메뉴 건너뛰기




Volumn 9, Issue 2, 2010, Pages 640-652

Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii part I: The effect of growth temperature

Author keywords

Cell envelope; iTRAQ; LC LC MS MS; Membrane proteinarchaea; Methanogen; Nucleic acid binding; Oxidative stress; Proteome; Psychrophilemethylotroph; S layer; Transcriptional regulator; Translation

Indexed keywords

CARRIER PROTEIN; CELL CYCLE PROTEIN; CELL PROTEIN; CELL SURFACE PROTEIN; MEMBRANE PROTEIN; METHANOL; NUCLEIC ACID BINDING PROTEIN; PROTEOME; TRIMETHYLAMINE;

EID: 76149124222     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900509n     Document Type: Article
Times cited : (39)

References (77)
  • 2
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G.; Gerday, C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 2003, 1, 200-208.
    • (2003) Nat. Rev. Microbiol , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 3
  • 8
    • 0002364934 scopus 로고    scopus 로고
    • The chemical stratification and microbial communities of Ace Lake, Antarctica: A review of the characteristics of a marine-derived meromictic lake
    • Rankin, L. M.; Gibson, J. A. E.; Franzmann, P. D.; Burton, H. R. The chemical stratification and microbial communities of Ace Lake, Antarctica: a review of the characteristics of a marine-derived meromictic lake. Polarforschung 1999, 66, 33-52.
    • (1999) Polarforschung , vol.66 , pp. 33-52
    • Rankin, L.M.1    Gibson, J.A.E.2    Franzmann, P.D.3    Burton, H.R.4
  • 9
    • 70349456541 scopus 로고    scopus 로고
    • Allen, M. A.; Lauro, F. M.; Williams, T. J.; Burg, D,; Siddiqui, K. S.; De Franciscii, D.; Chong, K. W. Y.; Pilak, O.; Chew, H. H.; De Maere, M. Z.; Ting, L.; Katrib, M.; Ng, C.; Sowers, K. R.; Galeprin, M. Y.; Anderson, I. J.; Ivanova, N.; Dalin, E.; Martinez, M.; Lapidus, A.; Hauser, L.; Land, M.; Thomas, T.; Cavicchioli, R. The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold-adaptation. ISME J. 2009, 3, 1012-1035.
    • Allen, M. A.; Lauro, F. M.; Williams, T. J.; Burg, D,; Siddiqui, K. S.; De Franciscii, D.; Chong, K. W. Y.; Pilak, O.; Chew, H. H.; De Maere, M. Z.; Ting, L.; Katrib, M.; Ng, C.; Sowers, K. R.; Galeprin, M. Y.; Anderson, I. J.; Ivanova, N.; Dalin, E.; Martinez, M.; Lapidus, A.; Hauser, L.; Land, M.; Thomas, T.; Cavicchioli, R. The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold-adaptation. ISME J. 2009, 3, 1012-1035.
  • 10
    • 10044245551 scopus 로고    scopus 로고
    • Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry
    • Goodchild, A.; Raftery, M.; Saunders, N. F. W.; Guilhaus, M.; Cavicchioli, R. Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry. J. Proteome Res. 2004, 3, 1164-1176.
    • (2004) J. Proteome Res , vol.3 , pp. 1164-1176
    • Goodchild, A.1    Raftery, M.2    Saunders, N.F.W.3    Guilhaus, M.4    Cavicchioli, R.5
  • 12
    • 17444384908 scopus 로고    scopus 로고
    • Cold adaptation of the Antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT
    • Goodchild, A.; Raftery, M.; Saunders, N. F. W.; Guilhaus, M.; Cavicchioli, R. Cold adaptation of the Antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT. J. Proteome. Res. 2005, 4, 473-480.
    • (2005) J. Proteome. Res , vol.4 , pp. 473-480
    • Goodchild, A.1    Raftery, M.2    Saunders, N.F.W.3    Guilhaus, M.4    Cavicchioli, R.5
  • 13
    • 33748333118 scopus 로고    scopus 로고
    • Proteomic and computational analysis of secreted proteins with type I signal peptides from the Antarctic archaeon Methanococcoides burtonii
    • Saunders, N. F. W.; Ng, C.; Raftery, M.; Guilhaus, M.; Goodchild, A.; Cavicchioli, R. Proteomic and computational analysis of secreted proteins with type I signal peptides from the Antarctic archaeon Methanococcoides burtonii. J. Proteome Res. 2006, 5, 2457-2464.
