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Volumn 94, Issue 6, 2014, Pages 1330-1342

Novel proteins for homocysteine biosynthesis in anaerobic microorganisms

Author keywords

[No Author keywords available]

Indexed keywords

HOMOCYSTEINE; SULFIDE; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; SULFUR;

EID: 84914811516     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12832     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 36548999148 scopus 로고
    • Making nucleic acid probes
    • Glover, D.M., and Hames, B.D. (eds). New York.: Oxford University Press
    • Alphey, L., and Parry, H.D. (1995) Making nucleic acid probes. In DNA Cloning 1. Glover, D.M., and Hames, B.D. (eds). New York.: Oxford University Press, pp. 121-123.
    • (1995) DNA Cloning 1 , pp. 121-123
    • Alphey, L.1    Parry, H.D.2
  • 2
    • 20144364162 scopus 로고    scopus 로고
    • Higher-level classification of the Archaea: evolution of methanogenesis and methanogens
    • Bapteste, E., Brochier, C., and Boucher, Y. (2005) Higher-level classification of the Archaea: evolution of methanogenesis and methanogens. Archaea 1: 353-363.
    • (2005) Archaea , vol.1 , pp. 353-363
    • Bapteste, E.1    Brochier, C.2    Boucher, Y.3
  • 3
    • 81555228426 scopus 로고    scopus 로고
    • The CBS domain: a protein module with an emerging prominent role in regulation
    • Baykov, A.A., Tuominen, H.K., and Lahti, R. (2011) The CBS domain: a protein module with an emerging prominent role in regulation. ACS Chem Biol 6: 1156-1163.
    • (2011) ACS Chem Biol , vol.6 , pp. 1156-1163
    • Baykov, A.A.1    Tuominen, H.K.2    Lahti, R.3
  • 4
    • 0031929614 scopus 로고    scopus 로고
    • The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium
    • Beck, B.J., and Downs, D.M. (1998) The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium. J Bacteriol 180: 885-891.
    • (1998) J Bacteriol , vol.180 , pp. 885-891
    • Beck, B.J.1    Downs, D.M.2
  • 5
    • 65249127932 scopus 로고    scopus 로고
    • Phylogenomic dating - the relative antiquity of archaeal metabolic and physiological traits
    • Blank, C.E. (2009) Phylogenomic dating - the relative antiquity of archaeal metabolic and physiological traits. Astrobiology 9: 193-219.
    • (2009) Astrobiology , vol.9 , pp. 193-219
    • Blank, C.E.1
  • 6
    • 84890110026 scopus 로고    scopus 로고
    • Phylogenomic data support a seventh order of Methylotrophic methanogens and provide insights into the evolution of Methanogenesis
    • Borrel, G., O'Toole, P.W., Harris, H.M.B., Peyret, P., Brugère, J.-F., and Gribaldo, S. (2013) Phylogenomic data support a seventh order of Methylotrophic methanogens and provide insights into the evolution of Methanogenesis. Genome Biol Evol 5: 1769-1780.
    • (2013) Genome Biol Evol , vol.5 , pp. 1769-1780
    • Borrel, G.1    O'Toole, P.W.2    Harris, H.M.B.3    Peyret, P.4    Brugère, J.-F.5    Gribaldo, S.6
  • 7
    • 79952613800 scopus 로고    scopus 로고
    • Genetic methods for methanosarcina species
    • Buan, N., Kulkarni, G., and Metcalf, W. (2011) Genetic methods for methanosarcina species. Methods Enzymol 494: 23-42.
    • (2011) Methods Enzymol , vol.494 , pp. 23-42
    • Buan, N.1    Kulkarni, G.2    Metcalf, W.3
  • 8
    • 2342661195 scopus 로고    scopus 로고
    • Detection of lateral gene transfer events in the prokaryotic tRNA synthetases by the ratios of evolutionary distances method
    • Farahi, K., Pusch, G.D., Overbeek, R., and Whitman, W.B. (2004) Detection of lateral gene transfer events in the prokaryotic tRNA synthetases by the ratios of evolutionary distances method. J Mol Evol 58: 615-631.
    • (2004) J Mol Evol , vol.58 , pp. 615-631
    • Farahi, K.1    Pusch, G.D.2    Overbeek, R.3    Whitman, W.B.4
  • 9
