메뉴 건너뛰기




Volumn 81, Issue 5, 2015, Pages 1708-1714

A novel co-responsive transcriptional regulator and enhanced H2 production by an engineered Thermococcus onnurineus NA1 strain

Author keywords

[No Author keywords available]

Indexed keywords

GENE EXPRESSION; MICROORGANISMS; NUCLEIC ACIDS; PROTEINS;

EID: 84922900706     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03019-14     Document Type: Article
Times cited : (34)

References (40)
  • 1
    • 4444331541 scopus 로고    scopus 로고
    • Life with carbon monoxide
    • Ragsdale SW. 2004. Life with carbon monoxide. Crit Rev Biochem Mol Biol 39:165-195. http://dx.doi.org/10.1080/10409230490496577.
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 165-195
    • Ragsdale, S.W.1
  • 2
    • 0035834117 scopus 로고    scopus 로고
    • Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
    • Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW. 2001. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc Natl Acad Sci USA 98:11973-11978. http://dx.doi.org/10.1073/pnas.211429998.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11973-11978
    • Drennan, C.L.1    Heo, J.2    Sintchak, M.D.3    Schreiter, E.4    Ludden, P.W.5
  • 3
    • 33750086029 scopus 로고    scopus 로고
    • The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif
    • Korbas M, Vogt S, Meyer-Klaucke W, Bill E, Lyon EJ, Thauer RK, Shima S. 2006. The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif. J Biol Chem 281:30804-30813. http://dx.doi.org/10.1074/jbc.M605306200.
    • (2006) J Biol Chem , vol.281 , pp. 30804-30813
    • Korbas, M.1    Vogt, S.2    Meyer-Klaucke, W.3    Bill, E.4    Lyon, E.J.5    Thauer, R.K.6    Shima, S.7
  • 4
    • 29844442868 scopus 로고    scopus 로고
    • Carbon monoxide: endogenous production, physiological functions, and pharmacological applications
    • Wu L, Wang R. 2005. Carbon monoxide: endogenous production, physiological functions, and pharmacological applications. Pharmacol Rev 57: 585-630. http://dx.doi.org/10.1124/pr.57.4.3.
    • (2005) Pharmacol Rev , vol.57 , pp. 585-630
    • Wu, L.1    Wang, R.2
  • 5
    • 0037069342 scopus 로고    scopus 로고
    • Prebiotic synthesis from CO atmospheres: implications for the origins of life
    • Miyakawa S, Yamanashi H, Kobayashi K, Cleaves HJ, Miller SL. 2002. Prebiotic synthesis from CO atmospheres: implications for the origins of life. Proc Natl Acad Sci USA 99:14628-14631. http://dx.doi.org/10.1073/pnas.192568299.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14628-14631
    • Miyakawa, S.1    Yamanashi, H.2    Kobayashi, K.3    Cleaves, H.J.4    Miller, S.L.5
  • 6
    • 49749116772 scopus 로고    scopus 로고
    • Carbon monoxide-dependent energy metabolism in anaerobic bacteria and archaea
    • Oelgeschläger E, Rother M. 2008. Carbon monoxide-dependent energy metabolism in anaerobic bacteria and archaea. Arch Microbiol 190:257-269. http://dx.doi.org/10.1007/s00203-008-0382-6.
    • (2008) Arch Microbiol , vol.190 , pp. 257-269
    • Oelgeschläger, E.1    Rother, M.2
  • 7
    • 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: 1515-1524.
    • (1996) J Bacteriol , vol.178 , pp. 1515-1524
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 8
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox JD, He Y, Shelver D, Roberts GP, Ludden PW. 1996. Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J Bacteriol 178:6200-6208.
    • (1996) J Bacteriol , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 9
    • 0036436922 scopus 로고    scopus 로고
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans. Eur J Biochem 269:5712-5721. http://dx.doi.org/10.1046/j.1432-1033.2002.03282.x.
    • (2002) Eur J Biochem , vol.269 , pp. 5712-5721
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 11
    • 0345161812 scopus 로고    scopus 로고
    • Sequence analysis, characterization and CO-specific transcription of the cox gene cluster on the megaplasmid pHCG3 of Oligotropha carboxidovorans
    • Santiago B, Schübel U, Egelseer C, Meyer O. 1999. Sequence analysis, characterization and CO-specific transcription of the cox gene cluster on the megaplasmid pHCG3 of Oligotropha carboxidovorans. Gene 236:115-124. http://dx.doi.org/10.1016/S0378-1119(99)00245-0.
