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Volumn 192, Issue 20, 2010, Pages 5329-5340

Regulation of autotrophic CO2 fixation in the archaeon Thermoproteus neutrophilus

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DIOXIDE; COENZYME A; CROTONYL COENZYME A; FUMARATE REDUCTASE; PHOSPHOENOLPYRUVATE CARBOXYLASE; SUCCINYL COENZYME A; UNCLASSIFIED DRUG; ACETIC ACID DERIVATIVE; ARCHAEAL PROTEIN;

EID: 77957848173     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00729-10     Document Type: Article
Times cited : (18)

References (70)
  • 2
    • 0141939275 scopus 로고    scopus 로고
    • Pyrobaculum calidifontis sp. nov., a novel hyperthermophilic archaeon that grows in atmospheric air
    • Amo, T., M. L. Paje, A. Inagaki, S. Ezaki, H. Atomi, and T. Imanaka. 2002. Pyrobaculum calidifontis sp. nov., a novel hyperthermophilic archaeon that grows in atmospheric air. Archaea 1:113-121.
    • (2002) Archaea , vol.1 , pp. 113-121
    • Amo, T.1    Paje, M.L.2    Inagaki, A.3    Ezaki, S.4    Atomi, H.5    Imanaka, T.6
  • 3
    • 33645814181 scopus 로고    scopus 로고
    • A leaderless mRNA can bind to mammalian 80S ribosomes and direct polypeptide synthesis in the absence of translation initiation factors
    • Andreev, D. E., I. M. Terenin, Y. E. Dunaevsky, S. E. Dimtriev, and I. N. Shatsky. 2006. A leaderless mRNA can bind to mammalian 80S ribosomes and direct polypeptide synthesis in the absence of translation initiation factors. Mol. Cell. Biol. 26:3164-3169.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3164-3169
    • Andreev, D.E.1    Terenin, I.M.2    Dunaevsky, Y.E.3    Dimtriev, S.E.4    Shatsky, I.N.5
  • 5
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • Bateman, A. 1997. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 22:12-13.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 12-13
    • Bateman, A.1
  • 6
    • 0027303801 scopus 로고
    • Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus
    • Beh, M., G. Strauss, R. Huber, K. O. Stetter, and G. Fuchs. 1993. Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus. Arch. Microbiol. 160:306-311.
    • (1993) Arch. Microbiol. , vol.160 , pp. 306-311
    • Beh, M.1    Strauss, G.2    Huber, R.3    Stetter, K.O.4    Fuchs, G.5
  • 7
    • 0037023326 scopus 로고    scopus 로고
    • The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation
    • Bell, S. D., C. H. Botting, B. N. Wardleworth, S. P. Jackson, and M. F. White. 2002. The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science 296:148-151.
    • (2002) Science , vol.296 , pp. 148-151
    • Bell, S.D.1    Botting, C.H.2    Wardleworth, B.N.3    Jackson, S.P.4    White, M.F.5
  • 8
    • 0033400812 scopus 로고    scopus 로고
    • Transcriptional regulation of an archaeal operon in vivo and in vitro
    • Bell, S. D., S. S. Cairns, R. L. Robson, and S. P. Jackson. 1999. Transcriptional regulation of an archaeal operon in vivo and in vitro. Mol. Cell 4:971-982.
    • (1999) Mol. Cell , vol.4 , pp. 971-982
    • Bell, S.D.1    Cairns, S.S.2    Robson, R.L.3    Jackson, S.P.4
  • 9
    • 0032102006 scopus 로고    scopus 로고
    • Transcription and translation in Archaea: A mosaic of eukaryal and bacterial features
    • Bell, S. D., and S. P. Jackson. 1998. Transcription and translation in Archaea: a mosaic of eukaryal and bacterial features. Trends Microbiol. 6:222-228.
    • (1998) Trends Microbiol. , vol.6 , pp. 222-228
    • Bell, S.D.1    Jackson, S.P.2
  • 10
    • 0034644711 scopus 로고    scopus 로고
    • Mechanism of autoregulation by an archaeal transcriptional repressor
    • Bell, S. D., and S. P. Jackson. 2000. Mechanism of autoregulation by an archaeal transcriptional repressor. J. Biol. Chem. 275:31624-31629.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31624-31629
    • Bell, S.D.1    Jackson, S.P.2
  • 12
    • 37249052742 scopus 로고    scopus 로고
    • A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea
    • Berg, I. A., D. Kockelkorn, W. Buckel, and G. Fuchs. 2007. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318:1782-1786.