    • (2006) J. Proteome Res , vol.5 , pp. 2457-2464
    • Saunders, N.F.W.1    Ng, C.2    Raftery, M.3    Guilhaus, M.4    Goodchild, A.5    Cavicchioli, R.6
  • 16
    • 0002156909 scopus 로고
    • Methanogenic Archaea: An overview
    • Robb, F. T, Place, A. R, Sowers, K. R, Schreier, H. J, DasSarma, S, Fleischmann, E. M, Eds, Cold Spring Harbor Laboratory Press: Plainview
    • Sowers, K. R. Methanogenic Archaea: an overview. In: Archaea. A Laboratory Manual; Robb, F. T., Place, A. R., Sowers, K. R., Schreier, H. J., DasSarma, S., Fleischmann, E. M., Eds.; Cold Spring Harbor Laboratory Press: Plainview, 1995; pp 3-13.
    • (1995) Archaea. A Laboratory Manual , pp. 3-13
    • Sowers, K.R.1
  • 17
    • 0036665518 scopus 로고    scopus 로고
    • Enrichment of integral membrane proteins for proteomic analysis using liquid chromatographytandem mass spectrometry
    • Blonder, J.; Goshe, M. B.; Moore, R. J.; Pasa-Tolic, L.; Masselon, C. D.; Lipton, M. S.; Smith, R. D. Enrichment of integral membrane proteins for proteomic analysis using liquid chromatographytandem mass spectrometry. J. Proteome Res. 2002, 1, 351-360.
    • (2002) J. Proteome Res , vol.1 , pp. 351-360
    • Blonder, J.1    Goshe, M.B.2    Moore, R.J.3    Pasa-Tolic, L.4    Masselon, C.D.5    Lipton, M.S.6    Smith, R.D.7
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding
    • Bradford, M. M. (1976). A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.1976 , Issue.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 66749192040 scopus 로고    scopus 로고
    • Global protein-level responses of Halobacterium salinarum NRC-1 to prolonged changes in external sodium chloride concentrations
    • Leuko, S.; Raftery, M.; Burns, B.; Walter, M.; Neilan, B. Global protein-level responses of Halobacterium salinarum NRC-1 to prolonged changes in external sodium chloride concentrations. J. Proteome Res. 2009, 8, 2218-2225.
    • (2009) J. Proteome Res , vol.8 , pp. 2218-2225
    • Leuko, S.1    Raftery, M.2    Burns, B.3    Walter, M.4    Neilan, B.5
  • 20
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Kall, L.; Storey, J. D.; MacCoss, M. J.; Noble, W. S. Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J. Proteome Res. 2008, 7, 29-34.
    • (2008) J. Proteome Res , vol.7 , pp. 29-34
    • Kall, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 21
    • 34748882621 scopus 로고    scopus 로고
    • Proteomic analysis of rabbit tear fluid: Defensin levels after an experimental corneal wound are correlated to wound closure
    • Zhou, L.; Beuerman, R. W.; Huang, L.; Barathi, A.; Foo, Y. H.; Li, S. F. Y.; Chew, F. T.; Tan, D. Proteomic analysis of rabbit tear fluid: Defensin levels after an experimental corneal wound are correlated to wound closure. Proteomics 2007, 7, 3194-3206.
    • (2007) Proteomics , vol.7 , pp. 3194-3206
    • Zhou, L.1    Beuerman, R.W.2    Huang, L.3    Barathi, A.4    Foo, Y.H.5    Li, S.F.Y.6    Chew, F.T.7    Tan, D.8
  • 22
    • 17444376059 scopus 로고    scopus 로고
    • Predicted roles for Hypothetical proteins in the low-temperature expressed proteome of the Antarctic archaeon Methanococcoides burtonii
    • Saunders, N. F. W.; Goodchild, A.; Raftery, M.; Guilhaus, M.; Curmi, P. M.; Cavicchioli, R. Predicted roles for Hypothetical proteins in the low-temperature expressed proteome of the Antarctic archaeon Methanococcoides burtonii. J. Proteome Res. 2005, 4, 464-472.
