메뉴 건너뛰기




Volumn 181, Issue 13, 1999, Pages 3935-3941

The 'green' form I ribulose 1,5-bisphosphate carboxylase/oxygenase from the nonsulfur purple bacterium Rhodobacter capsulatus

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DIOXIDE; RIBULOSEBISPHOSPHATE CARBOXYLASE; SULFUR;

EID: 0033016520     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.13.3935-3941.1999     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0021886337 scopus 로고
    • Catalytic properties of a hybrid between cyanobacterial large subunits and higher plant small subunits of ribulose bisphosphate carboxylase-oxygenase
    • Andrews, T. J., and G. H. Lorimer. 1985. Catalytic properties of a hybrid between cyanobacterial large subunits and higher plant small subunits of ribulose bisphosphate carboxylase-oxygenase. J. Biol. Chem. 260:4632-4636.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4632-4636
    • Andrews, T.J.1    Lorimer, G.H.2
  • 2
    • 0021507252 scopus 로고
    • Catalytically active hybrids formed in vitro between large and small subunits of different procaryotic ribulose bisphosphate carboxylases
    • Andrews, T. J., D. M. Greenwood, and D. Yellowlees. 1984. Catalytically active hybrids formed in vitro between large and small subunits of different procaryotic ribulose bisphosphate carboxylases. Arch. Biochem. Biophys. 234:313-317.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 313-317
    • Andrews, T.J.1    Greenwood, D.M.2    Yellowlees, D.3
  • 3
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A., S.-A. Raillard, E. Bermudez, and W. P. C. Stemmer. 1998. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391:288-291.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.-A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 4
    • 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
  • 5
    • 0025362836 scopus 로고
    • Residues in three conserved regions of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase are required for quarternary structure
    • Fitchen, J. H., S. Knight, I. Andersson, C.-I. Branden, and L. McIntosh. 1990. Residues in three conserved regions of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase are required for quarternary structure. Proc. Natl. Acad. Sci. USA 87:5768-5772.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5768-5772
    • Fitchen, J.H.1    Knight, S.2    Andersson, I.3    Branden, C.-I.4    McIntosh, L.5
  • 6
    • 0013659185 scopus 로고
    • 2 fixation genes
    • R. E. Blankenship, M. T. Badigan, and C. E. Bauer (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 2 fixation genes, p. 1107-1124. In R. E. Blankenship, M. T. Badigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1107-1124
    • Gibson, J.L.1
  • 7
    • 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
  • 8
    • 0017761052 scopus 로고
    • Isolation and preliminary characterization of two forms of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas capsulata
    • Gibson, J. L., and F. R. Tabita. 1977. Isolation and preliminary characterization of two forms of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas capsulata. J. Bacteriol. 132:818-823.
    • (1977) J. Bacteriol. , vol.132 , pp. 818-823
    • Gibson, J.L.1    Tabita, F.R.2
  • 9
    • 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. 43:197-234.
    • (1994) Annu. Rev. Biochem. , vol.43 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 10
    • 0031577711 scopus 로고    scopus 로고
    • The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas Hydrogenothermophila affect the conformational states and activity of RubisCO
    • Hayashi, N. R., H. Arai, T. Kodama, and Y. Igarashi. 1997. The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas Hydrogenothermophila affect the conformational states and activity of RubisCO. Biochem. Biophys. Res. Commun. 241:565-569.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 565-569
    • Hayashi, N.R.1    Arai, H.2    Kodama, T.3    Igarashi, Y.4
  • 11
    • 0030033929 scopus 로고    scopus 로고
    • Deduced amino acid sequence, functional expression, and unique enzymatic properties of the form I and form II ribulose bisphosphate carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus denitrificans
    • Hernandez, J. M., S. H. Baker, S. C. Lorbach, J. M. Shively, and F. R. Tabita. 1996. Deduced amino acid sequence, functional expression, and unique enzymatic properties of the form I and form II ribulose bisphosphate carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus denitrificans. J. Bacteriol. 178:347-356.
