메뉴 건너뛰기




Volumn 79, Issue 1-3, 2002, Pages 77-133

Molecular evolution before the origin of species

Author keywords

Cell formation; Code evolution; Cofactor anchor; Hydrophobic domain; Pre divergence proteins; Residue profile; Transitional genome

Indexed keywords

ARCHAEAL PROTEIN; BACTERIAL PROTEIN; DNA; FERREDOXIN; PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0036558591     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(02)00012-3     Document Type: Review
Times cited : (46)

References (132)
  • 2
    • 0031011715 scopus 로고    scopus 로고
    • An analysis of the metabolic theory of the genetic code
    • Amirnovin R. An analysis of the metabolic theory of the genetic code. J. Mol. Evol. 44:1997;473-476.
    • (1997) J. Mol. Evol. , vol.44 , pp. 473-476
    • Amirnovin, R.1
  • 3
    • 0000976278 scopus 로고
    • Ferredoxin and photosynthesis
    • Aron D.I. Ferredoxin and photosynthesis. Science. 149:1965;1460-1470.
    • (1965) Science , vol.149 , pp. 1460-1470
    • Aron, D.I.1
  • 4
    • 0031582711 scopus 로고    scopus 로고
    • Entropy and change in molecular evolution - The case of phosphate
    • Arrhenius G., Sales B., Mojzsis S., Lee T. Entropy and change in molecular evolution - the case of phosphate. J. Theor. Biol. 187:1997;503-522.
    • (1997) J. Theor. Biol. , vol.187 , pp. 503-522
    • Arrhenius, G.1    Sales, B.2    Mojzsis, S.3    Lee, T.4
  • 5
    • 0029819318 scopus 로고    scopus 로고
    • The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny
    • Baldauf S.L., Palmer J.P., Doolittle W.F. The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny. Proc. Natl. Acad. Sci. USA. 93:1996;7749-7754.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7749-7754
    • Baldauf, S.L.1    Palmer, J.P.2    Doolittle, W.F.3
  • 6
    • 0029832927 scopus 로고    scopus 로고
    • Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences
    • Barnes S.M., Delwiche C.F., Palmer J.D., Pace N.R. Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences. Proc. Natl. Acad. Sci. USA. 93:1996;9188-9193.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9188-9193
    • Barnes, S.M.1    Delwiche, C.F.2    Palmer, J.D.3    Pace, N.R.4
  • 7
    • 0028341044 scopus 로고
    • Assemblies of free amino acids as possible prebiotic catalysts
    • Bar-Nun A., Kochavi E., Bar-Nun S. Assemblies of free amino acids as possible prebiotic catalysts. J. Mol. Evol. 39:1994;116-122.
    • (1994) J. Mol. Evol. , vol.39 , pp. 116-122
    • Bar-Nun, A.1    Kochavi, E.2    Bar-Nun, S.3
  • 8
    • 0002643350 scopus 로고    scopus 로고
    • Do the geological and geochemical records of the early Earth support the prediction from global phylogenetic models of a thermophilic cenancestor?
    • J. Wiegel, & M.W.W. Adams. Philadelphia: Taylor & Francis
    • Baross J.A. Do the geological and geochemical records of the early Earth support the prediction from global phylogenetic models of a thermophilic cenancestor? Wiegel J., Adams M.W.W. Thermophiles: The Keys to Molecular Evolution and the Origin of Life? 1998;3-18 Taylor & Francis, Philadelphia.
    • (1998) Thermophiles: The Keys to Molecular Evolution and the Origin of Life? , pp. 3-18
    • Baross, J.A.1
  • 11
    • 0001339229 scopus 로고
    • Formation synthetique d'une substance sucre
    • Boutelrow A. Formation synthetique d'une substance sucre. C. R. Acad. Sci. 53:1861;145-147.
    • (1861) C. R. Acad. Sci. , vol.53 , pp. 145-147
    • Boutelrow, A.1
  • 13
    • 0028941917 scopus 로고
    • Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications
    • Brown J.R., Doolittle W.F. Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications. Proc. Natl. Acad. Sci. USA. 92:1995;2441-2445.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2441-2445
