메뉴 건너뛰기




Volumn 156, Issue 5-6, 2005, Pages 611-618

Was photosynthetic RuBisCO recruited by acquisitive evolution from RuBisCO-like proteins involved in sulfur metabolism?

Author keywords

Bacillus subtilis; Photosynthetic bacteria; RuBisCO; RuBisCO like protein

Indexed keywords

METHIONINE; PHOSPHATE; PROTEIN SUBUNIT; RIBULOSEBISPHOSPHATE CARBOXYLASE; SULFUR;

EID: 20444419762     PISSN: 09232508     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.resmic.2005.01.014     Document Type: Short Survey
Times cited : (83)

References (39)
  • 1
    • 0037561915 scopus 로고    scopus 로고
    • Structural framework for catalysis and regulation in ribulose-5- bisphosphate carboxylase/oxygenase
    • I. Andersson, and T.C. Taylor Structural framework for catalysis and regulation in ribulose- 1, 5 -bisphosphate carboxylase/oxygenase Arch. Biochem. Biophys. 414 2003 130 140
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 130-140
    • Andersson, I.1    Taylor, T.C.2
  • 3
    • 0141993683 scopus 로고    scopus 로고
    • A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO
    • H. Ashida, Y. Saito, C. Kojima, K. Kobayashi, N. Ogasawara, and A. Yokota A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO Science 302 2003 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
  • 4
    • 0027436432 scopus 로고
    • Appendix: Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca
    • R. Balakrishnan, M. Frohlich, P.T. Rahaim, K. Backman, and R.R. Yocum Appendix: Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca J. Biol. Chem. 268 1993 24792 24795
    • (1993) J. Biol. Chem. , vol.268 , pp. 24792-24795
    • Balakrishnan, R.1    Frohlich, M.2    Rahaim, P.T.3    Backman, K.4    Yocum, R.R.5
  • 5
    • 0037384217 scopus 로고    scopus 로고
    • Methionine regeneration and aminotransferase in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
    • B.J. Berger, S. English, G. Chan, and M.H. Knodel Methionine regeneration and aminotransferase in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis J. Bacteriol. 185 2003 2418 2431
    • (2003) J. Bacteriol. , vol.185 , pp. 2418-2431
    • Berger, B.J.1    English, S.2    Chan, G.3    Knodel, M.H.4
  • 6
    • 0037418252 scopus 로고    scopus 로고
    • Polyamines protect Escherichia coli cells from the toxic effect of oxygen
    • M.K. Chattopadhyay, C.W. Tabor, and H. Tabor Polyamines protect Escherichia coli cells from the toxic effect of oxygen Proc. Natl. Acad. Sci. USA 100 2003 2261 2265
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2261-2265
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 7
    • 49249144575 scopus 로고
    • The most abundant protein in the world
    • R.J. Ellis The most abundant protein in the world Trends Biochem. Sci. 4 1979 241 244
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 241-244
    • Ellis, R.J.1
  • 8
    • 0033582465 scopus 로고    scopus 로고
    • Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1
    • S. Ezaki, N. Maeda, T. Kishimoto, H. Atomi, and T. Imanaka Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1 J. Biol. Chem. 274 1999 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
  • 9
    • 0038643328 scopus 로고    scopus 로고
    • Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea
    • M.W. Finn, and F.R. Tabita Synthesis of catalytically active form III ribulose 1, 5 -bisphosphate carboxylase/oxygenase in archaea J. Bacteriol. 185 2003 3049 3059
    • (2003) J. Bacteriol. , vol.185 , pp. 3049-3059
    • Finn, M.W.1    Tabita, F.R.2
  • 10
    • 4544272017 scopus 로고    scopus 로고
    • Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea
    • M.W. Finn, and F.R. Tabita Modified pathway to synthesize ribulose 1, 5 -bisphosphate in methanogenic archaea J. Bacteriol. 186 2004 6360 6366
    • (2004) J. Bacteriol. , vol.186 , pp. 6360-6366
    • Finn, M.W.1    Tabita, F.R.2
  • 11
    • 0023718385 scopus 로고
    • Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae
    • E.S. Furfine, and R.H. Abeles Intermediates in the conversion of 5 ′ -S-methylthioadenosine to methionine in Klebsiella pneumoniae J. Biol. Chem. 263 1988 9598 9606
    • (1988) J. Biol. Chem. , vol.263 , pp. 9598-9606
    • Furfine, E.S.1    Abeles, R.H.2
  • 14
    • 0031794743 scopus 로고    scopus 로고
    • Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes
    • R.S. Gupta Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes Microbiol. Mol. Biol. Rev. 62 1998 1435 1491
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1435-1491
