메뉴 건너뛰기




Volumn 67, Issue 3, 2006, Pages 424-436

Comparison of aerobic and photosynthetic Rhodobacter sphaeroides 2.4.1 proteomes

Author keywords

Comparative proteomics; Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS); Photosynthesis; Rhodobacter sphaeroides

Indexed keywords

BACTERIAL PROTEIN; GENE PRODUCT; PROTEOME; TRANSCRIPTOME;

EID: 33750970838     PISSN: 01677012     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mimet.2006.04.021     Document Type: Article
Times cited : (34)

References (48)
  • 1
    • 0032696682 scopus 로고    scopus 로고
    • Physical mapping and functional assignment of the geranylgeranyl-bacteriochlorophyll reductase gene, bchP, of Rhodobacter sphaeroides
    • Addlesee H.A., and Hunter C.N. Physical mapping and functional assignment of the geranylgeranyl-bacteriochlorophyll reductase gene, bchP, of Rhodobacter sphaeroides. J. Bacteriol. 181 (1999) 7248-7255
    • (1999) J. Bacteriol. , vol.181 , pp. 7248-7255
    • Addlesee, H.A.1    Hunter, C.N.2
  • 3
    • 11144335426 scopus 로고    scopus 로고
    • Estimating probabilities of peptide assignments to LC-FTICR-MS observations
    • Anderson K.K., Monroe M.E., and Daly D.S. Estimating probabilities of peptide assignments to LC-FTICR-MS observations. Proc of the Intern Conf METMBS (2004) 151-156
    • (2004) Proc of the Intern Conf METMBS , pp. 151-156
    • Anderson, K.K.1    Monroe, M.E.2    Daly, D.S.3
  • 4
    • 0031437603 scopus 로고    scopus 로고
    • Bacterial chemotaxis: Rhodobacter sphaeroides and Sinorhizobium meliloti - variations on a theme?
    • Armitage J.P., and Schmitt R. Bacterial chemotaxis: Rhodobacter sphaeroides and Sinorhizobium meliloti - variations on a theme?. Microbiology 143 (1997) 3671-3682
    • (1997) Microbiology , vol.143 , pp. 3671-3682
    • Armitage, J.P.1    Schmitt, R.2
  • 6
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
    • Bolstad B.M., Irizarry R.A., Astrand M., and Speed T.P. A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19 (2003) 185-193
    • (2003) Bioinformatics , vol.19 , pp. 185-193
    • Bolstad, B.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 7
    • 0027238058 scopus 로고
    • The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA, consists of 3 genes, bchX, bchy, and bchZ
    • Burke D.H., Alberti M., and Hearst J.E. The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA, consists of 3 genes, bchX, bchy, and bchZ. J. Bacteriol. 175 (1993) 2407-2413
    • (1993) J. Bacteriol. , vol.175 , pp. 2407-2413
    • Burke, D.H.1    Alberti, M.2    Hearst, J.E.3
  • 8
    • 0021212130 scopus 로고
    • Induction of the photosynthetic membranes of Rhodopseudomonas sphaeroides - biochemical and morphological studies
    • Chory J., Donohue T.J., Varga A.R., Staehelin L.A., and Kaplan S. Induction of the photosynthetic membranes of Rhodopseudomonas sphaeroides - biochemical and morphological studies. J. Bacteriol. 159 (1984) 540-554
    • (1984) J. Bacteriol. , vol.159 , pp. 540-554
    • Chory, J.1    Donohue, T.J.2    Varga, A.R.3    Staehelin, L.A.4    Kaplan, S.5
  • 9
    • 0034651621 scopus 로고    scopus 로고
    • DNA sequence analysis of the photosynthesis region of Rhodobacter sphaeroides 2.4.1
    • Choudhary M., and Kaplan S. DNA sequence analysis of the photosynthesis region of Rhodobacter sphaeroides 2.4.1. Nucleic Acids Res. 28 (2000) 862-867
    • (2000) Nucleic Acids Res. , vol.28 , pp. 862-867
    • Choudhary, M.1    Kaplan, S.2
  • 10
    • 70449138041 scopus 로고