    • (2005) J. Proteome Res , vol.4 , pp. 464-472
    • Saunders, N.F.W.1    Goodchild, A.2    Raftery, M.3    Guilhaus, M.4    Curmi, P.M.5    Cavicchioli, R.6
  • 23
    • 0036774262 scopus 로고    scopus 로고
    • Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins
    • Jing, H.; Takagi, J.; Liu, J. H.; Lindgren, S.; Zhang, R. G.; Joachimiak, A.; Wang, J. H.; Springer, T. A. Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins. Structure 2002, 10, 1453-41464.
    • (2002) Structure , vol.10 , pp. 1453-41464
    • Jing, H.1    Takagi, J.2    Liu, J.H.3    Lindgren, S.4    Zhang, R.G.5    Joachimiak, A.6    Wang, J.H.7    Springer, T.A.8
  • 24
    • 35148889967 scopus 로고    scopus 로고
    • Proteinaceous surface layers of Archaea: Ultrastructure and biochemistry
    • Cavicchioli, R, Ed, ASM Press: Washington, DC
    • König, H.; Rachel, R.; Claus, H. Proteinaceous surface layers of Archaea: ultrastructure and biochemistry. In: Cavicchioli, R. (Ed.) Archaea. Molecular and Cellular Biology; ASM Press: Washington, DC, 2007; pp 315-340.
    • (2007) Archaea. Molecular and Cellular Biology , pp. 315-340
    • König, H.1    Rachel, R.2    Claus, H.3
  • 26
    • 11144251737 scopus 로고    scopus 로고
    • Cold shock of a hyperthermophilic archaeon: Pyrococcus furiosus exhibits multiple responses to a suboptimal growth temperature with a key role for membrane-bound glycoproteins
    • Weinberg, M. V.; Schut, G. J.; Brehm, S.; Datta, S.; Adams, M. W. Cold shock of a hyperthermophilic archaeon: Pyrococcus furiosus exhibits multiple responses to a suboptimal growth temperature with a key role for membrane-bound glycoproteins. J. Bacteriol. 2005, 187, 336-348.
    • (2005) J. Bacteriol , vol.187 , pp. 336-348
    • Weinberg, M.V.1    Schut, G.J.2    Brehm, S.3    Datta, S.4    Adams, M.W.5
  • 27
    • 0025325167 scopus 로고
    • Cadherins: A molecular family important in selective cell-cell adhesion
    • Takeichi, M. Cadherins: a molecular family important in selective cell-cell adhesion. Annu. Rev. Biochem. 1990, 59, 237-252.
    • (1990) Annu. Rev. Biochem , vol.59 , pp. 237-252
    • Takeichi, M.1
  • 29
    • 58149277107 scopus 로고    scopus 로고
    • Noncellulosomal cohesin- and dockerin-like modules in the three domains of life
    • Peer, A.; Smith, S. P.; Bayer, E. A.; Lamed, R.; Borovok, I. Noncellulosomal cohesin- and dockerin-like modules in the three domains of life. FEMS Microbiol. Lett. 2008, 291, 1-16.
    • (2008) FEMS Microbiol. Lett , vol.291 , pp. 1-16
    • Peer, A.1    Smith, S.P.2    Bayer, E.A.3    Lamed, R.4    Borovok, I.5
  • 30
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • Shoham, Y.; Lamed, R.; Bayer, E. A. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends. Microbiol. 1999, 7, 275-281.