    • (2007) Science , vol.318 , pp. 1782-1786
    • Berg, I.A.1    Kockelkorn, D.2    Buckel, W.3    Fuchs, G.4
  • 15
    • 0016723542 scopus 로고
    • Neue Werte für die molaren Extinktions-Koeffizienten von NADH und NADPH zum Gebrauch im Routine-Laboratorium
    • Bergmeyer, H. U. 1975. Neue Werte für die molaren Extinktions-Koeffizienten von NADH und NADPH zum Gebrauch im Routine-Laboratorium. Z. Klin. Chem. Klin. Biochem. 13:507-508.
    • (1975) Z. Klin. Chem. Klin. Biochem. , vol.13 , pp. 507-508
    • Bergmeyer, H.U.1
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 17
    • 37749051212 scopus 로고    scopus 로고
    • Experimental characterization of cis-acting elements important for translation and transcription in halophilic archaea
    • Brenneis, M., O. Hering, C. Lange, and J. Soppa. 2007. Experimental characterization of cis-acting elements important for translation and transcription in halophilic archaea. PloS Genet. 3:e229.
    • (2007) PloS Genet. , vol.3
    • Brenneis, M.1    Hering, O.2    Lange, C.3    Soppa, J.4
  • 18
    • 0032513241 scopus 로고    scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. J. Biol. Chem. 273:6149-6156.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6149-6156
    • Brunner, N.A.1    Brinkmann, H.2    Siebers, B.3    Hensel, R.4
  • 19
    • 0035321642 scopus 로고    scopus 로고
    • Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: Regulation on protein and transcript level
    • Brunner, N. A., B. Siebers, and R. Hensel. 2001. Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level. Extremophiles 5:101-109.
    • (2001) Extremophiles , vol.5 , pp. 101-109
    • Brunner, N.A.1    Siebers, B.2    Hensel, R.3
  • 21
    • 0025257201 scopus 로고
    • Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in δ-aminolevulinic acid formation during chlorophyll biosynthesis
    • Chen, M. W., D. Jahn, G. P. O'Neill, and D. Söll. 1990. Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in δ-aminolevulinic acid formation during chlorophyll biosynthesis. J. Biol. Chem. 265:4058-4063.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4058-4063
    • Chen, M.W.1    Jahn, D.2    O'Neill, G.P.3    Söll, D.4
  • 22
    • 33645216182 scopus 로고    scopus 로고
    • Identification of RamA, a novel LuxR-type transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum
    • Cramer, A., R. Gerstmeir, S. Schaffer, M. Bott, and B. Eikmanns. 2006. Identification of RamA, a novel LuxR-type transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum. J. Bacteriol. 188:2554-2567.
    • (2006) J. Bacteriol. , vol.188 , pp. 2554-2567
    • Cramer, A.1    Gerstmeir, R.2    Schaffer, S.3    Bott, M.4    Eikmanns, B.5
  • 23
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler, J., and M. W. W. Adams. 2005. Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 69:393-425.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 24
    • 0020701677 scopus 로고
    • Chemolithoautotrophic metabolism of anaerobic extremely thermophilic archaebacteria
    • DOI 10.1038/301511a0
    • Fischer, F., W. Zillig, K. O. Stetter, and G. Schreiber. 1983. Chemolithoautotrophic metabolism of anaerobic extremely thermophilic archaebacteria. Nature 301:511-513. (Pubitemid 13160568)
    • (1983) Nature , vol.301 , Issue.5900 , pp. 511-513
    • Fischer, F.1    Zillig, W.2    Stetter, K.O.3    Schreiber, G.4
  • 25
    • 0026768866 scopus 로고
    • Elements of an archaeal promoter defined by mutational analysis
    • Hain, J., W. D. Reiter, U. Hüdepohl, and W. Zillig. 1992. Elements of an archaeal promoter defined by mutational analysis. Nucleic Acids Res. 20: 5423-5428.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5423-5428
    • Hain, J.1    Reiter, W.D.2    Hüdepohl, U.3    Zillig, W.4
  • 26
    • 62449324914 scopus 로고    scopus 로고
    • A novel mechanism for translation initiation operates in haloarchaea
    • Hering, O., M. Brenneis, J. Beer, B. Suess, and J. Soppa. 2009. A novel mechanism for translation initiation operates in haloarchaea. Mol. Microbiol. 71:1451-1463.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1451-1463
    • Hering, O.1    Brenneis, M.2    Beer, J.3    Suess, B.4    Soppa, J.5
  • 29
    • 0037294946 scopus 로고    scopus 로고
    • Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Carboxylating enzyme in the 3-hydroxypropionate cycle for autotrophic carbon fixation
    • Hügler, M., R. S. Krieger, M. Jahn, and G. Fuchs. 2003. Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Carboxylating enzyme in the 3-hydroxypropionate cycle for autotrophic carbon fixation. Eur. J. Biochem. 270:736-744.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 736-744
    • Hügler, M.1    Krieger, R.S.2    Jahn, M.3    Fuchs, G.4
  • 30
    • 34249798717 scopus 로고    scopus 로고
    • 2 fixation pathway of the archaeon Ignicoccus hospitalis: Comprehensive analysis of the central carbon metabolism
    • 2 fixation pathway of the archaeon Ignicoccus hospitalis: comprehensive analysis of the central carbon metabolism. J. Bacteriol. 189:4108-4119.