    • (1999) Gene , vol.236 , pp. 115-124
    • Santiago, B.1    Schübel, U.2    Egelseer, C.3    Meyer, O.4
  • 12
    • 42549120776 scopus 로고    scopus 로고
    • RcoM: a new single-component transcriptional regulator of CO metabolism in bacteria
    • Kerby RL, Youn H, Roberts GP. 2008. RcoM: a new single-component transcriptional regulator of CO metabolism in bacteria. J Bacteriol 190: 3336-3343. http://dx.doi.org/10.1128/JB.00033-08.
    • (2008) J Bacteriol , vol.190 , pp. 3336-3343
    • Kerby, R.L.1    Youn, H.2    Roberts, G.P.3
  • 13
    • 0036606155 scopus 로고    scopus 로고
    • A novel type of conserved DNAbinding domain in the transcriptional regulators of the AlgR/AgrA/LytR family
    • Nikolskaya AN, Galperin MY. 2002. A novel type of conserved DNAbinding domain in the transcriptional regulators of the AlgR/AgrA/LytR family. Nucleic Acids Res 30:2453-2459. http://dx.doi.org/10.1093/nar/30.11.2453.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2453-2459
    • Nikolskaya, A.N.1    Galperin, M.Y.2
  • 14
    • 84922951754 scopus 로고    scopus 로고
    • Systematic mutational analysis of the LytTR DNA binding domain of Staphylococcus aureus virulence gene transcription factor AgrA
    • Nicod SS, Weinzierl RO, Burchell L, Escalera-Maurer A, James EH, Wigneshweraraj S. 2014. Systematic mutational analysis of the LytTR DNA binding domain of Staphylococcus aureus virulence gene transcription factor AgrA. Nucleic Acids Res 42:12523-12536. http://dx.doi.org/10.1093/nar/gku1015.
    • (2014) Nucleic Acids Res , vol.42 , pp. 12523-12536
    • Nicod, S.S.1    Weinzierl, R.O.2    Burchell, L.3    Escalera-Maurer, A.4    James, E.H.5    Wigneshweraraj, S.6
  • 15
    • 0942298565 scopus 로고    scopus 로고
    • Signal transduction by hemecontaining PAS-domain proteins
    • Gilles-Gonzalez MA, Gonzalez G. 2004. Signal transduction by hemecontaining PAS-domain proteins. J Appl Physiol 96:774-783. http://dx.doi.org/10.1152/japplphysiol.00941.2003.
    • (2004) J Appl Physiol , vol.96 , pp. 774-783
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 16
    • 0032885353 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the genes for carbon monoxide dehydrogenase and localization of molybdopterin, flavin adenine dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga pseudoflava
    • Kang BS, Kim YM. 1999. Cloning and molecular characterization of the genes for carbon monoxide dehydrogenase and localization of molybdopterin, flavin adenine dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga pseudoflava. J Bacteriol 181:5581-5590.
    • (1999) J Bacteriol , vol.181 , pp. 5581-5590
    • Kang, B.S.1    Kim, Y.M.2
  • 17
    • 0028603529 scopus 로고
    • DNA sequence of the cut A, B and C genes, encoding the molybdenum containing hydroxylase carbon monoxide dehydrogenase, from Pseudomonas thermocarboxydovorans strain C2
    • Pearson DM, O'Reilly C, Colby J, Black GW. 1994. DNA sequence of the cut A, B and C genes, encoding the molybdenum containing hydroxylase carbon monoxide dehydrogenase, from Pseudomonas thermocarboxydovorans strain C2. Biochim Biophys Acta 1188:432-438. http://dx.doi.org/10.1016/0005-2728(94)90066-3.
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 432-438
    • Pearson, D.M.1    O'Reilly, C.2    Colby, J.3    Black, G.W.4
  • 18
    • 77955293228 scopus 로고    scopus 로고
    • Identification of trans-and cis-control elements involved in regulation of the carbon monoxide dehydrogenase genes in Mycobacterium s. strain JC1 DSM 3803
    • Oh J-I, Park S-J, Shin S-J, Ko I-J, Han SJ, Park SW, Song T, Kim YM. 2010. Identification of trans-and cis-control elements involved in regulation of the carbon monoxide dehydrogenase genes in Mycobacterium sp. strain JC1 DSM 3803. J Bacteriol 192:3925-3933. http://dx.doi.org/10.1128/JB.00286-10.
    • (2010) J Bacteriol , vol.192 , pp. 3925-3933
    • Oh, J.-I.1    Park, S.-J.2    Shin, S.-J.3    Ko, I.-J.4    Han, S.J.5    Park, S.W.6    Song, T.7    Kim, Y.M.8