    • (1999) Trends. Microbiol , vol.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 31
    • 0036225678 scopus 로고    scopus 로고
    • Galagan, J. E, Nusbaum, C, Roy, A, Endrizzi, M. G, Macdonald, P, FitzHugh, W, Calvo, S, Engels, R, Smirnov, S, Atnoor, D, Brown, A, Allen, N, Naylor, J, Stange-Thomann, N, DeArellano, K, Johnson, R, Linton, L, McEwan, P, McKernan, K, Talamas, J, Tirrell, A, Ye, W, Zimmer, A, Barber, R. D, Cann, I, Graham, D. E, Grahame, D. A, Guss, A. M, Hedderich, R, Ingram-Smith, C, Kuettner, H. C, Krzycki, J. A, Leigh, J. A, Li, W, Liu, J, Mukhopadhyay, B, Reeve, J. N, Smith, K, Springer, T. A, Umayam, L. A, White, O, White, R. H, de Macario, E. C, Ferry, J. G, Jarrell, K. F, Jing, H, Macario, A. J, Paulsen, I, Pritchett, M, Sowers, K. R, Swanson, R. V, Zinder, S. H, Lander, E, Metcalf, W. W, Birren, B. The genome of M. acetivorans reveals extensive metabolic and physiological diversity. Genome Res. 2002, 12, 532-542
    • Galagan, J. E.; Nusbaum, C.; Roy, A.; Endrizzi, M. G.; Macdonald, P.; FitzHugh, W.; Calvo, S.; Engels, R.; Smirnov, S.; Atnoor, D.; Brown, A.; Allen, N.; Naylor, J.; Stange-Thomann, N.; DeArellano, K.; Johnson, R.; Linton, L.; McEwan, P.; McKernan, K.; Talamas, J.; Tirrell, A.; Ye, W.; Zimmer, A.; Barber, R. D.; Cann, I.; Graham, D. E.; Grahame, D. A.; Guss, A. M.; Hedderich, R.; Ingram-Smith, C.; Kuettner, H. C.; Krzycki, J. A.; Leigh, J. A.; Li, W.; Liu, J.; Mukhopadhyay, B.; Reeve, J. N.; Smith, K.; Springer, T. A.; Umayam, L. A.; White, O.; White, R. H.; de Macario, E. C.; Ferry, J. G.; Jarrell, K. F.; Jing, H.; Macario, A. J.; Paulsen, I.; Pritchett, M.; Sowers, K. R.; Swanson, R. V.; Zinder, S. H.; Lander, E.; Metcalf, W. W.; Birren, B. The genome of M. acetivorans reveals extensive metabolic and physiological diversity. Genome Res. 2002, 12, 532-542.
  • 32
    • 10044290651 scopus 로고    scopus 로고
    • Cold adaptation in the Antarctic archaeon Methanococcoides burtonii involves membrane lipid unsaturation
    • Nichols, D. S.; Miller, M. R.; Davies, N. W.; Goodchild, A.; Raftery, M.; Cavicchioli, R. Cold adaptation in the Antarctic archaeon Methanococcoides burtonii involves membrane lipid unsaturation. J. Bacteriol. 2004, 186, 8508-8515.
    • (2004) J. Bacteriol , vol.186 , pp. 8508-8515
    • Nichols, D.S.1    Miller, M.R.2    Davies, N.W.3    Goodchild, A.4    Raftery, M.5    Cavicchioli, R.6
  • 33
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F.; Aravind, L.; Spouge, J. L.; Koonin, E. V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 1999, 9, 27-43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 34
    • 0028808179 scopus 로고    scopus 로고
    • + as compatible solutes for osmotic adaptation. Appl. Environ. Microbiol. 1995, 61, 4382-4388.
    • + as compatible solutes for osmotic adaptation. Appl. Environ. Microbiol. 1995, 61, 4382-4388.
  • 35
    • 0035108129 scopus 로고    scopus 로고
    • Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
    • Thomas, T.; Kumar, N.; Cavicchioli, R. Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens. J. Bacteriol. 2001, 183, 1974-1982.
    • (2001) J. Bacteriol , vol.183 , pp. 1974-1982
    • Thomas, T.1    Kumar, N.2    Cavicchioli, R.3
  • 36
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker, J.; Maddox, P.; Salmon, E. D.; Erickson, H. P. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 3171-3175.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 37
    • 55949101226 scopus 로고    scopus 로고
    • DNA binding proteins and chromatin
    • Cavicchioli, R, Ed, ASM Press: Washington, DC
    • Samson, R. Y.; Reeve, J. N. DNA binding proteins and chromatin. In Archaea. Molecular and Cellular Biology; Cavicchioli, R., Ed.; ASM Press: Washington, DC, 2007; pp 110-119.
    • (2007) Archaea. Molecular and Cellular Biology , pp. 110-119
    • Samson, R.Y.1    Reeve, J.N.2
  • 38
    • 0024283673 scopus 로고
    • Characterization of the chromosomal protein MC1 from the thermophilic archaebacterium Methanosarcina sp. CHTI 55 and its effect on the thermal stability of DNA
    • Chartier, F.; Laine, B.; Sautiere, P. Characterization of the chromosomal protein MC1 from the thermophilic archaebacterium Methanosarcina sp. CHTI 55 and its effect on the thermal stability of DNA. Biochim. Biophys. Acta 1988, 951, 149-156. (1988).
