcanic deposits by use of the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase
    • Nanba, K., G. M. King, and K. Dunfield. 2004. Analysis of facultative lithotroph distribution and diversity on volcanic deposits by use of the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase. Appl. Environ. Microbiol. 70:2245-2253.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 2245-2253
    • Nanba, K.1    King, G.M.2    Dunfield, K.3
  • 48
    • 0347719528 scopus 로고    scopus 로고
    • Evaluation of protein fold comparison servers
    • Novotny, M., D. Madsen, and G. J. Kleywegt. 2004. Evaluation of protein fold comparison servers. Proteins 54:260-270.
    • (2004) Proteins , vol.54 , pp. 260-270
    • Novotny, M.1    Madsen, D.2    Kleywegt, G.J.3
  • 49
    • 0034714290 scopus 로고    scopus 로고
    • Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Nonconservative substitution in the large subunit alters species specificity of protein interaction
    • Ott, C. M., B. D. Smith, A. R. Portis, Jr., and R. J. Spreitzer. 2000. Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Nonconservative substitution in the large subunit alters species specificity of protein interaction. J. Biol. Chem. 275:26241- 26244.
    • (2000) J. Biol. Chem , vol.275 , pp. 26241-26244
    • Ott, C.M.1    Smith, B.D.2    Portis Jr., A.R.3    Spreitzer, R.J.4
  • 51
    • 0029608860 scopus 로고
    • Rubisco rules fall; gene transfer triumphs
    • Palmer, J. D. 1995. Rubisco rules fall; gene transfer triumphs. Bioessays 17:1005-1008.
    • (1995) Bioessays , vol.17 , pp. 1005-1008
    • Palmer, J.D.1
  • 52
    • 0030098202 scopus 로고    scopus 로고
    • Rubisco surprises in dinoflagellates
    • Palmer, J. D. 1996. Rubisco surprises in dinoflagellates. Plant Cell 8:343-345.
    • (1996) Plant Cell , vol.8 , pp. 343-345
    • Palmer, J.D.1
  • 55
    • 0030868741 scopus 로고    scopus 로고
    • Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities
    • Pichard, S. L., L. Campbell, and J. H. Paul. 1997. Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities. Appl. Environ. Microbiol. 63:3600-3606.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 3600-3606
    • Pichard, S.L.1    Campbell, L.2    Paul, J.H.3
  • 56
    • 0030800147 scopus 로고    scopus 로고
    • Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes
    • Rhee, S., K. D. Parris, C. C. Hyde, S. A. Ahmed, E. W. Miles, and D. R. Davies. 1997. Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes. Biochemistry 36:7664-7680.
    • (1997) Biochemistry , vol.36 , pp. 7664-7680
    • Rhee, S.1    Parris, K.D.2    Hyde, C.C.3    Ahmed, S.A.4    Miles, E.W.5    Davies, D.R.6
  • 57
    • 34047227131 scopus 로고    scopus 로고
    • The complete chloroplast and mitochondrial DNA sequence of Ostreococcus tauri: Organelle genomes of the smallest eukaryote are examples of compaction
    • Robbens, S., E. Derelle, C. Ferraz, J. Wuyts, H. Moreau, and Y. Van de Peer. 2007. The complete chloroplast and mitochondrial DNA sequence of Ostreococcus tauri: organelle genomes of the smallest eukaryote are examples of compaction. Mol. Biol. Evol. 24:956-968.
    • (2007) Mol. Biol. Evol , vol.24 , pp. 956-968
    • Robbens, S.1    Derelle, E.2    Ferraz, C.3    Wuyts, J.4    Moreau, H.5    Van de Peer, Y.6
  • 58
    • 0030096623 scopus 로고    scopus 로고
    • Rubisco in marine symbiotic dinoflagellates: Form II enzymes in eukaryotic oxygenic phototrophs encoded by a nuclear multigene family
    • Rowan, R., S. M. Whitney, A. Fowler, and D. Yellowlees. 1996. Rubisco in marine symbiotic dinoflagellates: form II enzymes in eukaryotic oxygenic phototrophs encoded by a nuclear multigene family. Plant Cell 8:539-553.
    • (1996) Plant Cell , vol.8 , pp. 539-553
    • Rowan, R.1    Whitney, S.M.2    Fowler, A.3    Yellowlees, D.4
  • 59
    • 33847157932 scopus 로고    scopus 로고
    • Archaeal type III RuBisCOs function in a pathway for AMP metabolism
    • Sato, T., H. Atomi, and T. Imanaka. 2007. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315:1003-1006.
    • (2007) Science , vol.315 , pp. 1003-1006
    • Sato, T.1    Atomi, H.2    Imanaka, T.3
  • 60
    • 0038824870 scopus 로고    scopus 로고
    • Saunders, N. F., T. Thomas, P. M. Curmi, J. S. Mattick, E. Kuczek, R. Slade, J. Davis, P. D. Franzmann, D. Boone, K. Rusterholtz, R. Feldman, C. Gates, S. Bench, K. Sowers, K. Kadner, A. Aerts, P. Dehal, C. Detter, T. Glavina, S. Lucas, P. Richardson, F. Larimer, L. Hauser, M. Land, and R. Cavicchioli. 2003. Mechanisms of thermal adaptation revealed from the genomes of the Antarctic archaea Methanogenium frigidum and Methanococcoides burtonii. Genome Res. 13:1580-1588.