    • Brown, J.R.1    Doolittle, W.F.2
  • 14
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult C.J., White O., Olsen G.J., Zhou L., Flieschmann R.D.et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science. 273:1996;1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Flieschmann, R.D.5
  • 16
    • 0011190457 scopus 로고
    • A model for the RNA-catalyzed replication of RNA
    • Cech T. A model for the RNA-catalyzed replication of RNA. Proc. Natl. Acad. Sci. USA. 83:1986;4360-4363.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4360-4363
    • Cech, T.1
  • 17
    • 0030002197 scopus 로고    scopus 로고
    • A helical arch allowing single stranded DNA to thread through T5 5′-exo-nuclease
    • Ceska T.A., Sayers J.R., Stier G., Suck D. A helical arch allowing single stranded DNA to thread through T5 5′-exo-nuclease. Nature. 382:1996;90-93.
    • (1996) Nature , vol.382 , pp. 90-93
    • Ceska, T.A.1    Sayers, J.R.2    Stier, G.3    Suck, D.4
  • 19
    • 0029781454 scopus 로고    scopus 로고
    • TRNA-dependent asparagine formation
    • Curnow A.W., Ibba M., Soll D. tRNA-dependent asparagine formation. Nature. 382:1996;589-590.
    • (1996) Nature , vol.382 , pp. 589-590
    • Curnow, A.W.1    Ibba, M.2    Soll, D.3
  • 21
    • 0032848426 scopus 로고    scopus 로고
    • Evolution of the genetic code
    • Davis B.K. Evolution of the genetic code. Prog. Biophys. Mol. Biol. 72:1999;157-243.
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 157-243
    • Davis, B.K.1
  • 24
    • 0024961968 scopus 로고
    • A gene encoding the proteolipid subunit of Sulfolobus acidocaldarius ATPase complex
    • Denda K., Konishi J., Oshima T., Date T., Yoshida M. A gene encoding the proteolipid subunit of Sulfolobus acidocaldarius ATPase complex. J. Biol. Chem. 264:1989;7119-7121.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7119-7121
    • Denda, K.1    Konishi, J.2    Oshima, T.3    Date, T.4    Yoshida, M.5
  • 25
    • 0032128172 scopus 로고    scopus 로고
    • Tubulin and FtsZ structures: Functional and therapeutic implications
    • Desai A., Mitchison T.J. Tubulin and FtsZ structures. functional and therapeutic implications BioEssays. 20:1998;523-527.
    • (1998) BioEssays , vol.20 , pp. 523-527
    • Desai, A.1    Mitchison, T.J.2
  • 26
    • 0033937045 scopus 로고    scopus 로고
    • The robust statistical bases of the coevolution theory of the genetic code origin
    • Di Giulio M., Medugno M. The robust statistical bases of the coevolution theory of the genetic code origin. J. Mol. Evol. 50:2000;258-263.
    • (2000) J. Mol. Evol. , vol.50 , pp. 258-263
    • Di Giulio, M.1    Medugno, M.2
  • 27
    • 0033603539 scopus 로고    scopus 로고
    • Phylogenetic classification and the universal tree
    • Doolittle W.F. Phylogenetic classification and the universal tree. Science. 284:2000;2124-2128.
    • (2000) Science , vol.284 , pp. 2124-2128
    • Doolittle, W.F.1
  • 28
    • 0014021204 scopus 로고
    • Triplet nucleotide-amino-acid pairing; A stereochemical basis for the division between protein and non-protein amino acids
    • Dunnill P. Triplet nucleotide-amino-acid pairing; a stereochemical basis for the division between protein and non-protein amino acids. Nature. 210:1966;1267-1268.
    • (1966) Nature , vol.210 , pp. 1267-1268
    • Dunnill, P.1
  • 29
    • 0001202417 scopus 로고
    • Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences
    • Eck R.V., Dayhoff M.O. Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences. Science. 152:1966;363-366.
    • (1966) Science , vol.152 , pp. 363-366
    • Eck, R.V.1    Dayhoff, M.O.2
  • 30
    • 0031587829 scopus 로고    scopus 로고