    • (1988) Biochim. Biophys. Acta , vol.1988 , Issue.951 , pp. 149-156
    • Chartier, F.1    Laine, B.2    Sautiere, P.3
  • 40
    • 0038824870 scopus 로고    scopus 로고
    • Saunders, N. F. W.; Thomas, T.; Curmi, P. M.; Mattick, J. S.; Kuczek, E.; Slade, R.; Davis, J.; Franzmann, P. D.; Boone, D.; Rusterholtz, K.; Feldman, R.; Gates, C.; Bench, S.; Sowers, K.; Kadner, K.; Aerts, A.; Dehal, P.; Detter, C.; Glavina, T.; Lucas, S.; Richardson, P.; Larimer, F.; Hauser, L.; Land, M.; Cavicchioli, R. Mechanisms of thermal adaptation revealed from the genomes of the Antarctic archaea Methanogenium frigidum and Methanococcoides burtonii. Genome Res. 2003, 13, 1580-1588.
    • Saunders, N. F. W.; Thomas, T.; Curmi, P. M.; Mattick, J. S.; Kuczek, E.; Slade, R.; Davis, J.; Franzmann, P. D.; Boone, D.; Rusterholtz, K.; Feldman, R.; Gates, C.; Bench, S.; Sowers, K.; Kadner, K.; Aerts, A.; Dehal, P.; Detter, C.; Glavina, T.; Lucas, S.; Richardson, P.; Larimer, F.; Hauser, L.; Land, M.; Cavicchioli, R. Mechanisms of thermal adaptation revealed from the genomes of the Antarctic archaea Methanogenium frigidum and Methanococcoides burtonii. Genome Res. 2003, 13, 1580-1588.
  • 41
    • 0034737312 scopus 로고    scopus 로고
    • Low temperature regulated DEAD-box RNA helicase from the Antarctic archaeon, Methanococcoides burtonii
    • Lim, J.; Thomas, T.; Cavicchioli, R. Low temperature regulated DEAD-box RNA helicase from the Antarctic archaeon, Methanococcoides burtonii. J. Mol. Biol. 2000, 297, 553-567.
    • (2000) J. Mol. Biol , vol.297 , pp. 553-567
    • Lim, J.1    Thomas, T.2    Cavicchioli, R.3
  • 42
    • 0030043216 scopus 로고    scopus 로고
    • Cold-shock induces a major ribosomal associated protein that unwinds double stranded RNA in Escherichia coli
    • Jones, P. G.; Mitta, M.; Kim, Y.; Jiang, W.; Inouye, M. Cold-shock induces a major ribosomal associated protein that unwinds double stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 76-80.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 76-80
    • Jones, P.G.1    Mitta, M.2    Kim, Y.3    Jiang, W.4    Inouye, M.5
  • 43
    • 9644284618 scopus 로고    scopus 로고
    • Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: Evidence for a 'cold shock degradosome'
    • Prud'homme-Généreux, A.; Beran, R. K.; Iost, I.; Ramey, C. S.; Mackie, G. A.; Simons, R. W. Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'. Mol. Microbiol. 2004, 54, 1409-1421.
    • (2004) Mol. Microbiol , vol.54 , pp. 1409-1421
    • Prud'homme-Généreux, A.1    Beran, R.K.2    Iost, I.3    Ramey, C.S.4    Mackie, G.A.5    Simons, R.W.6
  • 44
    • 0345689403 scopus 로고    scopus 로고
    • Polar-biased localization of the cold stress-induced RNA helicase, CrhC, in the cyanobacterium Anabaena sp. strain PCC 7120
    • El-Fahmawi, B.; Owttrim, G. W. Polar-biased localization of the cold stress-induced RNA helicase, CrhC, in the cyanobacterium Anabaena sp. strain PCC 7120. Mol. Microbiol. 2003, 50, 1439-1448.
    • (2003) Mol. Microbiol , vol.50 , pp. 1439-1448
    • El-Fahmawi, B.1    Owttrim, G.W.2
  • 46
    • 0035853480 scopus 로고    scopus 로고
    • Anantharaman, V.; Koonin, E. V.; Aravind, L. TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes. FEMS Microbiol. Lett. 2001, 197, 215-221.
    • Anantharaman, V.; Koonin, E. V.; Aravind, L. TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes. FEMS Microbiol. Lett. 2001, 197, 215-221.
  • 47
    • 0028363836 scopus 로고
    • The cold-shock response - a hot topic
    • Jones, P. G.; Inouye, M. The cold-shock response - a hot topic. Mol. Microbiol. 1994, 11, 811-818.