    • (2007) J. Bacteriol. , vol.189 , pp. 4108-4119
    • Jahn, U.1    Huber, H.2    Eisenreich, W.3    Hügler, M.4    Fuchs, G.5
  • 31
    • 0026686195 scopus 로고
    • Glutamyl-transfer RNA: A precursor of heme and chlorophyll biosynthesis
    • Jahn, D., E. Verkamp, and D. Söll. 1992. Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis. Trends Biochem. Sci. 17:215-218.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 215-218
    • Jahn, D.1    Verkamp, E.2    Söll, D.3
  • 32
    • 31444453261 scopus 로고    scopus 로고
    • The physiological role of the ribulose monophosphate pathway in bacteria and archaea
    • Kato, N., H. Yurimoto, and R. K. Thauer. 2006. The physiological role of the ribulose monophosphate pathway in bacteria and archaea. Biosci. Biotechnol. Biochem. 70:10-21.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 10-21
    • Kato, N.1    Yurimoto, H.2    Thauer, R.K.3
  • 33
    • 44649151037 scopus 로고    scopus 로고
    • Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon
    • King, N. P., T. M. Lee, M. R. Sawaya, D. Cascio, and T. O. Yeates. 2008. Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon. J. Mol. Biol. 380:181-192.
    • (2008) J. Mol. Biol. , vol.380 , pp. 181-192
    • King, N.P.1    Lee, T.M.2    Sawaya, M.R.3    Cascio, D.4    Yeates, T.O.5
  • 34
    • 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
  • 35
    • 0033598826 scopus 로고    scopus 로고
    • The structural basis for the oriented assembly of a TBP/TFB/promoter complex
    • Littlefield, O., Y. Korkhin, and P. B. Sigler. 1999. The structural basis for the oriented assembly of a TBP/TFB/promoter complex. Proc. Natl. Acad. Sci. U. S. A. 96:13668-13673.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13668-13673
    • Littlefield, O.1    Korkhin, Y.2    Sigler, P.B.3
  • 36
    • 4344591748 scopus 로고    scopus 로고
    • Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax
    • Lorentzen, E., R. Hensel, T. Knura, H. Ahmed, and E. Pohl. 2004. Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax. J. Mol. Biol. 341:815-828.
    • (2004) J. Mol. Biol. , vol.341 , pp. 815-828
    • Lorentzen, E.1    Hensel, R.2    Knura, T.3    Ahmed, H.4    Pohl, E.5
  • 37
    • 20444427964 scopus 로고    scopus 로고
    • Sir2 and the acetyltransferase, Pat, regulate the archaeal chromatin protein, Alba
    • Marsch, V. L., S. Y. Peak-Chew, and S. D. Bell. 2008. Sir2 and the acetyltransferase, Pat, regulate the archaeal chromatin protein, Alba. J. Biol. Chem. 380:21122-21128.