    • Archaea and the origin(s) of DNA replication proteins
    • Edgell D.R., Doolittle W.F. Archaea and the origin(s) of DNA replication proteins. Cell. 89:1997;995-998.
    • (1997) Cell , vol.89 , pp. 995-998
    • Edgell, D.R.1    Doolittle, W.F.2
  • 31
    • 0002004376 scopus 로고
    • Six questions raised by the bootstrap
    • A. Lepage, & L. Billiard. New York: Wiley-Interscience
    • Efron B. Six questions raised by the bootstrap. Lepage A., Billiard L. Exploring the Limits of the Bootstrap. 1992;99-126 Wiley-Interscience, New York.
    • (1992) Exploring the Limits of the Bootstrap , pp. 99-126
    • Efron, B.1
  • 32
    • 0030953924 scopus 로고    scopus 로고
    • Carbon isotope evidence for early life
    • Eiler J.M., Mojzsis S.J., Arrhenius G. Carbon isotope evidence for early life. Nature. 386:1997;665.
    • (1997) Nature , vol.386 , pp. 665
    • Eiler, J.M.1    Mojzsis, S.J.2    Arrhenius, G.3
  • 33
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • Erickson H.P., Taylor D.W., Bramhill D. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc. Natl. Acad. Sci. USA. 93:1996;519-523.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 519-523
    • Erickson, H.P.1    Taylor, D.W.2    Bramhill, D.3
  • 34
    • 0005209980 scopus 로고
    • A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium
    • Evans M.C.W., Buchanan B.D., Arnon D.I. A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA. 87:1966;8860-8863.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8860-8863
    • Evans, M.C.W.1    Buchanan, B.D.2    Arnon, D.I.3
  • 35
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J. Confidence limits on phylogenies. an approach using the bootstrap Evolution. 39:1985;783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 36
    • 84959747425 scopus 로고
    • Toward defining the course of evolution: Minimum change for a specific tree topology
    • Fitch W.M. Toward defining the course of evolution. minimum change for a specific tree topology Syst. Zool. 20:1971;406-416.
    • (1971) Syst. Zool. , vol.20 , pp. 406-416
    • Fitch, W.M.1
  • 37
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenza Rd
    • Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.et al. Whole-genome random sequencing and assembly of Haemophilus influenza Rd. Science. 269:1995;496-512.
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1    Adams, M.D.2    White, O.3    Clayton, R.A.4    Kirkness, E.F.5
  • 38
    • 0029876064 scopus 로고    scopus 로고
    • Synthesis of long prebiotic oligomers on mineral surfaces
    • Ferris J.P., Hill A.R., Liu R., Orgel L.E. Synthesis of long prebiotic oligomers on mineral surfaces. Nature. 381:1996;59-61.
    • (1996) Nature , vol.381 , pp. 59-61
    • Ferris, J.P.1    Hill, A.R.2    Liu, R.3    Orgel, L.E.4
  • 41
    • 0014192915 scopus 로고
    • Model for origin of monosaccharides
    • Gabel N.W., Ponnamperuma C. Model for origin of monosaccharides. Nature. 216:1967;453-455.
    • (1967) Nature , vol.216 , pp. 453-455
    • Gabel, N.W.1    Ponnamperuma, C.2
  • 45
    • 77956760389 scopus 로고
    • Ribosomal proteins: Their structure and spatial arrangement in prokaryotic ribosomes
    • Giri L., Hill W.E., Wittmann H.G. Ribosomal proteins. their structure and spatial arrangement in prokaryotic ribosomes Adv. Protein Chem. 36:1984;1-78.
    • (1984) Adv. Protein Chem. , vol.36 , pp. 1-78
    • Giri, L.1    Hill, W.E.2    Wittmann, H.G.3
  • 47
    • 0002695225 scopus 로고
    • Evolution of proton pumping ATPases: Rooting the tree of life
    • Gogarten J.P., Taiz L. Evolution of proton pumping ATPases. rooting the tree of life Photosynth. Res. 33:1992;137-146.
    • (1992) Photosynth. Res. , vol.33 , pp. 137-146
