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Volumn 273, Issue 3, 2005, Pages 225-239

DNA microarray analysis of Methanosarcina mazei Gö1 reveals adaptation to different methanogenic substrates

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETYL COENZYME A SYNTHETASE; CARBON; CARBON MONOXIDE DEHYDROGENASE; CARBONATE DEHYDRATASE; DNA; FERREDOXIN; FLAVOPROTEIN; METHANOL;

EID: 20044381310     PISSN: 16174615     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00438-005-1126-9     Document Type: Article
Times cited : (68)

References (66)
  • 1
    • 0026317878 scopus 로고
    • Resolution of component proteins in an enzyme complex from Methanosarcina thermophila catalyzing the synthesis or cleavage of acetyl-CoA
    • Abbanat DR, Ferry JG (1991) Resolution of component proteins in an enzyme complex from Methanosarcina thermophila catalyzing the synthesis or cleavage of acetyl-CoA. Proc Natl Acad Sci USA 88:3272-3276
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3272-3276
    • Abbanat, D.R.1    Ferry, J.G.2
  • 2
    • 0024297194 scopus 로고
    • Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila: Evidence for regulation of synthesis
    • Aceti DJ, Ferry JG (1988) Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila: evidence for regulation of synthesis. J Biol Chem 263:15444-15448
    • (1988) J Biol Chem , vol.263 , pp. 15444-15448
    • Aceti, D.J.1    Ferry, J.G.2
  • 3
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR (1997) A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143:3633-3647
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 4
    • 0037351028 scopus 로고    scopus 로고
    • Characterization, localization and functional analysis of Gpr1p, a protein affecting sensitivity to acetic acid in the yeast Yarrowia lipolytica
    • Augstein A, Barth K, Gentsch M, Kohlwein SD, Barth G (2003) Characterization, localization and functional analysis of Gpr1p, a protein affecting sensitivity to acetic acid in the yeast Yarrowia lipolytica. Microbiology 149:589-600
    • (2003) Microbiology , vol.149 , pp. 589-600
    • Augstein, A.1    Barth, K.2    Gentsch, M.3    Kohlwein, S.D.4    Barth, G.5
  • 5
    • 0034674063 scopus 로고    scopus 로고
    • 2 dehydrogenase from Methanosarcina mazei Gö1 is a redox-driven proton pump closely related to NADH dehydrogenases
    • 2 dehydrogenase from Methanosarcina mazei Gö1 is a redox-driven proton pump closely related to NADH dehydrogenases. J Biol Chem 275:17968-17973
    • (2000) J Biol Chem , vol.275 , pp. 17968-17973
    • Bäumer, S.1    Ide, T.2    Jacobi, C.3    Johann, A.4    Gottschalk, G.5    Deppenmeier, U.6
  • 6
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm R, Sauter M, Böck A (1990) Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol Microbiol 4:231-243
    • (1990) Mol Microbiol , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 10
    • 0026094290 scopus 로고
    • Nucleotide sequence and genetic analysis of a 131-kilobase-pair Pseudomonas denitrificans DNA fragment containing five cob genes and identification of structural genes encoding Cob(I)alamin adenosyl-transferase, cobyric acid synthase, and bifunctional cobinamide kinase-cobinamide phosphate guanylyltransferase
    • Crouzet J, Levy-Schil S, Cameron B, Cauchois L, Rigault S, Rouyez MC, Blanche F, Debussche L, Thibaut D (1991) Nucleotide sequence and genetic analysis of a 131-kilobase-pair Pseudomonas denitrificans DNA fragment containing five cob genes and identification of structural genes encoding Cob(I)alamin adenosyl-transferase, cobyric acid synthase, and bifunctional cobinamide kinase-cobinamide phosphate guanylyltransferase. J Bacteriol 173:6074-6087
    • (1991) J Bacteriol , vol.173 , pp. 6074-6087
    • Crouzet, J.1    Levy-Schil, S.2    Cameron, B.3    Cauchois, L.4    Rigault, S.5    Rouyez, M.C.6    Blanche, F.7    Debussche, L.8    Thibaut, D.9
  • 11
    • 0026539866 scopus 로고
    • Assay, purification and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans
    • Debussche L, Couder M, Thibaut D, Cameron B, Crouzet J, Blanche F (1992) Assay, purification and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans. J Bacteriol 174:7445-7451
    • (1992) J Bacteriol , vol.174 , pp. 7445-7451
    • Debussche, L.1    Couder, M.2    Thibaut, D.3    Cameron, B.4    Crouzet, J.5    Blanche, F.6
  • 12
    • 0039864615 scopus 로고    scopus 로고
    • Ruminants and environment: Methanogenesis
    • Demeyer D, Fievez V (2000) Ruminants and environment: methanogenesis. Ann Zootechnie 49:95-112
    • (2000) Ann Zootechnie , vol.49 , pp. 95-112
    • Demeyer, D.1    Fievez, V.2
  • 13
    • 0036357283 scopus 로고    scopus 로고
    • The unique biochemistry of methanogenesis
    • Deppenmeier U (2002a) The unique biochemistry of methanogenesis. Prog Nucleic Acids Res 71:223-283
    • (2002) Prog Nucleic Acids Res , vol.71 , pp. 223-283
    • Deppenmeier, U.1
  • 14
    • 0036709867 scopus 로고    scopus 로고
    • Redox-driven proton translocation in methanogenic Archaea
    • Deppenmeier U (2002b) Redox-driven proton translocation in methanogenic Archaea. Cell Mol Life Sci 59:1-21
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1-21
    • Deppenmeier, U.1
  • 16
    • 0037167474 scopus 로고    scopus 로고
    • Genomic and proteomic analyses reveal multiple homologs of genes encoding enzymes of the methanol:coenzyme M methyltransferase system that are differentially expressed in methanol- and acetate-grown Methanosarcina thermophila
    • Ding YH, Zhang SP, Tomb JF, Ferry JG (2002) Genomic and proteomic analyses reveal multiple homologs of genes encoding enzymes of the methanol:coenzyme M methyltransferase system that are differentially expressed in methanol- and acetate-grown Methanosarcina thermophila. FEMS Microbiol Lett 215:127-132
    • (2002) FEMS Microbiol Lett , vol.215 , pp. 127-132
    • Ding, Y.H.1    Zhang, S.P.2    Tomb, J.F.3    Ferry, J.G.4
  • 17
    • 0030012715 scopus 로고    scopus 로고
    • Carbon monoxide dehydrogenase from Methanosarcina frisia Gö1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters
    • Eggen RIL, VanKranenburg R, Vriesema AJM, Geerling ACM, Verhagen MFJM, Hagen WR, de Vos WM (1996) Carbon monoxide dehydrogenase from Methanosarcina frisia Gö1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters. J Biol Chem 271:14256-14263
    • (1996) J Biol Chem , vol.271 , pp. 14256-14263
    • Eggen, R.I.L.1    VanKranenburg, R.2    Vriesema, A.J.M.3    Geerling, A.C.M.4    Verhagen, M.F.J.M.5    Hagen, W.R.6    De Vos, W.M.7
  • 18
    • 0030838597 scopus 로고    scopus 로고
    • Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila
    • Ferry RG (1997) Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila. Biofactors 6:25-35
    • (1997) Biofactors , vol.6 , pp. 25-35
    • Ferry, R.G.1
  • 19
    • 0033005876 scopus 로고    scopus 로고
    • Enzymology of one-carbon metabolism in methanogenic pathways
    • Ferry RG (1999) Enzymology of one-carbon metabolism in methanogenic pathways. FEMS Microbiol Rev 23:13-38
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 13-38
    • Ferry, R.G.1
  • 20
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
    • Fox JD, Kerby RL, Roberts GP, Ludden PW (1996) Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J Bacteriol 178:1515-1521
    • (1996) J Bacteriol , vol.178 , pp. 1515-1521
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 21
    • 0036225678 scopus 로고    scopus 로고
    • The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity
    • Galagan JE, Nusbaum C, Roy A, Endrizzi MG, Macdonald P, FitzHugh WS et al (2002) The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity. Genome Res 12:532-542
    • (2002) Genome Res , vol.12 , pp. 532-542
    • Galagan, J.E.1    Nusbaum, C.2    Roy, A.3    Endrizzi, M.G.4    Macdonald, P.5    FitzHugh, W.S.6
  • 22
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin MY, Nikolskaya AN, Koonin EV (2001) Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol Lett 203:11-21
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 23
    • 0037727718 scopus 로고    scopus 로고