    • 0036225678 scopus 로고    scopus 로고
    • The genome of M. acetivorans reveals extensive metabolic and physiological diversity
    • Galagan, J.E., Nusbaum, C., Roy, A., Endrizzi, M.G., Macdonald, P., FitzHugh, W., etal. (2002) The genome of M. 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.6
  • 10
    • 57449120302 scopus 로고    scopus 로고
    • New methods for tightly regulated gene expression and highly efficient chromosomal integration of cloned genes for Methanosarcina species
    • Guss, A.M., Rother, M., Zhang, J.K., Kulkarni, G., and Metcalf, W.W. (2008) New methods for tightly regulated gene expression and highly efficient chromosomal integration of cloned genes for Methanosarcina species. Archaea 2: 193-203.
    • (2008) Archaea , vol.2 , pp. 193-203
    • Guss, A.M.1    Rother, M.2    Zhang, J.K.3    Kulkarni, G.4    Metcalf, W.W.5
  • 11
    • 0037147193 scopus 로고    scopus 로고
    • Calibration of sulfate levels in the archean ocean
    • Habicht, K.S., Gade, M., Thamdrup, B., Berg, P., and Canfield, D.E. (2002) Calibration of sulfate levels in the archean ocean. Science 298: 2372-2374.
    • (2002) Science , vol.298 , pp. 2372-2374
    • Habicht, K.S.1    Gade, M.2    Thamdrup, B.3    Berg, P.4    Canfield, D.E.5
  • 12
    • 52049114456 scopus 로고    scopus 로고
    • Redundant synthesis of cysteinyl-tRNACys in Methanosarcina mazei
    • Hauenstein, S.I., and Perona, J.J. (2008) Redundant synthesis of cysteinyl-tRNACys in Methanosarcina mazei. J Biol Chem 283: 22007-22017.
    • (2008) J Biol Chem , vol.283 , pp. 22007-22017
    • Hauenstein, S.I.1    Perona, J.J.2
  • 13
    • 84655163520 scopus 로고    scopus 로고
    • Mutational analysis of Sep-tRNA:Cys-tRNA synthase reveals critical residues for tRNA-dependent cysteine formation
    • Helgadóttir, S., Sinapah, S., Söll, D., and Ling, J. (2012) Mutational analysis of Sep-tRNA:Cys-tRNA synthase reveals critical residues for tRNA-dependent cysteine formation. FEBS Lett 586: 60-63.
    • (2012) FEBS Lett , vol.586 , pp. 60-63
    • Helgadóttir, S.1    Sinapah, S.2    Söll, D.3    Ling, J.4
  • 14
    • 79959190407 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors
    • Hidese, R., Mihara, H., and Esaki, N. (2011) Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors. Appl Microbiol Biotechnol 91: 47-61.
    • (2011) Appl Microbiol Biotechnol , vol.91 , pp. 47-61
    • Hidese, R.1    Mihara, H.2    Esaki, N.3
  • 15
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation
    • Kadaba, N.S., Kaiser, J.T., Johnson, E., Lee, A., and Rees, D.C. (2008) The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321: 250-253.
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 16
    • 84874110350 scopus 로고    scopus 로고
    • Genetic manipulation of Methanosarcina spp.
    • Kohler, P.R.A., and Metcalf, W.W. (2012) Genetic manipulation of Methanosarcina spp. Front Microbiol 3: 259.
    • (2012) Front Microbiol , vol.3 , pp. 259
    • Kohler, P.R.A.1    Metcalf, W.W.2
  • 17
    • 0018224280 scopus 로고
    • Trans-complementation-dependent replication of a low molecular weight origin fragment from plasmid R6K
    • Kolter, R., Inuzuka, M., and Helinski, D.R. (1978) Trans-complementation-dependent replication of a low molecular weight origin fragment from plasmid R6K. Cell 15: 1199-1208.
    • (1978) Cell , vol.15 , pp. 1199-1208
    • Kolter, R.1    Inuzuka, M.2    Helinski, D.R.3
  • 18
    • 77957809203 scopus 로고    scopus 로고
    • Cysteine is not the sulfur source for iron-sulfur cluster and methionine biosynthesis in the methanogenic archaeon Methanococcus maripaludis
    • Liu, Y., Sieprawska-Lupa, M., Whitman, W.B., and White, R.H. (2010) Cysteine is not the sulfur source for iron-sulfur cluster and methionine biosynthesis in the methanogenic archaeon Methanococcus maripaludis. J Biol Chem 285: 31923-31929.
