메뉴 건너뛰기




Volumn 130, Issue 3, 2007, Pages 440-453

Frankia alni proteome under nitrogen-fixing and nitrogen-replete conditions

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELLS; DETOXIFICATION; ELECTROPHORESIS; ENZYMES; MOLECULAR OXYGEN; PROTEINS;

EID: 34250166170     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2007.00859.x     Document Type: Conference Paper
Times cited : (41)

References (40)
  • 1
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts, and new words
    • Anderson NL, Anderson NG (1998) Proteome and proteomics: new technologies, new concepts, and new words. Electrophoresis 19 : 1853 1861
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 2
    • 0027191394 scopus 로고
    • Biology of Frankia strains, actinomycete symbionts of actinorhizal plants
    • Benson DR, Silvester WB (1993) Biology of Frankia strains, actinomycete symbionts of actinorhizal plants. Microbiol Rev 57 : 293 319
    • (1993) Microbiol Rev , vol.57 , pp. 293-319
    • Benson, D.R.1    Silvester, W.B.2
  • 3
    • 0034931519 scopus 로고    scopus 로고
    • Alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S (2001) alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40 : 1273 1287
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 4
    • 0027176916 scopus 로고
    • Hopanoid lipids compose the Frankia vesicle envelope, presumptive barrier of oxygen diffusion to nitrogenase
    • Berry A, Harriott O, Moreau R, Osman S, Benson D, Jones A (1993) Hopanoid lipids compose the Frankia vesicle envelope, presumptive barrier of oxygen diffusion to nitrogenase. Proc Nat Acad Sci USA 90 : 609 6094
    • (1993) Proc Nat Acad Sci USA , vol.90 , pp. 609-6094
    • Berry, A.1    Harriott, O.2    Moreau, R.3    Osman, S.4    Benson, D.5    Jones, A.6
  • 6
    • 12744281106 scopus 로고    scopus 로고
    • Proteomic approach: Identification of Medicago truncatula proteins induced in roots after infection with the pathogenic oomycete Aphanomyces euteiches
    • Colditz F, Nyamsuren O, Niehaus K, Eubel H, Braun HP, Krajinski F (2004) Proteomic approach: identification of Medicago truncatula proteins induced in roots after infection with the pathogenic oomycete Aphanomyces euteiches. Plant Mol Biol 55 : 109 120
    • (2004) Plant Mol Biol , vol.55 , pp. 109-120
    • Colditz, F.1    Nyamsuren, O.2    Niehaus, K.3    Eubel, H.4    Braun, H.P.5    Krajinski, F.6
  • 7
    • 3042772563 scopus 로고    scopus 로고
    • Sinorhizobium meliloti metabolism in the root nodule: A proteomic perspective
    • Djordjevic MA (2004) Sinorhizobium meliloti metabolism in the root nodule: a proteomic perspective. Proteomics 4 : 1859 1872
    • (2004) Proteomics , vol.4 , pp. 1859-1872
    • Djordjevic, M.A.1
  • 8
    • 0000299581 scopus 로고
    • The actinorhizal root-nodule symbiont Frankia sp. strain CpI1 has two glutamine synthetases
    • Edmands J, Noridge NA, Benson DR (1987) The actinorhizal root-nodule symbiont Frankia sp. strain CpI1 has two glutamine synthetases. Proc Natl Acad Sci USA 84 : 6126 6130
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6126-6130
    • Edmands, J.1    Noridge, N.A.2    Benson, D.R.3
  • 9
    • 27144538553 scopus 로고    scopus 로고
    • Ectopic expression of an FT homolog from citrus confers an early flowering phenotype on trifoliate orange (Poncirus trifoliata L. Raf
    • Endo T, Shimada T, Fujii H, Kobayashi Y, Araki T, Omura M (2005) Ectopic expression of an FT homolog from citrus confers an early flowering phenotype on trifoliate orange (Poncirus trifoliata L. Raf Transgenic Res 14 : 703 712
    • (2005) Transgenic Res , vol.14 , pp. 703-712
    • Endo, T.1    Shimada, T.2    Fujii, H.3    Kobayashi, Y.4    Araki, T.5    Omura, M.6
  • 10
    • 0023394497 scopus 로고
    • Requirement of succinate dehydrogenase activity for symbiotic bacteroid differentiation of Rhizobium meliloti in alfalfa nodules
    • Gardiol AE, Truchet GL, Dazzo FB (1987) Requirement of succinate dehydrogenase activity for symbiotic bacteroid differentiation of Rhizobium meliloti in alfalfa nodules. Appl Environ Microbiol 53 : 1947 1950
    • (1987) Appl Environ Microbiol , vol.53 , pp. 1947-1950
    • Gardiol, A.E.1    Truchet, G.L.2    Dazzo, F.B.3
  • 11
    • 0034857937 scopus 로고    scopus 로고