    • Gupta, R.S.1
  • 15
    • 0012999430 scopus 로고    scopus 로고
    • Phylogeny of bacteria: Are we now close to understanding it?
    • R.S. Gupta Phylogeny of bacteria: Are we now close to understanding it? ASM News 68 2002 284 291
    • (2002) ASM News , vol.68 , pp. 284-291
    • Gupta, R.S.1
  • 16
    • 0013356204 scopus 로고
    • Details of the reactions catalysed by mutant forms of RuBisCo
    • S. Gutteridge, J. Pierce, and G.H. Lorimer Details of the reactions catalysed by mutant forms of RuBisCo Plant Physiol. Biochem. 26 1989 675 682
    • (1989) Plant Physiol. Biochem. , vol.26 , pp. 675-682
    • Gutteridge, S.1    Pierce, J.2    Lorimer, G.H.3
  • 17
    • 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
    • T.E. Hanson, and F.R. Tabita 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 2001 4397 4402
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4397-4402
    • Hanson, T.E.1    Tabita, F.R.2
  • 18
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of d-ribulose-1,5- bisphosphate carboxylase/oxygenase
    • F.C. Hartman, and M.R. Harpel Structure, function, regulation, and assembly of d-ribulose- 1, 5 -bisphosphate carboxylase/oxygenase Annu. Rev. Biochem. 63 1994 197 234
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 20
    • 0000467650 scopus 로고
    • Reduction of ribulose-1,5-bisphosphate carboxylase/oxygenase content by antisense RNA reduces photosynthesis in transgenic tobacco plants
    • G.S. Hudson, J.R. Evans, S. von Caemmerer, Y.B.C. Arvidsson, and T.J. Andrews Reduction of ribulose- 1, 5 -bisphosphate carboxylase/oxygenase content by antisense RNA reduces photosynthesis in transgenic tobacco plants Plant Physiol. 98 1992 294 302
    • (1992) Plant Physiol. , vol.98 , pp. 294-302
    • Hudson, G.S.1    Evans, J.R.2    Von Caemmerer, S.3    Arvidsson, Y.B.C.4    Andrews, T.J.5
  • 21
    • 0034984584 scopus 로고    scopus 로고
    • Crystal structure of a novel-type archaeal RuBisCo with pentagonal symmetry
    • K. Kitano, N. Maeda, T. Fukui, H. Atomi, T. Imanaka, and K. Miki Crystal structure of a novel-type archaeal RuBisCo with pentagonal symmetry Structure 9 2001 473 481
    • (2001) Structure , vol.9 , pp. 473-481
    • Kitano, K.1    Maeda, N.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 22
    • 84989701101 scopus 로고
    • 5′-methylthioadenosine nucleosidase and 5-methylthioribose kinase activities in relation to stress-induced ethylene biosynthesis
    • M.M. Kushad, A. Orvos, and A.J. Ferro 5 ′ -methylthioadenosine nucleosidase and 5-methylthioribose kinase activities in relation to stress-induced ethylene biosynthesis Physiol. Plantarum 86 1992 532 538
    • (1992) Physiol. Plantarum , vol.86 , pp. 532-538
    • Kushad, M.M.1    Orvos, A.2    Ferro, A.J.3
  • 23
    • 0028933832 scopus 로고
    • Mechanistic insights provided by deletion of a flexible loop at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • E.M. Larson, F.W. Larimer, and F.C. Hartman Mechanistic insights provided by deletion of a flexible loop at the active site of ribulose- 1, 5 -bisphosphate carboxylase/oxygenase Biochemistry 34 1995 4531 4537
    • (1995) Biochemistry , vol.34 , pp. 4531-4537
    • Larson, E.M.1    Larimer, F.W.2    Hartman, F.C.3
  • 24
    • 0033555016 scopus 로고    scopus 로고
    • Genetic engineers aim to soup up crop photosynthesis
    • C.C. Mann Genetic engineers aim to soup up crop photosynthesis Science 283 1999 314 316
    • (1999) Science , vol.283 , pp. 314-316
    • Mann, C.C.1
  • 25
    • 0022412459 scopus 로고
    • The metabolism of 5′-methylthioadenosine and 5-methylthioribose-1- phosphate in Saccharomyces cerevisiae
    • K.S. Marchitto, and J.A. Ferro The metabolism of 5 ′ -methylthioadenosine and 5-methylthioribose-1-phosphate in Saccharomyces cerevisiae J. Gen. Microbiol. 131 1985 2153 2164
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2153-2164
    • Marchitto, K.S.1    Ferro, J.A.2
  • 26
    • 0032870941 scopus 로고    scopus 로고
    • Codon usage and lateral gene transfer in Bacillus subtilis
    • I. Moszer, E.P. Rocha, and A. Danchin Codon usage and lateral gene transfer in Bacillus subtilis Curr. Opin. Microbiol. 2 1999 524 528
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 524-528
    • Moszer, I.1    Rocha, E.P.2    Danchin, A.3
  • 27
    • 0037453069 scopus 로고    scopus 로고
    • Transcription termination control of the S box system: Direct measurement of s-adenosylmethionine by the leader RNA