    • (1994) Mol. Microbiol , vol.11 , pp. 811-818
    • Jones, P.G.1    Inouye, M.2
  • 48
    • 0031973901 scopus 로고    scopus 로고
    • The CspA family in Escherichia coli: Multiple gene duplication for stress adaptation
    • Yamanaka, K.; Fang, L.; Inouye, M. The CspA family in Escherichia coli: multiple gene duplication for stress adaptation. Mol. Microbiol. 1998, 27, 247-255.
    • (1998) Mol. Microbiol , vol.27 , pp. 247-255
    • Yamanaka, K.1    Fang, L.2    Inouye, M.3
  • 49
  • 50
    • 17844361922 scopus 로고    scopus 로고
    • Ribonucleases J1 and J2: Two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E
    • Even, S.; Pellegrini, O.; Zig, L.; Labas, V.; Vinh, J.; Bréchemmier-Baey, D.; Putzer, H. Ribonucleases J1 and J2: two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E. Nucleic Acids Res. 2005, 33, 2141-2152.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2141-2152
    • Even, S.1    Pellegrini, O.2    Zig, L.3    Labas, V.4    Vinh, J.5    Bréchemmier-Baey, D.6    Putzer, H.7
  • 51
    • 59749105974 scopus 로고    scopus 로고
    • RecA family proteins in archaea: RadA and its cousins
    • Haldenby, S.; White, M. F.; Allers, T. RecA family proteins in archaea: RadA and its cousins. Biochem. Soc. Trans. 2009, 37, 102-107.
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 102-107
    • Haldenby, S.1    White, M.F.2    Allers, T.3
  • 52
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan, G. L.; Pfander, B.; Jentsch, S. PCNA, the maestro of the replication fork. Cell 2007, 129, 665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 53
    • 33645988522 scopus 로고    scopus 로고
    • Conserved XPB core structure and motifs for DNA unwinding: Implications for pathway selection of transcription or excision repair
    • Fan, L.; Arvai, A. S.; Cooper, P. K.; Iwai, S.; Hanaoka, F.; Tainer, J. A. Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair. Mol. Cell 2006, 22, 27-37.
    • (2006) Mol. Cell , vol.22 , pp. 27-37
    • Fan, L.1    Arvai, A.S.2    Cooper, P.K.3    Iwai, S.4    Hanaoka, F.5    Tainer, J.A.6
  • 55
    • 0025169144 scopus 로고
    • Reaction of thiyl radicals with alcohols, ethers and polyunsaturated fatty acids: A possible role of thiyl free radicals in thiol mutagenesis
    • Schöneich, C.; Asmus, K. D. Reaction of thiyl radicals with alcohols, ethers and polyunsaturated fatty acids: a possible role of thiyl free radicals in thiol mutagenesis. Radiat. Environ. Biophys. 1990, 29, 263-271.
    • (1990) Radiat. Environ. Biophys , vol.29 , pp. 263-271
    • Schöneich, C.1    Asmus, K.D.2
  • 56
    • 47049096866 scopus 로고    scopus 로고
    • Mechanisms of protein damage induced by cysteine thiyl radical formation
    • Schöneich, C. Mechanisms of protein damage induced by cysteine thiyl radical formation. Chem. Res. Toxicol. 2008, 21, 1175-1179.
    • (2008) Chem. Res. Toxicol , vol.21 , pp. 1175-1179
    • Schöneich, C.1
  • 57
    • 18644362920 scopus 로고    scopus 로고
    • Thiyl radicals in biosystems: Effects on lipid structures and metabolisms
    • Ferreri, C.; Kratzsch, S.; Landi, L.; Brede, O. Thiyl radicals in biosystems: effects on lipid structures and metabolisms. Cell. Mol. Life Sci. 2006, 62, 834-847.
    • (2006) Cell. Mol. Life Sci , vol.62 , pp. 834-847
    • Ferreri, C.1    Kratzsch, S.2    Landi, L.3    Brede, O.4
  • 58
    • 33847635732 scopus 로고    scopus 로고
    • S-adenosylmethionine as an oxidant: The radical SAM superfamily
    • Wang, S. C.; Frey, P. A. S-adenosylmethionine as an oxidant: the radical SAM superfamily. Trends Biochem. Sci. 2007, 32, 101-110.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 101-110
    • Wang, S.C.1    Frey, P.A.2
  • 59
    • 0037432317 scopus 로고    scopus 로고
    • Control of adenosylmethionine-dependent radical generation in biotin synthase: A kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB
    • Ugulava, N. B.; Frederick, K. K.; Jarrett, J. T. Control of adenosylmethionine-dependent radical generation in biotin synthase: A kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB. Biochemistry 2003, 42, 2708-2719.