    • Acetate C-C bond formation and decomposition in the anaerobic world: The structure of a central enzyme and its key active-site metal cluster
    • Grahame DA (2003) Acetate C-C bond formation and decomposition in the anaerobic world: the structure of a central enzyme and its key active-site metal cluster. Trends Biochem Sci 28:221-224
    • (2003) Trends Biochem Sci , vol.28 , pp. 221-224
    • Grahame, D.A.1
  • 26
    • 0345194051 scopus 로고
    • Utilization of trimethylamine and other N-methyl compounds for growth and methane formation by Methanosarcina barkeri
    • Hippe H, Caspari D, Fiebig K, Gottschalk G (1979) Utilization of trimethylamine and other N-methyl compounds for growth and methane formation by Methanosarcina barkeri. Proc Natl Acad Sci USA 76:494-498
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 494-498
    • Hippe, H.1    Caspari, D.2    Fiebig, K.3    Gottschalk, G.4
  • 27
    • 0345359589 scopus 로고    scopus 로고
    • Development of a Corynebacterium glutamicum DNA microarray and validation by genome-wide expression profiling during growth with propionate as carbon source
    • Hüser AT, Becker A, Brune I, Dondrup M, Kalinowski J, Plassmeier J, Pühler A, Wiegräbe I, Tauch A (2003) Development of a Corynebacterium glutamicum DNA microarray and validation by genome-wide expression profiling during growth with propionate as carbon source. J Biotechnol 106:269-286
    • (2003) J Biotechnol , vol.106 , pp. 269-286
    • Hüser, A.T.1    Becker, A.2    Brune, I.3    Dondrup, M.4    Kalinowski, J.5    Plassmeier, J.6    Pühler, A.7    Wiegräbe, I.8    Tauch, A.9
  • 28
    • 0032586857 scopus 로고    scopus 로고
    • 2:heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: Identification of two proton-translocating segments
    • 2:heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: identification of two proton-translocating segments. J Bacteriol 181:4076-4080
    • (1999) J Bacteriol , vol.181 , pp. 4076-4080
    • Ide, T.1    Bäumer, S.2    Deppenmeier, U.3
  • 29
    • 0025213114 scopus 로고
    • Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila
    • Jablonski PE, Dimarco AA, Bobik TA, Cabell MC, Ferry JG (1990) Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila. J Bacteriol 172:1271-1275
    • (1990) J Bacteriol , vol.172 , pp. 1271-1275
    • Jablonski, P.E.1    Dimarco, A.A.2    Bobik, T.A.3    Cabell, M.C.4    Ferry, J.G.5
  • 30
    • 0001780722 scopus 로고
    • Conversion of methanol and methylamines to methane and carbon dioxide
    • Ferry JG (ed) Chapman and Hall, New York
    • Keltjens JT, Vogels GD (1993) Conversion of methanol and methylamines to methane and carbon dioxide. In: Ferry JG (ed) Methanogenesis: ecology, physiology, biochemistry and genetics. Chapman and Hall, New York, pp 253-303
    • (1993) Methanogenesis: Ecology, Physiology, Biochemistry and Genetics , pp. 253-303
    • Keltjens, J.T.1    Vogels, G.D.2
  • 31
    • 0037883611 scopus 로고    scopus 로고
    • Global expression profiling and physiological characterization of Corynebacterium glutamicum grown in the presence of L-valine
    • Lange C, Rittmann D, Wendisch VF, Bott M, Sahm H (2003) Global expression profiling and physiological characterization of Corynebacterium glutamicum grown in the presence of L-valine. Appl Environ Microbiol 69:2521-2532
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2521-2532
    • Lange, C.1    Rittmann, D.2    Wendisch, V.F.3    Bott, M.4    Sahm, H.5
  • 32
    • 0034730124 scopus 로고    scopus 로고
    • Importance of replication in microarray gene expression studies: Statistical methods and evidence from repetitive cDNA hybridizations
    • Lee MLT, Kuo FC, Whitmore GA, Sklar J (2000) Importance of replication in microarray gene expression studies: statistical methods and evidence from repetitive cDNA hybridizations. Proc Nat Soc Sci USA 97:9834-9839
    • (2000) Proc Nat Soc Sci USA , vol.97 , pp. 9834-9839
    • Lee, M.L.T.1    Kuo, F.C.2    Whitmore, G.A.3    Sklar, J.4
  • 33
    • 0037133256 scopus 로고    scopus 로고
    • The Ni-containing carbon monoxide dehydrogenase family: Light at the end of the tunnel?