    • Kinetic studies of pigment synthesis by non-sulfur purple bacteria
    • Cohen-Bazire G., Sistrom W.R., and Stanier R.Y. Kinetic studies of pigment synthesis by non-sulfur purple bacteria. J. Cell. Comp. Physiol. 49 (1957) 25-68
    • (1957) J. Cell. Comp. Physiol. , vol.49 , pp. 25-68
    • Cohen-Bazire, G.1    Sistrom, W.R.2    Stanier, R.Y.3
  • 12
    • 0029981912 scopus 로고    scopus 로고
    • The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition
    • Dmello R., Hill S., and Poole R.K. The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition. Microbiology-Uk 142 (1996) 755-763
    • (1996) Microbiology-Uk , vol.142 , pp. 755-763
    • Dmello, R.1    Hill, S.2    Poole, R.K.3
  • 14
    • 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 (2004) 353-376
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 353-376
    • Dubbs, J.M.1    Tabita, F.R.2
  • 15
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng J.K., Mccormack A.L., and Yates J.R. An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database. J. Am. Soc. Mass Spectrom. 5 (1994) 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    Mccormack, A.L.2    Yates, J.R.3
  • 16
    • 15944369336 scopus 로고    scopus 로고
    • Phototrophic hydrogen production from acetate and butyrate in wastewater
    • Fang H.H.P., Liu H., and Zhang T. Phototrophic hydrogen production from acetate and butyrate in wastewater. Int. J. Hydrogen Energy 30 (2005) 785-793
    • (2005) Int. J. Hydrogen Energy , vol.30 , pp. 785-793
    • Fang, H.H.P.1    Liu, H.2    Zhang, T.3
  • 17
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi S.P., Rochon Y., Franza B.R., and Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol. Cell. Biol. 19 (1999) 1720-1730
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 18
    • 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 Tabita F.R. A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 14515-14520
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14515-14520
    • Joshi, H.M.1    Tabita, F.R.2
  • 20
    • 0034940062 scopus 로고    scopus 로고
    • The roles of the multiple CheW and CheA homologues in chemotaxis and in chemoreceptor localization in Rhodobacter sphaeroides
    • Martin A.C., Wadhams G.H., and Armitage J.P. The roles of the multiple CheW and CheA homologues in chemotaxis and in chemoreceptor localization in Rhodobacter sphaeroides. Mol. Microbiol. 40 (2001) 1261-1272
    • (2001) Mol. Microbiol. , vol.40 , pp. 1261-1272
    • Martin, A.C.1    Wadhams, G.H.2    Armitage, J.P.3
  • 22
    • 0026008705 scopus 로고
    • Characterization of the assimilatory and dissimilatory nitrate-reducing systems in Rhodobacter - a comparative study
    • Martinezluque M., Dobao M.M., and Castillo F. Characterization of the assimilatory and dissimilatory nitrate-reducing systems in Rhodobacter - a comparative study. FEMS Microbiol. Lett. 83 (1991) 329-334
    • (1991) FEMS Microbiol. Lett. , vol.83 , pp. 329-334
    • Martinezluque, M.1    Dobao, M.M.2    Castillo, F.3
  • 23
    • 0027452672 scopus 로고
    • Genetic analysis of the bchC gene and bchA gene of Rhodobacter sphaeroides
    • Mcglynn P., and Hunter C.N. Genetic analysis of the bchC gene and bchA gene of Rhodobacter sphaeroides. Mol. Gen. Genet. 236 (1993) 227-234
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 227-234
    • Mcglynn, P.1    Hunter, C.N.2
  • 24
    • 0023162757 scopus 로고
    • Efficiency of light energy conversion to hydrogen by the photosynthetic bacterium Rhodobacter sphaeroides