  • 19
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell MA. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu Rev Microbiol 47:597-626. http://dx.doi.org/10.1146/annurev.mi.47.100193.003121.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 20
    • 0344066227 scopus 로고    scopus 로고
    • Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA
    • Aono S. 2003. Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA. Acc Chem Res 36:825-831. http://dx.doi.org/10.1021/ar020097p.
    • (2003) Acc Chem Res , vol.36 , pp. 825-831
    • Aono, S.1
  • 24
    • 77956803428 scopus 로고    scopus 로고
    • Identification of a novel class of membrane-bound [NiFe]-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis
    • Lim JK, Kang SG, Lebedinsky AV, Lee J-H, Lee HS. 2010. Identification of a novel class of membrane-bound [NiFe]-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis. Appl Environ Microbiol 76: 6286-6289. http://dx.doi.org/10.1128/AEM.00123-10.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 6286-6289
    • Lim, J.K.1    Kang, S.G.2    Lebedinsky, A.V.3    Lee, J.-H.4    Lee, H.S.5
  • 25
    • 0030856066 scopus 로고    scopus 로고
    • CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein
    • Shelver D, Kerby RL, He Y, Roberts GP. 1997. CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. Proc Natl Acad Sci USA 94:11216-11220. http://dx.doi.org/10.1073/pnas.94.21.11216.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11216-11220
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 27
    • 33845593742 scopus 로고    scopus 로고
    • Thermococcus onnurineus sp. nov., a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent area at the PACMANUS field
    • Bae SS, Kim YJ, Yang SH, Lim JK, Jeon JH, Lee HS, Kang SG, Kim SJ, Lee JH. 2006. Thermococcus onnurineus sp. nov., a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent area at the PACMANUS field. J Microbiol Biotechnol 16:1826-1831.
    • (2006) J Microbiol Biotechnol , vol.16 , pp. 1826-1831
    • Bae, S.S.1    Kim, Y.J.2    Yang, S.H.3    Lim, J.K.4    Jeon, J.H.5    Lee, H.S.6    Kang, S.G.7    Kim, S.J.8    Lee, J.H.9
  • 29
    • 0035000622 scopus 로고    scopus 로고
    • Diversity among three novel groups of hyperthermophilic deepsea Thermococcus species from three sites in the northeastern Pacific Ocean
    • Holden JF, Takai K, Summit M, Bolton S, Zyskowski J, Baross JA. 2001. Diversity among three novel groups of hyperthermophilic deepsea Thermococcus species from three sites in the northeastern Pacific Ocean. FEMS Microbiol Ecol 36:51-60. http://dx.doi.org/10.1111/j.1574-6941.2001.tb00825.x.
    • (2001) FEMS Microbiol Ecol , vol.36 , pp. 51-60
    • Holden, J.F.1    Takai, K.2    Summit, M.3    Bolton, S.4    Zyskowski, J.5    Baross, J.A.6
  • 30
    • 0017030513 scopus 로고
    • New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere
    • Balch WE, Wolfe RS. 1976. New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere. Appl Environ Microbiol 32:781-791.
    • (1976) Appl Environ Microbiol , vol.32 , pp. 781-791
    • Balch, W.E.1    Wolfe, R.S.2
  • 31
    • 34147158720 scopus 로고    scopus 로고
    • Disruption of a sugar transporter gene cluster in a hyperthermophilic archaeon using a host-marker system based on antibiotic resistance
    • Matsumi R, Manabe K, Fukui T, Atomi H, Imanaka T. 2007. Disruption of a sugar transporter gene cluster in a hyperthermophilic archaeon using a host-marker system based on antibiotic resistance. J Bacteriol 189:2683-2691. http://dx.doi.org/10.1128/JB.01692-06.
    • (2007) J Bacteriol , vol.189 , pp. 2683-2691
    • Matsumi, R.1    Manabe, K.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5
  • 32
    • 0035853296 scopus 로고    scopus 로고
    • Regulatory potential, phyletic distribution and evolution of ancient, intracellular smallmolecule-binding domains
    • Anantharaman V, Koonin EV, Aravind L. 2001. Regulatory potential, phyletic distribution and evolution of ancient, intracellular smallmolecule-binding domains. J Mol Biol 307:1271-1292. http://dx.doi.org/10.1006/jmbi.2001.4508.