    • Lindahl PA (2002) The Ni-containing carbon monoxide dehydrogenase family: light at the end of the tunnel? Biochemistry 41:2097-2105
    • (2002) Biochemistry , vol.41 , pp. 2097-2105
    • Lindahl, P.A.1
  • 34
    • 0024962598 scopus 로고
    • Activation of acetate by Methanosarcina thermophila - Purification and characterization of phosphotransacetylase
    • Lundie LL, Ferry JG (1989) Activation of acetate by Methanosarcina thermophila - purification and characterization of phosphotransacetylase. J Biol Chem 264:18392-18396
    • (1989) J Biol Chem , vol.264 , pp. 18392-18396
    • Lundie, L.L.1    Ferry, J.G.2
  • 35
    • 0030058857 scopus 로고    scopus 로고
    • Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila
    • Maupin-Furlow J, Ferry JG (1996) Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila. J Bacteriol 178:340-346
    • (1996) J Bacteriol , vol.178 , pp. 340-346
    • Maupin-Furlow, J.1    Ferry, J.G.2
  • 36
    • 0023276124 scopus 로고
    • Immunoelectron microscopic demonstration of ATPase on the cytoplasmic membrane of the methanogenic bacterium strain Gö1
    • Mayer F, Jussofie A, Salzmann M, Lübben M, Rohde M, Gottschalk G (1987) Immunoelectron microscopic demonstration of ATPase on the cytoplasmic membrane of the methanogenic bacterium strain Gö1. J Bacteriol 169:2307-2309
    • (1987) J Bacteriol , vol.169 , pp. 2307-2309
    • Mayer, F.1    Jussofie, A.2    Salzmann, M.3    Lübben, M.4    Rohde, M.5    Gottschalk, G.6
  • 37
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer J, Bartoschek S, Koch J, Künkel A, Hedderich R (1999) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur J Biochem 265:325-335
    • (1999) Eur J Biochem , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Künkel, A.4    Hedderich, R.5
  • 38
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer J, Kuettner HC, Zhang JK, Hedderich R, Metcalf WW (2002) Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc Natl Acad Sci USA 99:5632-5637
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 39
    • 0028810413 scopus 로고
    • Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro
    • Michel R, Massanz C, Kostka S, Richter M, Fiebig K (1995) Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro. Eur J Biochem 233:727-735
    • (1995) Eur J Biochem , vol.233 , pp. 727-735
    • Michel, R.1    Massanz, C.2    Kostka, S.3    Richter, M.4    Fiebig, K.5
  • 40
    • 0037955289 scopus 로고    scopus 로고
    • ATP synthases: Structure, function and evolution of unique energy converters
    • Müller V, Gruber G (2003) ATP synthases: structure, function and evolution of unique energy converters. Cell Mol Life Sci 60:474-494
    • (2003) Cell Mol Life Sci , vol.60 , pp. 474-494
    • Müller, V.1    Gruber, G.2
  • 42
    • 0032885357 scopus 로고    scopus 로고
    • Acetyl coenzyme a synthetase (ADP forming) from the hyperthermophilic archaeon Pyrococcus furiosus: Identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits
    • Musfeldt M, Selig M, Schönheit P (1999) Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic archaeon Pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits. J Bacteriol 181:5885-5888
    • (1999) J Bacteriol , vol.181 , pp. 5885-5888
    • Musfeldt, M.1    Selig, M.2    Schönheit, P.3
  • 43
    • 0034005319 scopus 로고    scopus 로고
    • The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons
    • Paul L, Ferguson DJ, Krzycki JA (2000) The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons. J Bacteriol 182:2520-2529
    • (2000) J Bacteriol , vol.182 , pp. 2520-2529
    • Paul, L.1    Ferguson, D.J.2    Krzycki, J.A.3
  • 44
    • 0035057561 scopus 로고    scopus 로고
    • Validation of array-based gene expression profiles by real-time (kinetic) RT-PCR
    • Rajeevan MS, Vernon SD, Taysavang N, Unger ER (2001) Validation of array-based gene expression profiles by real-time (kinetic) RT-PCR. J Mol Diagnostics 1:26-31