    • (2003) Biochemistry , vol.42 , pp. 2708-2719
    • Ugulava, N.B.1    Frederick, K.K.2    Jarrett, J.T.3
  • 60
    • 34248648767 scopus 로고    scopus 로고
    • Coordinating responses to iron and oxygen stress with DNA and mRNA promoters: The ferritin story
    • Theil, E. C. Coordinating responses to iron and oxygen stress with DNA and mRNA promoters: the ferritin story. Biometals 2007, 20, 513-521.
    • (2007) Biometals , vol.20 , pp. 513-521
    • Theil, E.C.1
  • 61
    • 24944557141 scopus 로고    scopus 로고
    • Differential roles of the universal stress proteins of Escherichia coli in oxidative stress resistance, adhesion, and motility
    • Nachin, L.; Nannmark, U.; Nyström, T. Differential roles of the universal stress proteins of Escherichia coli in oxidative stress resistance, adhesion, and motility. J. Bacteriol. 2005, 187, 6265-6272.
    • (2005) J. Bacteriol , vol.187 , pp. 6265-6272
    • Nachin, L.1    Nannmark, U.2    Nyström, T.3
  • 62
    • 0038013951 scopus 로고    scopus 로고
    • The bacterial universal stress protein: Function and regulation
    • Kvint, K.; Nachin, L.; Diez, A.; Nystrom, T. The bacterial universal stress protein: function and regulation. Curr. Opin. Microbiol. 2003, 6, 140-145.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 140-145
    • Kvint, K.1    Nachin, L.2    Diez, A.3    Nystrom, T.4
  • 63
    • 33645028071 scopus 로고    scopus 로고
    • Heat stress promotes mitochondrial instability and oxidative responses in yeast deficient in thiazole biosynthesis
    • Medina-Silva, R.; Barros, M. P.; Galhardo, R. S.; Netto, L. E.; Colepicolo, P.; Menck, C. F. Heat stress promotes mitochondrial instability and oxidative responses in yeast deficient in thiazole biosynthesis. Res. Microbiol. 2006, 157, 275-281.
    • (2006) Res. Microbiol , vol.157 , pp. 275-281
    • Medina-Silva, R.1    Barros, M.P.2    Galhardo, R.S.3    Netto, L.E.4    Colepicolo, P.5    Menck, C.F.6
  • 64
    • 14844326682 scopus 로고    scopus 로고
    • Proteome of Methanosarcina acetivorans Part I: An expanded view of the biology of the cell
    • Li, Q.; Li, L.; Rejtar, T.; Karger, B. L.; Ferry, J. G. Proteome of Methanosarcina acetivorans Part I: an expanded view of the biology of the cell. J. Proteome Res. 2005, 4, 112-128.
    • (2005) J. Proteome Res , vol.4 , pp. 112-128
    • Li, Q.1    Li, L.2    Rejtar, T.3    Karger, B.L.4    Ferry, J.G.5
  • 65
    • 76149103318 scopus 로고    scopus 로고
    • Translation
    • Cavicchioli, R, Ed, ASM Press: Washington, DC
    • Londei, P. Translation. In Archaea. Molecular and Cellular Biology; Cavicchioli, R., Ed.; ASM Press: Washington, DC, 2007; pp 175-208.
    • (2007) Archaea. Molecular and Cellular Biology , pp. 175-208
    • Londei, P.1
  • 66
    • 1242272089 scopus 로고    scopus 로고
    • Membrane binding of ribosomes occurs at SecYE-based sites in the Archaea Haloferax volcanii
    • Ring, G.; Eichler, J. Membrane binding of ribosomes occurs at SecYE-based sites in the Archaea Haloferax volcanii. J. Mol. Biol. 2004, 336, 997-1010.
    • (2004) J. Mol. Biol , vol.336 , pp. 997-1010
    • Ring, G.1    Eichler, J.2
  • 67
    • 65249129827 scopus 로고    scopus 로고
    • Francoleon, D. R.; Boontheung, P.; Yang, Y.; Kim, U.; Ytterberg, A. J.; Denny, P. A.; Denny, P. C.; Loo, J. A.; Gunsalus, R. P.; Ogorzalek, Loo; R. R. S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei. J. Proteome Res. 2009, 8, 1972-1982.