    • Modification of the protein expression pattern induced in the nitrogen-fixing actinomycete Frankia sp. strain ACN14a-tsr by root exudates of its symbiotic host Alnus glutinosa and cloning of the sodF gene
    • Hammad Y, Marechal J, Cournoyer B, Normand P, Domenach AM (2001) Modification of the protein expression pattern induced in the nitrogen-fixing actinomycete Frankia sp. strain ACN14a-tsr by root exudates of its symbiotic host Alnus glutinosa and cloning of the sodF gene. Can J Microbiol 47 : 541 547
    • (2001) Can J Microbiol , vol.47 , pp. 541-547
    • Hammad, Y.1    Marechal, J.2    Cournoyer, B.3    Normand, P.4    Domenach, A.M.5
  • 12
    • 24344476344 scopus 로고    scopus 로고
    • Genetic diversity of Frankia microsymbionts from the relict species Myrica faya (Ait.) and Myrica rivas-martinezii (S.) in Canary Islands and Hawaii
    • Huguet V, Land EO, Casanova JG, Zimpfer JF, Fernandez MP (2005) Genetic diversity of Frankia microsymbionts from the relict species Myrica faya (Ait.) and Myrica rivas-martinezii (S.) in Canary Islands and Hawaii. Microb Ecol 49 : 617 625
    • (2005) Microb Ecol , vol.49 , pp. 617-625
    • Huguet, V.1    Land, E.O.2    Casanova, J.G.3    Zimpfer, J.F.4    Fernandez, M.P.5
  • 13
    • 0033520985 scopus 로고    scopus 로고
    • A pair of related genes with antagonistic roles in mediating flowering signals
    • Kobayashi Y, Kaya H, Goto K, Iwabuchi M, Araki T (1999) A pair of related genes with antagonistic roles in mediating flowering signals. Science 286 : 1960 1962
    • (1999) Science , vol.286 , pp. 1960-1962
    • Kobayashi, Y.1    Kaya, H.2    Goto, K.3    Iwabuchi, M.4    Araki, T.5
  • 14
    • 0017709228 scopus 로고
    • Citric acid cycle enzymes and nitrogenase in nodules of Pisum sativum
    • Kurz WG, LaRue T (1977) Citric acid cycle enzymes and nitrogenase in nodules of Pisum sativum. Can J Microbiol 23 : 1197 1200
    • (1977) Can J Microbiol , vol.23 , pp. 1197-1200
    • Kurz, W.G.1    Larue, T.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laëmmli U (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
    • Laëmmli, U.1
  • 16
    • 0242416602 scopus 로고    scopus 로고
    • Identification of Streptomyces coelicolor proteins that are differentially expressed in the presence of plant material
    • Langlois P, Bourassa S, Poirier GG, Beaulieu C (2003) Identification of Streptomyces coelicolor proteins that are differentially expressed in the presence of plant material. Appl Environ Microbiol 69 : 1884 1889
    • (2003) Appl Environ Microbiol , vol.69 , pp. 1884-1889
    • Langlois, P.1    Bourassa, S.2    Poirier, G.G.3    Beaulieu, C.4
  • 17
    • 0030474295 scopus 로고    scopus 로고
    • Rubrerythrin from Clostridium perfringens: Cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function
    • Lehmann Y, Meile L, Teuber M (1996) Rubrerythrin from Clostridium perfringens: cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function. J Bacteriol 178 : 7152 7158
    • (1996) J Bacteriol , vol.178 , pp. 7152-7158
    • Lehmann, Y.1    Meile, L.2    Teuber, M.3
  • 18
    • 0035190269 scopus 로고    scopus 로고
    • Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: A novel oxidative stress protection system
    • Lumppio HL, Shenvi NV, Summers AO, Voordouw G, Kurtz DM Jr. (2001) Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system. J Bacteriol 183 : 101 108
    • (2001) J Bacteriol , vol.183 , pp. 101-108
    • Lumppio, H.L.1    Shenvi, N.V.2    Summers, A.O.3    Voordouw, G.4    Kurtz Jr., D.M.5
  • 20
    • 4444328040 scopus 로고    scopus 로고
    • A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21
    • May A, Hillmann F, Riebe O, Fischer RJ, Bahl H (2004) A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21. FEMS Microbiol Lett 238 : 249 254
    • (2004) FEMS Microbiol Lett , vol.238 , pp. 249-254
    • May, A.1    Hillmann, F.2    Riebe, O.3    Fischer, R.J.4    Bahl, H.5
  • 21
    • 0001273228 scopus 로고
    • Nitrogenase is restricted to the vesicles in Frankia strain EAN1pec
    • Meesters T, van Vliet M, Akkermans A (1987) Nitrogenase is restricted to the vesicles in Frankia strain EAN1pec. Physiol Plant 70 : 267 271
    • (1987) Physiol Plant , vol.70 , pp. 267-271
    • Meesters, T.1    Van Vliet, M.2    Akkermans, A.3