    • Saunders, N. F., T. Thomas, P. M. Curmi, J. S. Mattick, E. Kuczek, R. Slade, J. Davis, P. D. Franzmann, D. Boone, K. Rusterholtz, R. Feldman, C. Gates, S. Bench, K. Sowers, K. Kadner, A. Aerts, P. Dehal, C. Detter, T. Glavina, S. Lucas, P. Richardson, F. Larimer, L. Hauser, M. Land, and R. Cavicchioli. 2003. Mechanisms of thermal adaptation revealed from the genomes of the Antarctic archaea Methanogenium frigidum and Methanococcoides burtonii. Genome Res. 13:1580-1588.
  • 62
    • 0027371878 scopus 로고
    • Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form
    • Schreuder, H. A., S. Knight, P. M. Curmi, I. Andersson, D. Cascio, C. I. Branden, and D. Eisenberg. 1993. Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form. Proc. Natl. Acad. Sci. USA 90:9968-9972.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9968-9972
    • Schreuder, H.A.1    Knight, S.2    Curmi, P.M.3    Andersson, I.4    Cascio, D.5    Branden, C.I.6    Eisenberg, D.7
  • 63
    • 19044362589 scopus 로고    scopus 로고
    • The methionine salvage pathway in Bacillus subtilis
    • Sekowska, A., and A. Danchin. 2002. The methionine salvage pathway in Bacillus subtilis. BMC Microbiol. 2:8.
    • (2002) BMC Microbiol , vol.2 , pp. 8
    • Sekowska, A.1    Danchin, A.2
  • 64
    • 0023998613 scopus 로고
    • Essentiality of Lys-329 of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as demonstrated by site-directed mutagenesis
    • Soper, T. S., R. J. Mural, F. W. Larimer, E. H. Lee, R. Machanoff, and F. C. Hartman. 1988. Essentiality of Lys-329 of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as demonstrated by site-directed mutagenesis. Protein Eng. 2:39-44.
    • (1988) Protein Eng , vol.2 , pp. 39-44
    • Soper, T.S.1    Mural, R.J.2    Larimer, F.W.3    Lee, E.H.4    Machanoff, R.5    Hartman, F.C.6
  • 65
    • 16644364478 scopus 로고    scopus 로고
    • An oligonucleotide primer system for amplification of the ribulose-1,5-bisphosphate carboxylase/oxygenase genes of bacteria of various taxonomic groups
    • In Russian
    • Spiridonova, E. M., I. A. Berg, T. V. Kolganova, R. N. Ivanovskii, B. B. Kuznetsov, and T. P. Turova. 2004. An oligonucleotide primer system for amplification of the ribulose-1,5-bisphosphate carboxylase/oxygenase genes of bacteria of various taxonomic groups. Mikrobiologiia 73:377-387. (In Russian.)
    • (2004) Mikrobiologiia , vol.73 , pp. 377-387
    • Spiridonova, E.M.1    Berg, I.A.2    Kolganova, T.V.3    Ivanovskii, R.N.4    Kuznetsov, B.B.5    Turova, T.P.6
  • 66
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • Spreitzer, R. J., and M. E. Salvucci. 2002. Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Annu. Rev. Plant Biol. 53:449-475.
    • (2002) Annu. Rev. Plant Biol , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 67
    • 0000947778 scopus 로고
    • 2 fixation in purple bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer ed, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 2 fixation in purple bacteria, p. 885-914. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic photosynthetic bacteria , pp. 885-914
    • Tabita, F.R.1
  • 68
    • 0032840522 scopus 로고    scopus 로고
    • Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
    • Tabita, F. R. 1999. Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: a different perspective. Photosynth. Res. 60:1-28.
    • (1999) Photosynth. Res , vol.60 , pp. 1-28
    • Tabita, F.R.1
  • 69
    • 0016137330 scopus 로고
    • D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. I. Levels, purification, and effects of metallic ions
    • Tabita, F. R., and B. A. McFadden. 1974. D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. I. Levels, purification, and effects of metallic ions. J. Biol. Chem. 249:3453-3458.
    • (1974) J. Biol. Chem , vol.249 , pp. 3453-3458
    • Tabita, F.R.1    McFadden, B.A.2
  • 70
    • 0016165638 scopus 로고    scopus 로고
    • Tabita, F. R., and B. A. McFadden. 1974. D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quaternary structure, composition, catalytic, and immunological properties. J. Biol. Chem. 249:3459-3464.
    • Tabita, F. R., and B. A. McFadden. 1974. D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quaternary structure, composition, catalytic, and immunological properties. J. Biol. Chem. 249:3459-3464.