    • Miyake J., and Kawamura S. Efficiency of light energy conversion to hydrogen by the photosynthetic bacterium Rhodobacter sphaeroides. Int. J. Hydrogen Energy 12 (1987) 147-149
    • (1987) Int. J. Hydrogen Energy , vol.12 , pp. 147-149
    • Miyake, J.1    Kawamura, S.2
  • 25
    • 0026506213 scopus 로고
    • Identification of intrinsic high-level resistance to rareearth-oxides and oxyanions in members of the class proteobacteria - characterization of tellurite, selenite, and rhodium sesquioxide reduction in Rhodobacter sphaeroides
    • Moore M.D., and Kaplan S. Identification of intrinsic high-level resistance to rareearth-oxides and oxyanions in members of the class proteobacteria - characterization of tellurite, selenite, and rhodium sesquioxide reduction in Rhodobacter sphaeroides. J.Bacteriol. 174 (1992) 1505-1514
    • (1992) J.Bacteriol. , vol.174 , pp. 1505-1514
    • Moore, M.D.1    Kaplan, S.2
  • 27
    • 28444475607 scopus 로고    scopus 로고
    • Correlation between mRNA and protein abundance in Desulfovibrio vulgaris: a multiple regression to identify sources of variations
    • Nie L., Wu G., and Zhang W.W. Correlation between mRNA and protein abundance in Desulfovibrio vulgaris: a multiple regression to identify sources of variations. Biochem. Biophys. Res. Commun. 339 (2006) 603-610
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 603-610
    • Nie, L.1    Wu, G.2    Zhang, W.W.3
  • 30
    • 0029670068 scopus 로고    scopus 로고
    • A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum
    • Preisig O., Zufferey R., Thonymeyer L., Appleby C.A., and Hennecke H. A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum. J. Bacteriol. 178 (1996) 1532-1538
    • (1996) J. Bacteriol. , vol.178 , pp. 1532-1538
    • Preisig, O.1    Zufferey, R.2    Thonymeyer, L.3    Appleby, C.A.4    Hennecke, H.5
  • 31
  • 32
    • 1542275267 scopus 로고    scopus 로고
    • Effects of oxygen and light intensity on transcriptome expression in Rhodobacter sphaeroides 2.4.1: redox active gene expression profile
    • Roh J.H., Smith W.E., and Kaplan S. Effects of oxygen and light intensity on transcriptome expression in Rhodobacter sphaeroides 2.4.1: redox active gene expression profile. J. Biol. Chem. 279 (2004) 9146-9155
    • (2004) J. Biol. Chem. , vol.279 , pp. 9146-9155
    • Roh, J.H.1    Smith, W.E.2    Kaplan, S.3
  • 33
    • 0032921284 scopus 로고    scopus 로고
    • Roles of chemosensory pathways in transient changes in swimming speed of Rhodobacter sphaeroides induced by changes in photosynthetic electron transport
    • Romagnoli S., and Armitage J.P. Roles of chemosensory pathways in transient changes in swimming speed of Rhodobacter sphaeroides induced by changes in photosynthetic electron transport. J. Bacteriol. 181 (1999) 34-39
    • (1999) J. Bacteriol. , vol.181 , pp. 34-39
    • Romagnoli, S.1    Armitage, J.P.2
  • 34
    • 0036786855 scopus 로고    scopus 로고
    • Tactic responses to oxygen in the phototrophic bacterium Rhodobacter sphaeroides WS8N
    • Romagnoli S., Packer H.L., and Armitage J.P. Tactic responses to oxygen in the phototrophic bacterium Rhodobacter sphaeroides WS8N. J. Bacteriol. 184 (2002) 5590-5598
    • (2002) J. Bacteriol. , vol.184 , pp. 5590-5598
    • Romagnoli, S.1    Packer, H.L.2    Armitage, J.P.3
  • 35
    • 0020077920 scopus 로고
    • Fermentation and anaerobic respiration by Rhodospirillum rubrum and Rhodopseudomonas capsulata
    • Schultz J.E., and Weaver P.F. Fermentation and anaerobic respiration by Rhodospirillum rubrum and Rhodopseudomonas capsulata. J. Bacteriol. 149 (1982) 181-190