  • 23
    • 0002151087 scopus 로고
    • Growth kinetics and nitrogenase induction in Frankia sp. HFPArI3 grown in batch culture
    • Murry M, Fontaine M, Torrey J (1984) Growth kinetics and nitrogenase induction in Frankia sp. HFPArI3 grown in batch culture. Plant Soil 78 : 61 78
    • (1984) Plant Soil , vol.78 , pp. 61-78
    • Murry, M.1    Fontaine, M.2    Torrey, J.3
  • 24
    • 0033846005 scopus 로고    scopus 로고
    • Proteome analysis of differentially displayed proteins as a tool for the investigation of symbiosis
    • Natera SH, Guerreiro N, Djordjevic MA (2000) Proteome analysis of differentially displayed proteins as a tool for the investigation of symbiosis. Mol Plant Microbe Interact 13 : 995 1009
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 995-1009
    • Natera, S.H.1    Guerreiro, N.2    Djordjevic, M.A.3
  • 25
    • 0000614499 scopus 로고
    • Evaluation of Frankia strains isolated from provenances of two Alnus species
    • Normand P, Lalonde M (1982) Evaluation of Frankia strains isolated from provenances of two Alnus species. Can J Microbiol 28 : 1133 1142
    • (1982) Can J Microbiol , vol.28 , pp. 1133-1142
    • Normand, P.1    Lalonde, M.2
  • 28
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • Pancholi V, Chhatwal GS (2003) Housekeeping enzymes as virulence factors for pathogens. Int J Med Microbiol 293 : 391 401
    • (2003) Int J Med Microbiol , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 29
    • 2542574741 scopus 로고    scopus 로고
    • Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology
    • Schmidt F, Donahoe S, Hagens K, Mattow J, Schaible UE, Kaufmann SH, Aebersold R, Jungblut PR (2004) Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology. Mol Cell Proteomics 3 : 24 42
    • (2004) Mol Cell Proteomics , vol.3 , pp. 24-42
    • Schmidt, F.1    Donahoe, S.2    Hagens, K.3    Mattow, J.4    Schaible, U.E.5    Kaufmann, S.H.6    Aebersold, R.7    Jungblut, P.R.8
  • 31
    • 0025210160 scopus 로고
    • Enzymes of ammonia assimilation in hyphae and vesicles of Frankia sp. strain CpI1
    • Schultz NA, Benson DR (1990) Enzymes of ammonia assimilation in hyphae and vesicles of Frankia sp. strain CpI1. J Bacteriol 172 : 1380 1384
    • (1990) J Bacteriol , vol.172 , pp. 1380-1384
    • Schultz, N.A.1    Benson, D.R.2
  • 32
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein
    • Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H (2001) Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. J Mol Biol 310 : 617 634
    • (2001) J Mol Biol , vol.310 , pp. 617-634
    • Serre, L.1    Pereira De Jesus, K.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Benedetti, H.6
  • 34
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996b) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68 : 850 858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 36
    • 0033105190 scopus 로고    scopus 로고
    • Bacterial tellurite resistance
    • Taylor DE (1999) Bacterial tellurite resistance. Trends Microbiol 7 : 111 115
    • (1999) Trends Microbiol , vol.7 , pp. 111-115
    • Taylor, D.E.1
  • 37
    • 0019425229 scopus 로고
    • Factors affecting vesicle formation and acetylene reduction (nitrogenase activity) in Frankia sp. CpI1
    • Tjepkema J, Ormerod W, Torrey J (1981) Factors affecting vesicle formation and acetylene reduction (nitrogenase activity) in Frankia sp. CpI1. Can J Microbiol 27 : 815 823
    • (1981) Can J Microbiol , vol.27 , pp. 815-823
    • Tjepkema, J.1    Ormerod, W.2    Torrey, J.3
  • 39
    • 0028053680 scopus 로고
    • Expression and functional properties of fumarate reductase
    • Van Hellemond J, Tielens A (1994) Expression and functional properties of fumarate reductase. Biochem J 304 : 321 331
    • (1994) Biochem J , vol.304 , pp. 321-331
    • Van Hellemond, J.1    Tielens, A.2
  • 40
    • 9244263012 scopus 로고    scopus 로고
    • Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase
    • Weinberg MV, Jenney FE Jr., Cui X, Adams MW (2004) Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase. J Bacteriol 186 : 7888 7895
    • (2004) J Bacteriol , vol.186 , pp. 7888-7895
    • Weinberg, M.V.1    Jenney Jr., F.E.2    Cui, X.3    Adams, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.