    • (1996) J. Bacteriol. , vol.178 , pp. 347-356
    • Hernandez, J.M.1    Baker, S.H.2    Lorbach, S.C.3    Shively, J.M.4    Tabita, F.R.5
  • 12
    • 0345259911 scopus 로고    scopus 로고
    • Ph.D. dissertation. The Ohio State University, Columbus, Ohio
    • Horken, K. M. 1998. Ph.D. dissertation. The Ohio State University, Columbus, Ohio.
    • (1998)
    • Horken, K.M.1
  • 13
    • 0012148036 scopus 로고    scopus 로고
    • Genes related to carbon dioxide fixation in Hydrogenovibrio marinus and Pseudomonas hydrogenothermophila
    • M. E. Lidstrom and F. R. Tabita (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 1 compounds. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) 1 Compounds , pp. 88-93
    • Igarashi, Y.1    Kodama, T.2
  • 14
    • 0022435201 scopus 로고
    • Heterologous hybridization of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) restores the enzyme activities
    • Incharoensakdi, A., T. Takabe, and T. Akazawa. 1985. Heterologous hybridization of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) restores the enzyme activities. Biochem. Biophys. Res. Commun. 126:698-704.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 698-704
    • Incharoensakdi, A.1    Takabe, T.2    Akazawa, T.3
  • 15
    • 0000240773 scopus 로고
    • A sensitive assay procedure for simultaneous determination of ribulose-1,5-bisphosphate carboxylase and oxygenase activities
    • Jordan, D. B., and W. L. Ogren. 1981. A sensitive assay procedure for simultaneous determination of ribulose-1,5-bisphosphate carboxylase and oxygenase activities. Plant Physiol. 67:237-245.
    • (1981) Plant Physiol. , vol.67 , pp. 237-245
    • Jordan, D.B.1    Ogren, W.L.2
  • 16
    • 0029855868 scopus 로고    scopus 로고
    • A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation
    • Joshi, H. M., and F. R. Tabita. 1996. A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation. Proc. Natl. Acad. Sci. USA 93:14515-14520.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14515-14520
    • Joshi, H.M.1    Tabita, F.R.2
  • 17
    • 0000550176 scopus 로고
    • Physiological and molecular aspects of the inorganic carbon-concentrating mechanism in cyanobacteria
    • Kaplan, A., R. Schwarz, J. Lieman-Hurwitz, and L. Reinhold. 1991. Physiological and molecular aspects of the inorganic carbon-concentrating mechanism in cyanobacteria. Plant Physiol. 97:851-855.
    • (1991) Plant Physiol. , vol.97 , pp. 851-855
    • Kaplan, A.1    Schwarz, R.2    Lieman-Hurwitz, J.3    Reinhold, L.4
  • 18
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution
    • Knight, S., I. Andersson, and C.-I. Branden. 1990. Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution. 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
  • 19
    • 0025720491 scopus 로고
    • Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans
    • Kusano, T., T. Takeshima, C. Inoue, and K. Sugawara. 1991. Evidence for two sets of structural genes coding for ribulose bisphosphate carboxylase in Thiobacillus ferrooxidans. J. Bacteriol. 173:7313-7323.
    • (1991) J. Bacteriol. , vol.173 , pp. 7313-7323
    • Kusano, T.1    Takeshima, T.2    Inoue, C.3    Sugawara, K.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0142101295 scopus 로고
    • Sequence and expression of the form II ribulose bisphosphate carboxylase/oxygenase (RUBISCO) gene from Rhodobacter capsulatus
    • Larimer, F. W., T.-Y. Lu, and D. M. Bailey. 1995. Sequence and expression of the form II ribulose bisphosphate carboxylase/oxygenase (RUBISCO) gene from Rhodobacter capsulatus. FASEB J. 9:A1275.