    • (2001) J Mol Diagnostics , vol.1 , pp. 26-31
    • Rajeevan, M.S.1    Vernon, S.D.2    Taysavang, N.3    Unger, E.R.4
  • 45
    • 0034486651 scopus 로고    scopus 로고
    • Biosynthesis of cobalamin (vitamin B-12): A bacterial conundrum
    • Raux E, Schubert HL, Warren MJ (2000) Biosynthesis of cobalamin (vitamin B-12): a bacterial conundrum. Cell Mol Life Sci 57:1880-1893
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1880-1893
    • Raux, E.1    Schubert, H.L.2    Warren, M.J.3
  • 46
    • 0000973692 scopus 로고    scopus 로고
    • Regulation of carbon utilization
    • Neidhardt FC, Curtiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) ASM, Washington
    • Saier MH, Ramseier TM, Reizer J (1996) Regulation of carbon utilization. In: Neidhardt FC, Curtiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella: cellular and molecular biology, 2nd edn. ASM, Washington, pp 1325-1343
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Edn. , pp. 1325-1343
    • Saier, M.H.1    Ramseier, T.M.2    Reizer, J.3
  • 47
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase-3 formation in Escherichia coli
    • Sauter M, Böhm R, Böck A (1992) Mutational analysis of the operon (hyc) determining hydrogenase-3 formation in Escherichia coli. Mol Microbiol 6:1523-1532
    • (1992) Mol Microbiol , vol.6 , pp. 1523-1532
    • Sauter, M.1    Böhm, R.2    Böck, A.3
  • 48
    • 0028922177 scopus 로고
    • Transcriptional regulation of the phosphotransacetylase-encoding and acetate kinase-encod-ing genes (pta and ack) from Methanosarcina thermophila
    • Singh-Wissmann K, Ferry JG (1995) Transcriptional regulation of the phosphotransacetylase-encoding and acetate kinase-encod-ing genes (pta and ack) from Methanosarcina thermophila. J Bacteriol 177:1699-1702
    • (1995) J Bacteriol , vol.177 , pp. 1699-1702
    • Singh-Wissmann, K.1    Ferry, J.G.2
  • 49
    • 0020604041 scopus 로고
    • Proteins induced by aerobiosis in Escherichia coli
    • Smith MW, Neidhardt FC (1983a) Proteins induced by aerobiosis in Escherichia coli. J Bacteriol 154:344-350
    • (1983) J Bacteriol , vol.154 , pp. 344-350
    • Smith, M.W.1    Neidhardt, F.C.2
  • 50
    • 0020587228 scopus 로고
    • Proteins induced by anaerobiosis in Escherichia coli
    • Smith MW, Neidhardt FC (1983b) Proteins induced by anaerobiosis in Escherichia coli. J Bacteriol 154:336-343
    • (1983) J Bacteriol , vol.154 , pp. 336-343
    • Smith, M.W.1    Neidhardt, F.C.2
  • 51
    • 0027433047 scopus 로고
    • Transcriptional regulation of the carbon monoxide dehydrogenase gene (cdhA) in Methanosarcina thermophila
    • Sowers KR, Thai TT, Gunsalus RP (1993) Transcriptional regulation of the carbon monoxide dehydrogenase gene (cdhA) in Methanosarcina thermophila. J Biol Chem 268:23172-23178
    • (1993) J Biol Chem , vol.268 , pp. 23172-23178
    • Sowers, K.R.1    Thai, T.T.2    Gunsalus, R.P.3
  • 52
    • 0042424602 scopus 로고    scopus 로고
    • Statistical significance for genomewide studies
    • Storey JD, Tibshirani R (2003) Statistical significance for genomewide studies. Proc Natl Acad Sci USA 100:9440-9445
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9440-9445
    • Storey, J.D.1    Tibshirani, R.2
  • 53
    • 0030785505 scopus 로고    scopus 로고
    • Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate
    • Tallant TC, Krzycki JA (1997) Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate. J Bacteriol 179:6902-6911
    • (1997) J Bacteriol , vol.179 , pp. 6902-6911
    • Tallant, T.C.1    Krzycki, J.A.2
  • 54
    • 0032693327 scopus 로고    scopus 로고
    • Functional genomics: Expression analysis of Escherichia coli growing on minimal and rich media
    • Tao H, Bausch C, Richmond C, Blattner FR, Conway T (1999) Functional genomics: expression analysis of Escherichia coli growing on minimal and rich media. J Bacteriol 181:6425-6440