    • (2008) J. Biol. Chem. , vol.380 , pp. 21122-21128
    • Marsch, V.L.1    Peak-Chew, S.Y.2    Bell, S.D.3
  • 38
    • 8144230590 scopus 로고    scopus 로고
    • Crystal structure of 4-hydroxybutyryl-CoA dehydratase: Radical catalysis involving a [4Fe-4S] cluster and flavin
    • Martins, B. M., H. Dobbek, I. Cinkaya, W. Buckel, and A. Messerschmidt. 2004. Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin. Proc. Natl. Acad. Sci. U. S. A. 101:15645-15649.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15645-15649
    • Martins, B.M.1    Dobbek, H.2    Cinkaya, I.3    Buckel, W.4    Messerschmidt, A.5
  • 39
    • 3042690803 scopus 로고    scopus 로고
    • Translation initiation with 70S ribosomes: An alternative pathway for leaderless mRNAs
    • DOI 10.1093/nar/gkh663
    • Moll, I., G. Hirokawa, M. C. Kiel, A. Kaji, and U. Bläsi. 2004. Translation initiation with 70S ribosomes: an alternative pathway for leaderless mRNAs. Nucleic Acids Res. 32:3354-3363. (Pubitemid 39117451)
    • (2004) Nucleic Acids Research , vol.32 , Issue.11 , pp. 3354-3363
    • Moll, I.1    Hirokawa, G.2    Kiel, M.C.3    Kaji, A.4    Blasi, U.5
  • 40
    • 0026044139 scopus 로고
    • Carboxy-terminal sequence conservation among variant-specific surface proteins of Giardia lamblia
    • Mowatt, M. R., A. Aggarwal, and T. E. Nash. 1991. Carboxy-terminal sequence conservation among variant-specific surface proteins of Giardia lamblia. Mol. Biochem. Parasitol. 49:215-227.
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 215-227
    • Mowatt, M.R.1    Aggarwal, A.2    Nash, T.E.3
  • 42
    • 33745444345 scopus 로고    scopus 로고
    • The ribulose monophosphate pathway substitutes for the missing pentose phosphate pathway in the archaeon Thermococcus kodakaraensis
    • Orita, I., T. Sato, N. Kato, H. Atomi, T. Imanaka, and Y. Sakai. 2006. The ribulose monophosphate pathway substitutes for the missing pentose phosphate pathway in the archaeon Thermococcus kodakaraensis. J. Bacteriol. 188:4698-4704.
    • (2006) J. Bacteriol. , vol.188 , pp. 4698-4704
    • Orita, I.1    Sato, T.2    Kato, N.3    Atomi, H.4    Imanaka, T.5    Sakai, Y.6
  • 43
    • 0028908091 scopus 로고
    • In vivo definition of an archaeal promoter
    • Palmer, J. R., and C. J. Daniels. 1995. In vivo definition of an archaeal promoter. J. Bacteriol. 177:1844-1849.
    • (1995) J. Bacteriol. , vol.177 , pp. 1844-1849
    • Palmer, J.R.1    Daniels, C.J.2
  • 45
    • 0031990302 scopus 로고    scopus 로고
    • Sequence-specific DNA binding by the S. shibatae TFIIB homolog, TFB, and its effect on promoter strength
    • Qureshi, S. A., and S. P. Jackson. 1998. Sequence-specific DNA binding by the S. shibatae TFIIB homolog, TFB, and its effect on promoter strength. Mol. Cell 1:389-400.
    • (1998) Mol. Cell , vol.1 , pp. 389-400
    • Qureshi, S.A.1    Jackson, S.P.2
  • 46
    • 67649413349 scopus 로고    scopus 로고
    • Autotrophic carbon dioxide assimilation in Thermoproteales revisited
    • Ramos-Vera, W. H., I. A. Berg, and G. Fuchs. 2009. Autotrophic carbon dioxide assimilation in Thermoproteales revisited. J. Bacteriol. 191:4286-4297.
    • (2009) J. Bacteriol. , vol.191 , pp. 4286-4297
    • Ramos-Vera, W.H.1    Berg, I.A.2    Fuchs, G.3
  • 47
    • 0025630439 scopus 로고
    • Mutational analysis of an archaebacterial promoter: Essential role of a TATA box for transcription efficiency and start-site selection in vitro
    • Reiter, W. D., U. Hüdepohl, and W. Zilling. 1990. Mutational analysis of an archaebacterial promoter: essential role of a TATA box for transcription efficiency and start-site selection in vitro. Proc. Natl. Acad. Sci. U. S. A. 87:9509-9513.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 9509-9513
    • Reiter, W.D.1    Hüdepohl, U.2    Zilling, W.3
  • 48
    • 0028361219 scopus 로고
    • The TATA-binding protein: A general transcription factor in eukaryotes and archaebacteria
    • Rowlands, T., P. Baumann, and S. P. Jackson. 1994. The TATA-binding protein: a general transcription factor in eukaryotes and archaebacteria. Science 264:1326-1329.