    • Francoleon, D. R.; Boontheung, P.; Yang, Y.; Kim, U.; Ytterberg, A. J.; Denny, P. A.; Denny, P. C.; Loo, J. A.; Gunsalus, R. P.; Ogorzalek, Loo; R. R. S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei. J. Proteome Res. 2009, 8, 1972-1982.
  • 68
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-Tu
    • Caldas, T. D.; El Yaagoubi, A.; Richarme, G. Chaperone properties of bacterial elongation factor EF-Tu. J. Biol. Chem. 1998, 273, 11478-11482.
    • (1998) J. Biol. Chem , vol.273 , pp. 11478-11482
    • Caldas, T.D.1    El Yaagoubi, A.2    Richarme, G.3
  • 69
    • 0033969301 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2
    • Caldas, T.; Laalami, S.; Richarme, G. J. Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2. Biol. Chem. 2000, 275, 855-860.
    • (2000) Biol. Chem , vol.275 , pp. 855-860
    • Caldas, T.1    Laalami, S.2    Richarme, G.J.3
  • 70
    • 57749208682 scopus 로고    scopus 로고
    • Janus chaperones: Assistance of both RNA- and protein-folding by ribosomal proteins
    • Kovacs, D.; Rakacs, M.; Agoston, B.; Lenkey, K.; Semrad, K.; Schroeder, R.; Tompa, P. Janus chaperones: assistance of both RNA- and protein-folding by ribosomal proteins. FEBS Lett. 2009, 583, 88-92.
    • (2009) FEBS Lett , vol.583 , pp. 88-92
    • Kovacs, D.1    Rakacs, M.2    Agoston, B.3    Lenkey, K.4    Semrad, K.5    Schroeder, R.6    Tompa, P.7
  • 71
    • 0030973119 scopus 로고    scopus 로고
    • Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures
    • Kandror, O.; Goldberg, A. L. Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 4978-4981.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 4978-4981
    • Kandror, O.1    Goldberg, A.L.2
  • 72
    • 0035878729 scopus 로고    scopus 로고
    • FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins
    • Ideno, A.; Yoshida, T.; Iida, T.; Furutani, M.; Maruyama, T. FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins. Biochem. J. 2001, 357, 465-471.
    • (2001) Biochem. J , vol.357 , pp. 465-471
    • Ideno, A.1    Yoshida, T.2    Iida, T.3    Furutani, M.4    Maruyama, T.5
  • 73
    • 1942467448 scopus 로고    scopus 로고
    • Recent developments in bacterial cold-shock response
    • Phadtare, S. Recent developments in bacterial cold-shock response. Curr. Issues Mol. Biol. 2004, 6, 125-136.
    • (2004) Curr. Issues Mol. Biol , vol.6 , pp. 125-136
    • Phadtare, S.1
  • 75
    • 4644325614 scopus 로고    scopus 로고
    • Serpins in unicellular Eukarya, Archaea, and Bacteria: Sequence analysis and evolution
    • Roberts, T. H.; Hejgaard, J.; Saunders, N. F. W.; Cavicchioli, R.; Curmi, P. M. Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution. J. Mol. Evol. 2004, 59, 437-447.
    • (2004) J. Mol. Evol , vol.59 , pp. 437-447
    • Roberts, T.H.1    Hejgaard, J.2    Saunders, N.F.W.3    Cavicchioli, R.4    Curmi, P.M.5
  • 76
    • 0001590871 scopus 로고    scopus 로고
    • The SPFH domain: Implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins
    • Tavernarakis, N.; Driscoll, M.; Kyrpides, N. C. The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Trends Biochem. Sci. 1999, 24, 425-427.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 425-427
    • Tavernarakis, N.1    Driscoll, M.2    Kyrpides, N.C.3
  • 77
    • 25844456936 scopus 로고    scopus 로고
    • Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli
    • Sakoh, M.; Ito, K.; Akiyama, Y. Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli. J. Biol. Chem. 2005, 280, 33305-33310.
    • (2005) J. Biol. Chem , vol.280 , pp. 33305-33310
    • Sakoh, M.1    Ito, K.2    Akiyama, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.