    • B.A. Murphy MaDaniel, F.J. Grundy, I. Artsimovitch, and T.M. Henkin Transcription termination control of the S box system: Direct measurement of s-adenosylmethionine by the leader RNA Proc. Natl. Acad. Sci. USA 100 2003 3083 3088
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3083-3088
    • Murphy Madaniel, B.A.1    Grundy, F.J.2    Artsimovitch, I.3    Henkin, T.M.4
  • 28
    • 0036202171 scopus 로고    scopus 로고
    • Prediction of gene function in methylthioadenosine recycling from regulatory signals
    • B.A. Murphy, F.J. Grundy, and T.M. Henkin Prediction of gene function in methylthioadenosine recycling from regulatory signals J. Bacteriol. 184 2002 2314 2318
    • (2002) J. Bacteriol. , vol.184 , pp. 2314-2318
    • Murphy, B.A.1    Grundy, F.J.2    Henkin, T.M.3
  • 29
    • 0027367423 scopus 로고
    • Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
    • R.W. Myers, J.W. Wray, S. Fish, and R.H. Abeles Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae J. Biol. Chem. 268 1993 24785 24791
    • (1993) J. Biol. Chem. , vol.268 , pp. 24785-24791
    • Myers, R.W.1    Wray, J.W.2    Fish, S.3    Abeles, R.H.4
  • 30
    • 0033615370 scopus 로고    scopus 로고
    • Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis
    • A. Sekowska, and A. Danchin Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis DNA Res. 6 1999 255 264
    • (1999) DNA Res. , vol.6 , pp. 255-264
    • Sekowska, A.1    Danchin, A.2
  • 31
    • 19044362589 scopus 로고    scopus 로고
    • The methionine salvage pathway in Bacillus subtilis
    • A. Sekowska, and A. Danchin The methionine salvage pathway in Bacillus subtilis BMC Microbiol. 2 2002 8
    • (2002) BMC Microbiol. , vol.2 , pp. 8
    • Sekowska, A.1    Danchin, A.2
  • 33
    • 0033995794 scopus 로고    scopus 로고
    • Sulfur metabolism in Escherichia coli and related bacteria: Facts and fiction
    • A. Sekowska, H.F. Kung, and A. Danchin Sulfur metabolism in Escherichia coli and related bacteria: Facts and fiction J. Mol. Microbiol. Biotechnol. 2 2000 145 177
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 145-177
    • Sekowska, A.1    Kung, H.F.2    Danchin, A.3
  • 34
    • 19044394765 scopus 로고    scopus 로고
    • MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis
    • A. Sekowska, L. Mulard, S. Krogh, J.K. Tse, and A. Danchin MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis BMC Microbiol. 1 2001 15
    • (2001) BMC Microbiol. , vol.1 , pp. 15
    • Sekowska, A.1    Mulard, L.2    Krogh, S.3    Tse, J.K.4    Danchin, A.5
  • 35
    • 0032840522 scopus 로고    scopus 로고
    • Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
    • F.R. Tabita Microbial ribulose 1, 5 -bisphosphate carboxylase/oxygenase: A different perspective Photosynth. Res. 60 1999 1 28
    • (1999) Photosynth. Res. , vol.60 , pp. 1-28
    • Tabita, F.R.1
  • 36
    • 0030901120 scopus 로고    scopus 로고
    • 4 plant Flaveria bidentis leads to reduced assimilation rates and increased carbon isotope discrimination
    • 4 plant Flaveria bidentis leads to reduced assimilation rates and increased carbon isotope discrimination Plant Physiol. 113 1997 469 477
    • (1997) Plant Physiol. , vol.113 , pp. 469-477
    • Von Caemmerer, S.1    Millgate, A.2    Farquhar, G.D.3    Furbank, R.T.4
  • 37
    • 0033027258 scopus 로고    scopus 로고
    • Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic Archaea
    • G.M. Watson, and F.R. Tabita Unusual ribulose 1, 5 -bisphosphate carboxylase/oxygenase of anoxic Archaea J. Bacteriol. 181 1999 1569 1575
    • (1999) J. Bacteriol. , vol.181 , pp. 1569-1575
    • Watson, G.M.1    Tabita, F.R.2
  • 38
    • 0027378886 scopus 로고
    • A bacterial enzyme that catalyzes formation of carbon monoxide
    • J.W. Wray, and R.H. Abeles A bacterial enzyme that catalyzes formation of carbon monoxide J. Biol. Chem. 268 1993 21466 21469
    • (1993) J. Biol. Chem. , vol.268 , pp. 21466-21469
    • Wray, J.W.1    Abeles, R.H.2
  • 39
    • 0028850881 scopus 로고
    • The methionine salvage pathway in Klebsiella pneumoniae and rat liver: Identification and characterization of two novel dioxygenases
    • J.W. Wray, and R.H. Abeles The methionine salvage pathway in Klebsiella pneumoniae and rat liver: Identification and characterization of two novel dioxygenases J. Biol. Chem. 270 1995 3147 3153
    • (1995) J. Biol. Chem. , vol.270 , pp. 3147-3153
    • Wray, J.W.1    Abeles, R.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.