    • (1999) J Bacteriol , vol.181 , pp. 6425-6440
    • Tao, H.1    Bausch, C.2    Richmond, C.3    Blattner, F.R.4    Conway, T.5
  • 55
    • 0032694979 scopus 로고    scopus 로고
    • Aerotaxis and other energy-sensing behavior in bacteria
    • Taylor BL, Zhulin IB, Johnson MS (1999) Aerotaxis and other energy-sensing behavior in bacteria. Annu Rev Microbiol 53:103-128
    • (1999) Annu Rev Microbiol , vol.53 , pp. 103-128
    • Taylor, B.L.1    Zhulin, I.B.2    Johnson, M.S.3
  • 56
    • 0022860139 scopus 로고
    • Isolation of an enzyme complex with carbon monoxide dehydrogenase activity containing corrinoid and nickel from acetate-grown Methanosarcina thermophila
    • Terlesky K, Nelson MJK, Ferry JG (1986) Isolation of an enzyme complex with carbon monoxide dehydrogenase activity containing corrinoid and nickel from acetate-grown Methanosarcina thermophila. J Bacteriol 168:1053-1058
    • (1986) J Bacteriol , vol.168 , pp. 1053-1058
    • Terlesky, K.1    Nelson, M.J.K.2    Ferry, J.G.3
  • 57
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer RK (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144:2377-2406
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 58
    • 0035875553 scopus 로고    scopus 로고
    • Issues in cDNA microarray analysis: Quality filtering, channel normalization, models of variations and assessment of gene effects
    • Tseng GC, Oh MK, Rohlin L, Liao JC, Wong WH (2001) Issues in cDNA microarray analysis: quality filtering, channel normalization, models of variations and assessment of gene effects. Nucleic Acids Res 29:2549-2557
    • (2001) Nucleic Acids Res , vol.29 , pp. 2549-2557
    • Tseng, G.C.1    Oh, M.K.2    Rohlin, L.3    Liao, J.C.4    Wong, W.H.5
  • 59
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to ionizingradiation response
    • Tusher V, Tibshirani R, Chu C (2001) Significance analysis of microarrays applied to ionizingradiation response. Proc Natl Acad Sci USA 98:5116-5121
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5116-5121
    • Tusher, V.1    Tibshirani, R.2    Chu, C.3
  • 60
    • 0030613533 scopus 로고    scopus 로고
    • 2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea
    • 2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. Eur J Biochem 248:919-924
    • (1997) Eur J Biochem , vol.248 , pp. 919-924
    • Vorholt, J.A.1    Thauer, R.K.2
  • 61
    • 0029915852 scopus 로고    scopus 로고
    • A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri
    • Vorholt JA, Vaupel M, Thauer RK (1996) A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri. Eur J Biochem 236:309-317
    • (1996) Eur J Biochem , vol.236 , pp. 309-317
    • Vorholt, J.A.1    Vaupel, M.2    Thauer, R.K.3
  • 63
    • 0034782618 scopus 로고    scopus 로고
    • Model-based clustering and data transformations for gene expression data
    • Yeung KY, Fraley C, Murua A, Raftery AE, Ruzzo WL (2001) Model-based clustering and data transformations for gene expression data. Bioinformatics 17:977-987
    • (2001) Bioinformatics , vol.17 , pp. 977-987
    • Yeung, K.Y.1    Fraley, C.2    Murua, A.3    Raftery, A.E.4    Ruzzo, W.L.5
  • 64
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox
    • Zhulin IB, Taylor BL, Dixon R (1997) PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Trends Biochem Sci 22:331-333
    • (1997) Trends Biochem Sci , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 66
    • 0021876570 scopus 로고
    • Growth substrate effects on acetate and methanol catabolism in Methanosarcina sp. strain TM-1
    • Zinder SH, Elias AF (1985) Growth substrate effects on acetate and methanol catabolism in Methanosarcina sp. strain TM-1. J Bacteriol 163:317-323
    • (1985) J Bacteriol , vol.163 , pp. 317-323
    • Zinder, S.H.1    Elias, A.F.2


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