    • (2001) J Mol Biol , vol.307 , pp. 1271-1292
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 33
    • 0031945812 scopus 로고    scopus 로고
    • Aromatic ligand binding and intramolecular signalling of the phenol-responsive σ54-dependent regulator DmpR
    • O'Neill E, Ng LC, Sze CC, Shingler V. 1998. Aromatic ligand binding and intramolecular signalling of the phenol-responsive σ54-dependent regulator DmpR. Mol Microbiol 28:131-141.
    • (1998) Mol Microbiol , vol.28 , pp. 131-141
    • O'Neill, E.1    Ng, L.C.2    Sze, C.C.3    Shingler, V.4
  • 34
    • 78049425692 scopus 로고    scopus 로고
    • The methanogen-specific transcription factor MsvR regulates the fpaA-rlp-rub oxidative stress operon adjacent to msvR in Methanothermobacter thermautotrophicus
    • Karr EA. 2010. The methanogen-specific transcription factor MsvR regulates the fpaA-rlp-rub oxidative stress operon adjacent to msvR in Methanothermobacter thermautotrophicus. J Bacteriol 192:5914-5922. http://dx.doi.org/10.1128/JB.00816-10.
    • (2010) J Bacteriol , vol.192 , pp. 5914-5922
    • Karr, E.A.1
  • 35
    • 84880125786 scopus 로고    scopus 로고
    • Redox-sensitive DNA binding by homodimeric Methanosarcina acetivorans MsvR is modulated by cysteine residues
    • Isom CE, Turner JL, Lessner DJ, Karr EA. 2013. Redox-sensitive DNA binding by homodimeric Methanosarcina acetivorans MsvR is modulated by cysteine residues. BMC Microbiol 13:163. http://dx.doi.org/10.1186/1471-2180-13-163.
    • (2013) BMC Microbiol , vol.13 , pp. 163
    • Isom, C.E.1    Turner, J.L.2    Lessner, D.J.3    Karr, E.A.4
  • 36
    • 84874106658 scopus 로고    scopus 로고
    • Performance of a Carboxydothermus hydrogenoformans-immobilizing membrane reactor for syngas upgrading into hydrogen
    • Zhao Y, Haddad M, Cimpoiab R, Liua Z, Guiot SR. 2013. Performance of a Carboxydothermus hydrogenoformans-immobilizing membrane reactor for syngas upgrading into hydrogen. Int J Hydrogen Energy 38:2167-2175. http://dx.doi.org/10.1016/j.ijhydene.2012.11.038.
    • (2013) Int J Hydrogen Energy , vol.38 , pp. 2167-2175
    • Zhao, Y.1    Haddad, M.2    Cimpoiab, R.3    Liua, Z.4    Guiot, S.R.5
  • 37
    • 21644443908 scopus 로고    scopus 로고
    • Biohydrogen production from carbon monoxide and water by Rhodopseudomonas palustris P4
    • Oh Y-K, Kim Y-J, Park J-Y, Lee TH, Kim M-S, Park S. 2005. Biohydrogen production from carbon monoxide and water by Rhodopseudomonas palustris P4. Biotechnol Bioprocess Eng 10:270-274. http://dx.doi.org/10.1007/BF02932024.
    • (2005) Biotechnol Bioprocess Eng , vol.10 , pp. 270-274
    • Oh, Y.-K.1    Kim, Y.-J.2    Park, J.-Y.3    Lee, T.H.4    Kim, M.-S.5    Park, S.6
  • 38
    • 0036604203 scopus 로고    scopus 로고
    • Hydrogen production by a new chemoheterotrophic bacterium Citrobacter sp. Y19
    • Jung GY, Kim JR, Park JY, Park S. 2002. Hydrogen production by a new chemoheterotrophic bacterium Citrobacter sp. Y19. Int J Hydrogen Energy 27:601-610. http://dx.doi.org/10.1016/S0360-3199(01)00176-8.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 601-610
    • Jung, G.Y.1    Kim, J.R.2    Park, J.Y.3    Park, S.4
  • 39
    • 0027246095 scopus 로고
    • Kinetics of light limited growth and biological hydrogen production from carbon monoxide and water by Rhodospirillum rubrum
    • Klasson KT, Lundbäck KMO, Clausen EC, Gaddy JL. 1993. Kinetics of light limited growth and biological hydrogen production from carbon monoxide and water by Rhodospirillum rubrum. J Biotechnol 29:177-188. http://dx.doi.org/10.1016/0168-1656(93)90049-S.
    • (1993) J Biotechnol , vol.29 , pp. 177-188
    • Klasson, K.T.1    Lundbäck, K.M.O.2    Clausen, E.C.3    Gaddy, J.L.4
  • 40
    • 0036237146 scopus 로고    scopus 로고
    • Bioreactor design studies for a hydrogenproducing bacterium
    • Wolfrum EJ, Watt AS. 2002. Bioreactor design studies for a hydrogenproducing bacterium. Appl Biochem Biotechnol 98-100:611-625. http://dx.doi.org/10.1385/ABAB:98-100:1-9:611.
    • (2002) Appl Biochem Biotechnol , vol.98-100 , pp. 611-625
    • Wolfrum, E.J.1    Watt, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.