    • (1994) Science , vol.264 , pp. 1326-1329
    • Rowlands, T.1    Baumann, P.2    Jackson, S.P.3
  • 49
    • 0022895194 scopus 로고
    • Carbon assimilation by the autotrophic thermophilic archaebacterium Thermoproteus neutrophilus
    • Schäfer, S., C. Barkowski, and G. Fuchs. 1986. Carbon assimilation by the autotrophic thermophilic archaebacterium Thermoproteus neutrophilus. Arch. Microbiol. 146:301-308.
    • (1986) Arch. Microbiol. , vol.146 , pp. 301-308
    • Schäfer, S.1    Barkowski, C.2    Fuchs, G.3
  • 52
    • 0023051874 scopus 로고
    • The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA
    • Schön, A., G. Krupp, S. Gough, S. Berry-Lowe, C. G. Kannangara, and D. Söll. 1986. The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA. Nature 322:281-284.
    • (1986) Nature , vol.322 , pp. 281-284
    • Schön, A.1    Krupp, G.2    Gough, S.3    Berry-Lowe, S.4    Kannangara, C.G.5    Söll, D.6
  • 54
    • 0001571980 scopus 로고
    • δ-Aminolevulinic acid, its role in the biosynthesis of porphyrins and purines
    • Shemin, D., and C. Russel. 1953. δ-Aminolevulinic acid, its role in the biosynthesis of porphyrins and purines. J. Am. Chem. Soc. 75:4873-4875.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 4873-4875
    • Shemin, D.1    Russel, C.2
  • 56
    • 0033052407 scopus 로고    scopus 로고
    • Transcription initiation in Archaea: Facts, factors and future aspects
    • Soppa, J. 1999. Transcription initiation in Archaea: facts, factors and future aspects. Mol. Microbiol. 31:1295-1305.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1295-1305
    • Soppa, J.1
  • 57
    • 0026611716 scopus 로고
    • 2 fixation pathways in the sulphur-reducing archaebacterium Thermoproteus neutrophilus and in the phototrophic eubacterium Chloroflexus aurantiacus
    • 2 fixation pathways in the sulphur-reducing archaebacterium Thermoproteus neutrophilus and in the phototrophic eubacterium Chloroflexus aurantiacus. Eur. J. Biochem. 205:853-866.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 853-866
    • Strauss, G.1    Eisenreich, W.2    Bacher, A.3    Fuchs, G.4
  • 58
    • 0021919826 scopus 로고
    • A bacteriophage-T7 RNA-polymerase promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage-T7 RNA-polymerase promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. U. S. A. 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 59
    • 0029887361 scopus 로고    scopus 로고
    • Archaeal transcription factors and their role in transcription initiation
    • Thomm, M. 1996. Archaeal transcription factors and their role in transcription initiation. FEMS Microbiol. Rev. 18:159-171.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 159-171
    • Thomm, M.1
  • 60
    • 84890639854 scopus 로고    scopus 로고
    • Transcriptional mechanisms
    • R. A. Garrett and H. P. Klenk (ed.), Blackwell Publishing, Malden, MA
    • Thomm, M., and W. Hausner. 2007. Transcriptional mechanisms, p. 187-198. In R. A. Garrett and H. P. Klenk (ed.), Archaea: evolution, physiology, and molecular biology. Blackwell Publishing, Malden, MA.
    • (2007) Archaea: Evolution, Physiology, and Molecular Biology , pp. 187-198
    • Thomm, M.1    Hausner, W.2
  • 61
    • 33645324044 scopus 로고    scopus 로고
    • Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase of Thermoproteus tenax: Key pieces in the puzzle of archaeal carbohydrate metabolism
    • Tjaden, B., A. Plagens, C. Dörr, B. Siebers, and R. Hensel. 2006. Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase of Thermoproteus tenax: key pieces in the puzzle of archaeal carbohydrate metabolism. Mol. Microbiol. 60:287-298.