    • (2010) J Biol Chem , vol.285 , pp. 31923-31929
    • Liu, Y.1    Sieprawska-Lupa, M.2    Whitman, W.B.3    White, R.H.4
  • 19
    • 84862815590 scopus 로고    scopus 로고
    • Methanogens: a window into ancient sulfur metabolism
    • Liu, Y., Beer, L.L., and Whitman, W.B. (2012a) Methanogens: a window into ancient sulfur metabolism. Trends Microbiol 20: 251-258.
    • (2012) Trends Microbiol , vol.20 , pp. 251-258
    • Liu, Y.1    Beer, L.L.2    Whitman, W.B.3
  • 20
    • 84863116891 scopus 로고    scopus 로고
    • Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide
    • Liu, Y., Dos Santos, P.C., Zhu, X., Orlando, R., Dean, D.R., Söll, D., and Yuan, J. (2012b) Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide. J Biol Chem 287: 5426-5433.
    • (2012) J Biol Chem , vol.287 , pp. 5426-5433
    • Liu, Y.1    Dos Santos, P.C.2    Zhu, X.3    Orlando, R.4    Dean, D.R.5    Söll, D.6    Yuan, J.7
  • 21
    • 84868233239 scopus 로고    scopus 로고
    • Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis
    • Liu, Y., Zhu, X., Nakamura, A., Orlando, R., Söll, D., and Whitman, W.B. (2012c) Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis. J Biol Chem 287: 36683-36692.
    • (2012) J Biol Chem , vol.287 , pp. 36683-36692
    • Liu, Y.1    Zhu, X.2    Nakamura, A.3    Orlando, R.4    Söll, D.5    Whitman, W.B.6
  • 22
    • 84896077979 scopus 로고    scopus 로고
    • The putative tRNA 2-thiouridine synthetase Ncs6 is an essential sulfur carrier in Methanococcus maripaludis
    • Liu, Y., Long, F., Wang, L., Söll, D., and Whitman, W.B. (2014) The putative tRNA 2-thiouridine synthetase Ncs6 is an essential sulfur carrier in Methanococcus maripaludis. FEBS Lett 588: 873-877.
    • (2014) FEBS Lett , vol.588 , pp. 873-877
    • Liu, Y.1    Long, F.2    Wang, L.3    Söll, D.4    Whitman, W.B.5
  • 23
    • 77949314227 scopus 로고    scopus 로고
    • Binding of S-methyl-5′-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair
    • Lucas, M., Encinar, J.A., Arribas, E.A., Oyenarte, I., García, I.G., Kortazar, D., etal. (2010) Binding of S-methyl-5′-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair. J Mol Biol 396: 800-820.
    • (2010) J Mol Biol , vol.396 , pp. 800-820
    • Lucas, M.1    Encinar, J.A.2    Arribas, E.A.3    Oyenarte, I.4    García, I.G.5    Kortazar, D.6
  • 24
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: protein domain annotations on the fly
    • Marchler-Bauer, A., and Bryant, S.H. (2004) CD-Search: protein domain annotations on the fly. Nucleic Acids Res 32: W327-W331.
    • (2004) Nucleic Acids Res , vol.32 , pp. W327-W331
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 26
    • 0029796392 scopus 로고    scopus 로고
    • Molecular, genetic, and biochemical characterization of the serC gene of Methanosarcina barkeri Fusaro
    • Metcalf, W.W., Zhang, J.K., Shi, X., and Wolfe, R.S. (1996) Molecular, genetic, and biochemical characterization of the serC gene of Methanosarcina barkeri Fusaro. J Bacteriol 178: 5797-5802.
    • (1996) J Bacteriol , vol.178 , pp. 5797-5802
    • Metcalf, W.W.1    Zhang, J.K.2    Shi, X.3    Wolfe, R.S.4
  • 27
    • 0015837485 scopus 로고
    • Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. VII. Properties of homoserine O-transacetylase
    • Miyajima, R., and Shiio, I. (1973) Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. VII. Properties of homoserine O-transacetylase. J Biochem (Tokyo) 73: 1061-1068.
    • (1973) J Biochem (Tokyo) , vol.73 , pp. 1061-1068
    • Miyajima, R.1    Shiio, I.2
  • 28
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: delivering sulfur in biosynthetic pathways
    • Mueller, E.G. (2006) Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2: 185-194.