    • (1995) FASEB J. , vol.9
    • Larimer, F.W.1    Lu, T.-Y.2    Bailey, D.M.3
  • 22
    • 0026316524 scopus 로고
    • Catalytic properties of recombinant octameric, hexadecameric, and heterologous cyanobacterial/bacterial ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Lee, B., B. A. Read, and F. R. Tabita. 1991. Catalytic properties of recombinant octameric, hexadecameric, and heterologous cyanobacterial/bacterial ribulose-1,5-bisphosphate carboxylase/oxygenase. Arch. Biochem. Biophys. 291:263-269.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 263-269
    • Lee, B.1    Read, B.A.2    Tabita, F.R.3
  • 23
    • 0030970919 scopus 로고    scopus 로고
    • Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene
    • Li, L.-A., and F. R. Tabita. 1997. Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene. J. Bacteriol. 179:3793-3796.
    • (1997) J. Bacteriol. , vol.179 , pp. 3793-3796
    • Li, L.-A.1    Tabita, F.R.2
  • 24
    • 0017253134 scopus 로고
    • The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
    • Lorimer, G. H., M. R. Badger, and T. J. Andrews. 1976. The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. Biochemistry 15:529-536.
    • (1976) Biochemistry , vol.15 , pp. 529-536
    • Lorimer, G.H.1    Badger, M.R.2    Andrews, T.J.3
  • 25
    • 50549188450 scopus 로고
    • Light dependent utilization of organic compounds and photoproduction of molecular hydrogen by photosynthetic bacteria; relationships with nitrogen metabolism
    • Ormerod, J. G., K. D. Omerod, and H. Gest. 1961. Light dependent utilization of organic compounds and photoproduction of molecular hydrogen by photosynthetic bacteria; relationships with nitrogen metabolism. Arch. Biochem. Biophys. 94:449-463.
    • (1961) Arch. Biochem. Biophys. , vol.94 , pp. 449-463
    • Ormerod, J.G.1    Omerod, K.D.2    Gest, H.3
  • 26
    • 0344828667 scopus 로고    scopus 로고
    • Personal communication
    • Paoli, G. Personal communication.
    • Paoli, G.1
  • 27
    • 0029614795 scopus 로고
    • Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus
    • Paoli, G. C., N. S. Morgan, F. R. Tabita, and J. M. Shively. 1995. Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus. Arch. Microbiol. 164:396-405.
    • (1995) Arch. Microbiol. , vol.164 , pp. 396-405
    • Paoli, G.C.1    Morgan, N.S.2    Tabita, F.R.3    Shively, J.M.4
  • 28
    • 0031962934 scopus 로고    scopus 로고
    • Rhodobacter capsulatus genes encoding form I ribulose-1,5-bisphosphate carboxylase/oxygenase (cbbLS) and neighboring genes were acquired by a horizontal gene transfer
    • Paoli, G. C., F. Soyer, J. Shively, and F. R. Tabita. 1998. Rhodobacter capsulatus genes encoding form I ribulose-1,5-bisphosphate carboxylase/oxygenase (cbbLS) and neighboring genes were acquired by a horizontal gene transfer. Microbiology 144:219-227.
    • (1998) Microbiology , vol.144 , pp. 219-227
    • Paoli, G.C.1    Soyer, F.2    Shively, J.3    Tabita, F.R.4
  • 29
    • 0031876149 scopus 로고    scopus 로고
    • Physiological control and regulation of the Rhodobacter capsulatus cbb operons
    • Paoli, G. C., P. Vichivanives, and F. R. Tabita. 1998. Physiological control and regulation of the Rhodobacter capsulatus cbb operons. J. Bacteriol. 180:4258-4269.
    • (1998) J. Bacteriol. , vol.180 , pp. 4258-4269
    • Paoli, G.C.1    Vichivanives, P.2    Tabita, F.R.3
  • 30
    • 0000384908 scopus 로고
    • Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity
    • Portis, A. R., Jr. 1992. Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity. Annu. Rev. Plant Physiol. 43:415-437.