    • (1982) J. Bacteriol. , vol.149 , pp. 181-190
    • Schultz, J.E.1    Weaver, P.F.2
  • 38
    • 0028909207 scopus 로고
    • Altered monovinyl and divinyl protochlorophyllide pools in bchJ mutants of Rhodobacter capsulatus
    • Suzuki J.Y., and Bauer C.E. Altered monovinyl and divinyl protochlorophyllide pools in bchJ mutants of Rhodobacter capsulatus. J. Biol. Chem. 270 (1995) 3732-3740
    • (1995) J. Biol. Chem. , vol.270 , pp. 3732-3740
    • Suzuki, J.Y.1    Bauer, C.E.2
  • 39
    • 0024026753 scopus 로고
    • Molecular and cellular regulation of autotrophic carbon dioxide fixation in microorganisms
    • Tabita F.R. Molecular and cellular regulation of autotrophic carbon dioxide fixation in microorganisms. Microbiol. Rev. 52 (1988) 155-189
    • (1988) Microbiol. Rev. , vol.52 , pp. 155-189
    • Tabita, F.R.1
  • 40
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov R.L., Koonin E.V., and Lipman D.J. A genomic perspective on protein families. Science 278 (1997) 631-637
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 41
    • 22544463928 scopus 로고    scopus 로고
    • Identification of genes required for recycling reducing power during photosynthetic growth
    • Tavano C.L., Podevels A.M., and Donohue T.J. Identification of genes required for recycling reducing power during photosynthetic growth. J. Bacteriol. 187 (2005) 5249-5258
    • (2005) J. Bacteriol. , vol.187 , pp. 5249-5258
    • Tavano, C.L.1    Podevels, A.M.2    Donohue, T.J.3
  • 42
    • 0027182943 scopus 로고
    • Synthesis and stability of reaction center polypeptides and implications for reaction center assembly in Rhodobacter sphaeroides
    • Varga A.R., and Kaplan S. Synthesis and stability of reaction center polypeptides and implications for reaction center assembly in Rhodobacter sphaeroides. J. Biol. Chem. 268 (1993) 19842-19850
    • (1993) J. Biol. Chem. , vol.268 , pp. 19842-19850
    • Varga, A.R.1    Kaplan, S.2
  • 43
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: bacterial chemotaxis
    • Wadhams G.H., and Armitage J.P. Making sense of it all: bacterial chemotaxis. Nat. Rev. 5 (2004) 1024-1037
    • (2004) Nat. Rev. , vol.5 , pp. 1024-1037
    • Wadhams, G.H.1    Armitage, J.P.2
  • 44
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese C.R. Bacterial evolution. Microbiol. Rev. 51 (1987) 221-271
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 46
    • 0017405949 scopus 로고
    • Growth of Rhodopseudomonas capsulata under anaerobic dark conditions with dimethyl-sulfoxide
    • Yen H.C., and Marrs B. Growth of Rhodopseudomonas capsulata under anaerobic dark conditions with dimethyl-sulfoxide. Arch. Biochem. Biophys. 181 (1977) 411-418
    • (1977) Arch. Biochem. Biophys. , vol.181 , pp. 411-418
    • Yen, H.C.1    Marrs, B.2
  • 48
    • 0021813055 scopus 로고
    • Effects of light, oxygen, and substrates on steady-state levels of mRNA coding for ribulose-1,5-bisphosphate carboxylase and light-harvesting and reaction center polypeptides in Rhodopseudomonas sphaeroides
    • Zhu Y.S., and Kaplan S. Effects of light, oxygen, and substrates on steady-state levels of mRNA coding for ribulose-1,5-bisphosphate carboxylase and light-harvesting and reaction center polypeptides in Rhodopseudomonas sphaeroides. J. Bacteriol. 162 (1985) 925-932
    • (1985) J. Bacteriol. , vol.162 , pp. 925-932
    • Zhu, Y.S.1    Kaplan, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.