  • 71
    • 37349063071 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 72
    • 0035930525 scopus 로고    scopus 로고
    • First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii
    • Taylor, T. C., A. Backlund, K. Bjorhall, R. J. Spreitzer, and I. Andersson. 2001. First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii. J. Biol. Chem. 276:48159-48164.
    • (2001) J. Biol. Chem , vol.276 , pp. 48159-48164
    • Taylor, T.C.1    Backlund, A.2    Bjorhall, K.3    Spreitzer, R.J.4    Andersson, I.5
  • 73
    • 0033027258 scopus 로고    scopus 로고
    • Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic archaea
    • Watson, G. M., J. P. Yu, and F. R. Tabita. 1999. Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic archaea. J. Bacteriol. 181:1569-1575.
    • (1999) J. Bacteriol , vol.181 , pp. 1569-1575
    • Watson, G.M.1    Yu, J.P.2    Tabita, F.R.3
  • 74
    • 0031024440 scopus 로고    scopus 로고
    • Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A molecule for phylogenetic and enzymological investigation
    • Watson, G. M. F., and F. R. Tabita. 1997. Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: a molecule for phylogenetic and enzymological investigation. FEMS Microbiol. Lett. 146:13-22.
    • (1997) FEMS Microbiol. Lett , vol.146 , pp. 13-22
    • Watson, G.M.F.1    Tabita, F.R.2
  • 75
    • 0036324122 scopus 로고    scopus 로고
    • Real-time PCR quantification of rbcL (ribulose-1,5-bisphosphate carboxylase/oxygenase) mRNA in diatoms and pelagophytes
    • Wawrik, B., J. H. Paul, and F. R. Tabita. 2002. Real-time PCR quantification of rbcL (ribulose-1,5-bisphosphate carboxylase/oxygenase) mRNA in diatoms and pelagophytes. Appl. Environ. Microbiol. 68:3771-3779.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 3771-3779
    • Wawrik, B.1    Paul, J.H.2    Tabita, F.R.3
  • 76
    • 0035896377 scopus 로고    scopus 로고
    • The TIM-barrel fold: A versatile framework for efficient enzymes
    • Wierenga, R. K. 2001. The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett. 492:193-198.
    • (2001) FEBS Lett , vol.492 , pp. 193-198
    • Wierenga, R.K.1
  • 77
    • 0037177237 scopus 로고    scopus 로고
    • Homologous (beta/alpha)-barrel enzymes that catalyze unrelated reactions: Orotidine 5′-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase
    • Wise, E., W. S. Yew, P. C. Babbitt, J. A. Gerlt, and I. Rayment. 2002. Homologous (beta/alpha)-barrel enzymes that catalyze unrelated reactions: orotidine 5′-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry 41:3861-3869.
    • (2002) Biochemistry , vol.41 , pp. 3861-3869
    • Wise, E.1    Yew, W.S.2    Babbitt, P.C.3    Gerlt, J.A.4    Rayment, I.5
  • 78
    • 0030008621 scopus 로고    scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase gene expression and diversity of Lake Erie planktonic microorganisms
    • Xu, H. H., and F. R. Tabita. 1996. Ribulose-1,5-bisphosphate carboxylase/oxygenase gene expression and diversity of Lake Erie planktonic microorganisms. Appl. Environ. Microbiol. 62:1913-1921.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 1913-1921
    • Xu, H.H.1    Tabita, F.R.2
  • 80
    • 33947235074 scopus 로고    scopus 로고
    • Yooseph, S., G. Sutton, D. B. Rusch, A. L. Halpern, S. J. Williamson, K. Remington, J. A. Eisen, K. B. Heidelberg, G. Manning, W. Li, L. Jaroszewski, P. Cieplak, C. S. Miller, H. Li, S. T. Mashiyama, M. P. Joachimiak, C. van Belle, J. M. Chandonia, D. A. Soergel, Y. Zhai, K. Natarajan, S. Lee, B. J. Raphael, V. Bafna, R. Friedman, S. E. Brenner, A. Godzik, D. Eisenberg, J. E. Dixon, S. S. Taylor, R. L. Strausberg, M. Frazier, and J. C. Venter. 2007. The Sorcerer II global ocean sampling expedition: expanding the universe of protein families. PLoS Biol. 5:e16.
    • Yooseph, S., G. Sutton, D. B. Rusch, A. L. Halpern, S. J. Williamson, K. Remington, J. A. Eisen, K. B. Heidelberg, G. Manning, W. Li, L. Jaroszewski, P. Cieplak, C. S. Miller, H. Li, S. T. Mashiyama, M. P. Joachimiak, C. van Belle, J. M. Chandonia, D. A. Soergel, Y. Zhai, K. Natarajan, S. Lee, B. J. Raphael, V. Bafna, R. Friedman, S. E. Brenner, A. Godzik, D. Eisenberg, J. E. Dixon, S. S. Taylor, R. L. Strausberg, M. Frazier, and J. C. Venter. 2007. The Sorcerer II global ocean sampling expedition: expanding the universe of protein families. PLoS Biol. 5:e16.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.