    • (1992) Annu. Rev. Plant Physiol. , vol.43 , pp. 415-437
    • Portis A.R., Jr.1
  • 31
    • 0023629563 scopus 로고
    • New and versatile cloning vectors with kanamycin-resistance marker
    • Pridemore, R. D. 1987. New and versatile cloning vectors with kanamycin-resistance marker. Gene 56:309-312.
    • (1987) Gene , vol.56 , pp. 309-312
    • Pridemore, R.D.1
  • 32
    • 0030046502 scopus 로고    scopus 로고
    • 2 fixation in Rhodobacter sphaeroides
    • 2 fixation in Rhodobacter sphaeroides. J. Bacteriol. 178:12-18.
    • (1996) J. Bacteriol. , vol.178 , pp. 12-18
    • Qian, Y.1    Tabita, F.R.2
  • 33
    • 0026643280 scopus 로고
    • A hybrid ribulosebisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor
    • Read, B. A., and F. R. Tabita. 1992. A hybrid ribulosebisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor. Biochemistry 31:5553-5560.
    • (1992) Biochemistry , vol.31 , pp. 5553-5560
    • Read, B.A.1    Tabita, F.R.2
  • 34
    • 0021185932 scopus 로고
    • Derepression of the synthesis of the intermediate and large forms of ribulose-1,5-bisphosphate carboxylase/oxygenase in Rhodopseudomonas capsulata
    • Shively, J. M., E. Davidson, and B. L. Marrs. 1984. Derepression of the synthesis of the intermediate and large forms of ribulose-1,5-bisphosphate carboxylase/oxygenase in Rhodopseudomonas capsulata. Arch. Microbiol. 138:233-236.
    • (1984) Arch. Microbiol. , vol.138 , pp. 233-236
    • Shively, J.M.1    Davidson, E.2    Marrs, B.L.3
  • 35
    • 0023002584 scopus 로고
    • Molecular evolution of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO)
    • Shively, J. M., W. Devon, L. Stratford, L. Porter, L. Medlin, and S. E. Stevens, Jr. 1986. Molecular evolution of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). FEMS Microbiol. Lett. 37: 251-257.
    • (1986) FEMS Microbiol. Lett. , vol.37 , pp. 251-257
    • Shively, J.M.1    Devon, W.2    Stratford, L.3    Porter, L.4    Medlin, L.5    Stevens S.E., Jr.6
  • 36
    • 0025822722 scopus 로고
    • Purification and characterization of large and small subunits of ribulose 1,5-bisphosphate carboxylase expressed separately in Escherichia coli
    • Smrcka, A. V., R. T. Ramage, H. J. Bohnert, and R. G. Jensen. 1991. Purification and characterization of large and small subunits of ribulose 1,5-bisphosphate carboxylase expressed separately in Escherichia coli. Arch. Biochem. Biophys. 286:6-13.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 6-13
    • Smrcka, A.V.1    Ramage, R.T.2    Bohnert, H.J.3    Jensen, R.G.4
  • 37
    • 0000947778 scopus 로고
    • 2 fixation in purple bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer, 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, Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 885-914
    • Tabita, F.R.1
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 39
    • 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 Lett. 146:13-22.
    • (1997) FEMS Lett. , vol.146 , pp. 13-22
    • Watson, G.M.F.1    Tabita, F.R.2
  • 40
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 41
    • 0028834124 scopus 로고
    • Genes encoding RubisCO in Pseudomonas hydrogenothermophila are followed by a novel cbbQ gene simitar to nirQ of the denitrification gene cluster from Pseudomonas species
    • Yokoyama, K., N. Hayashi, H. Arai, S. Chung, Y. Igarashi, and T. Kodama. 1995. Genes encoding RubisCO in Pseudomonas hydrogenothermophila are followed by a novel cbbQ gene simitar to nirQ of the denitrification gene cluster from Pseudomonas species. Gene 153:75-79.
    • (1995) Gene , vol.153 , pp. 75-79
    • Yokoyama, K.1    Hayashi, N.2    Arai, H.3    Chung, S.4    Igarashi, Y.5    Kodama, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.