    • (2006) Nat Chem Biol , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 30
    • 84875551750 scopus 로고    scopus 로고
    • MGcV: the microbial genomic context viewer for comparative genome analysis
    • Overmars, L., Kerkhoven, R., Siezen, R.J., and Francke, C. (2013) MGcV: the microbial genomic context viewer for comparative genome analysis. BMC Genomics 14: 209.
    • (2013) BMC Genomics , vol.14 , pp. 209
    • Overmars, L.1    Kerkhoven, R.2    Siezen, R.J.3    Francke, C.4
  • 31
    • 0008544314 scopus 로고
    • The utilization of cloned DNAs to study gene organization and expression
    • Glover, D.M., and Hames, B.D. (eds). New York.: Oxford University Press
    • Parry, H.D., and Alphey, L. (1995) The utilization of cloned DNAs to study gene organization and expression. In DNA Cloning 1. Glover, D.M., and Hames, B.D. (eds). New York.: Oxford University Press, pp. 143-158.
    • (1995) DNA Cloning 1 , pp. 143-158
    • Parry, H.D.1    Alphey, L.2
  • 32
    • 84875251958 scopus 로고    scopus 로고
    • Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis
    • Sarmiento, F., Mrázek, J., and Whitman, W.B. (2013) Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis. Proc Natl Acad Sci USA 110: 4726-4731.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 4726-4731
    • Sarmiento, F.1    Mrázek, J.2    Whitman, W.B.3
  • 34
    • 0033995794 scopus 로고    scopus 로고
    • Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction
    • Sekowska, A., Kung, H.F., and Danchin, A. (2000) Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction. J Mol Microbiol Biotechnol 2: 145-177.
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 145-177
    • Sekowska, A.1    Kung, H.F.2    Danchin, A.3
  • 35
    • 0037216551 scopus 로고    scopus 로고
    • Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium
    • Skovran, E., and Downs, D.M. (2003) Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster metabolism in Salmonella enterica serovar Typhimurium. J Bacteriol 185: 98-106.
    • (2003) J Bacteriol , vol.185 , pp. 98-106
    • Skovran, E.1    Downs, D.M.2
  • 36
    • 0027504911 scopus 로고
    • Disaggregation of Methanosarcina spp. and growth as single cells at elevated osmolarity
    • Sowers, K.R., Boone, J.E., and Gunsalus, R.P. (1993) Disaggregation of Methanosarcina spp. and growth as single cells at elevated osmolarity. Appl Environ Microbiol 59: 3832-3839.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3832-3839
    • Sowers, K.R.1    Boone, J.E.2    Gunsalus, R.P.3
  • 37
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov, R.L., Koonin, E.V., and Lipman, D.J. (1997) A genomic perspective on protein families. Science 278: 631-637.
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 38
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture
    • Thauer, R.K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture. Microbiology 144 (Part 9): 2377-2406.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 39
    • 0345258439 scopus 로고    scopus 로고
    • The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii
    • White, R.H. (2003) The biosynthesis of cysteine and homocysteine in Methanococcus jannaschii. Biochim Biophys Acta 1624: 46-53.
    • (2003) Biochim Biophys Acta , vol.1624 , pp. 46-53
    • White, R.H.1
  • 40
    • 77953707932 scopus 로고    scopus 로고
    • A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli
    • Yuan, J., Hohn, M.J., Sherrer, R.L., Palioura, S., Su, D., and Söll, D. (2010) A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli. FEBS Lett 584: 2857-2861.
    • (2010) FEBS Lett , vol.584 , pp. 2857-2861
    • Yuan, J.1    Hohn, M.J.2    Sherrer, R.L.3    Palioura, S.4    Su, D.5    Söll, D.6


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