    • (2006) Mol. Microbiol. , vol.60 , pp. 287-298
    • Tjaden, B.1    Plagens, A.2    Dörr, C.3    Siebers, B.4    Hensel, R.5
  • 62
    • 0034202785 scopus 로고    scopus 로고
    • Two different and highly organized mechanisms of translation initiation in the archaeon Sulfolobus solfataricus
    • Tolstrup, N., C. W. Sensen, R. A. Garrett, and I. G. Clausen. 2000. Two different and highly organized mechanisms of translation initiation in the archaeon Sulfolobus solfataricus. Extremophiles 4:175-179.
    • (2000) Extremophiles , vol.4 , pp. 175-179
    • Tolstrup, N.1    Sensen, C.W.2    Garrett, R.A.3    Clausen, I.G.4
  • 63
    • 0037009516 scopus 로고    scopus 로고
    • Structure of Alba: An archaeal chromatin protein modulated by acetylation
    • Wardleworth, B. N., R. J. Russell, S. D. Bell, G. L. Taylor, and M. F. White. 2002. Structure of Alba: an archaeal chromatin protein modulated by acetylation. EMBO J. 21:4654-4662.
    • (2002) EMBO J. , vol.21 , pp. 4654-4662
    • Wardleworth, B.N.1    Russell, R.J.2    Bell, S.D.3    Taylor, G.L.4    White, M.F.5
  • 64
    • 0030293885 scopus 로고    scopus 로고
    • Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP: ATP ratio
    • Wilson, W. A., S. A. Hawley, and D. G. Hardie. 1996. Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP: ATP ratio. Curr. Biol. 6:1426-1434.
    • (1996) Curr. Biol. , vol.6 , pp. 1426-1434
    • Wilson, W.A.1    Hawley, S.A.2    Hardie, D.G.3
  • 65
    • 39149121854 scopus 로고    scopus 로고
    • ε-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
    • ε-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function. Nucleic Acids Res. 36:570-577.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 570-577
    • Wiśniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 66
    • 0033917479 scopus 로고    scopus 로고
    • An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion
    • Xue, H., R. Guo, Y. Wenn, D. Liu, and L. Huang. 2000. An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion. J. Bacteriol. 182:3929-3933.
    • (2000) J. Bacteriol. , vol.182 , pp. 3929-3933
    • Xue, H.1    Guo, R.2    Wenn, Y.3    Liu, D.4    Huang, L.5
  • 67
    • 49749100770 scopus 로고    scopus 로고
    • The central carbohydrate metabolism of the hyperthermophilic crenarchaeote Thermoproteus tenax: Pathways and insights into their regulation
    • Zaparty, M., B. Tjaden, R. Hensel, and B. Siebers. 2008. The central carbohydrate metabolism of the hyperthermophilic crenarchaeote Thermoproteus tenax: pathways and insights into their regulation. Arch. Microbiol. 190:231-245.
    • (2008) Arch. Microbiol. , vol.190 , pp. 231-245
    • Zaparty, M.1    Tjaden, B.2    Hensel, R.3    Siebers, B.4
  • 68
    • 40449104806 scopus 로고    scopus 로고
    • DNA microarray analysis of central carbohydrate metabolism: Glycolytic/gluconeogenic carbon switch in the hyperthermophilic crenarchaeum Thermoproteus tenax
    • Zaparty, M., A. Zaigler, C. Stamme, J. Soppa, R. Hensel, and B. Siebers. 2008. DNA microarray analysis of central carbohydrate metabolism: glycolytic/gluconeogenic carbon switch in the hyperthermophilic crenarchaeum Thermoproteus tenax. J. Bacteriol. 190:2231-2238.
    • (2008) J. Bacteriol. , vol.190 , pp. 2231-2238
    • Zaparty, M.1    Zaigler, A.2    Stamme, C.3    Soppa, J.4    Hensel, R.5    Siebers, B.6
  • 69
    • 0017709116 scopus 로고
    • Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum
    • Zeikus, J. G., G. Fuchs, W. Kenealy, and R. K. Thauer. 1977. Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum. J. Bacteriol. 132:604-613.
    • (1977) J. Bacteriol. , vol.132 , pp. 604-613
    • Zeikus, J.G.1    Fuchs, G.2    Kenealy, W.3    Thauer, R.K.4
  • 70
    • 0038168161 scopus 로고    scopus 로고
    • Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA-binding
    • Zhao, K., X. Chai, and R. Marmorstein. 2003. Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA-binding. J. Biol. Chem. 278:26071-26077.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26071-26077
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3


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