    • Gogarten, J.P.1    Taiz, L.2
  • 49
    • 0031735878 scopus 로고    scopus 로고
    • The root of the universal tree of life inferred from anciently duplicated genes encoding components of the protein targeting machinery
    • Gribaldo S., Cammarano P. The root of the universal tree of life inferred from anciently duplicated genes encoding components of the protein targeting machinery. J. Mol. Evol. 47:1998;508-516.
    • (1998) J. Mol. Evol. , vol.47 , pp. 508-516
    • Gribaldo, S.1    Cammarano, P.2
  • 52
    • 0016612552 scopus 로고
    • Speculations on the origins and evolution of metabolism
    • Hartman H. Speculations on the origins and evolution of metabolism. J. Mol. Evol. 4:1975;359-370.
    • (1975) J. Mol. Evol. , vol.4 , pp. 359-370
    • Hartman, H.1
  • 53
    • 0030478259 scopus 로고    scopus 로고
    • Organic sulfur compounds resulting from the interaction of iron sulfide, hydrogen sulfide and carbon dioxide in an anaerobic aqueous environment
    • Heinen W., Lauwers A.M. Organic sulfur compounds resulting from the interaction of iron sulfide, hydrogen sulfide and carbon dioxide in an anaerobic aqueous environment. Origins of Life. 26:1996;131-150.
    • (1996) Origins of Life , vol.26 , pp. 131-150
    • Heinen, W.1    Lauwers, A.M.2
  • 54
    • 0027738868 scopus 로고
    • Horizontal transfer of ATPase genes - The tree of life becomes a net of life
    • Hilario E., Gogarten J.P. Horizontal transfer of ATPase genes - the tree of life becomes a net of life. BioSystems. 31:1993;111-119.
    • (1993) BioSystems , vol.31 , pp. 111-119
    • Hilario, E.1    Gogarten, J.P.2
  • 55
    • 13144259724 scopus 로고    scopus 로고
    • Polymerization on the rocks: Negatively charged α-amino acids
    • Hill A.R., Bohler C., Orgel L.E. Polymerization on the rocks. negatively charged α-amino acids Origins of Life. 28:1998;235-243.
    • (1998) Origins of Life , vol.28 , pp. 235-243
    • Hill, A.R.1    Bohler, C.2    Orgel, L.E.3
  • 57
    • 0030620774 scopus 로고    scopus 로고
    • Activated acetic acid by carbon fixation on (Fe,Ni)S under primordial conditions
    • Huber C., Wachterhauser G. Activated acetic acid by carbon fixation on (Fe,Ni)S under primordial conditions. Science. 276:1997;245-247.
    • (1997) Science , vol.276 , pp. 245-247
    • Huber, C.1    Wachterhauser, G.2
  • 58
    • 0020370504 scopus 로고
    • Oligomerization of (guanosine 5′-phosphor)-2-methylimidazolide on poly(c). A RNA polymerase model
    • Inoue T., Orgel L.E. Oligomerization of (guanosine 5′-phosphor)-2-methylimidazolide on poly(c). A RNA polymerase model. J. Mol. Biol. 162:1982;201-217.
    • (1982) J. Mol. Biol. , vol.162 , pp. 201-217
    • Inoue, T.1    Orgel, L.E.2
  • 59
    • 0025938587 scopus 로고
    • MsDNA and bacterial reverse transcriptase
    • Inouye M., Inouye S. msDNA and bacterial reverse transcriptase. Ann. Rev. Microbiol. 45:1991;163-186.
    • (1991) Ann. Rev. Microbiol. , vol.45 , pp. 163-186
    • Inouye, M.1    Inouye, S.2
  • 60
    • 0024358140 scopus 로고
    • Evolutionary relationships of archaebacteria, eubacteria and eukaryotes inferred from phylogenetic trees of duplicated genes
    • Iwabe N., Kuma K.-I., Hasegawa M., Osawa S., Miyata T. Evolutionary relationships of archaebacteria, eubacteria and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc. Natl. Acad Sci. USA. 86:1989;9355-9359.
    • (1989) Proc. Natl. Acad Sci. USA , vol.86 , pp. 9355-9359
    • Iwabe, N.1    Kuma, K.-I.2    Hasegawa, M.3    Osawa, S.4    Miyata, T.5
  • 61
    • 0040322929 scopus 로고    scopus 로고
    • Mutational analysis of structure-function relationship of RNA polymerase in Escherichia coli
    • S. Adhya. San Diego: Academic Press
    • Jin D.J., Zhou Y.N. Mutational analysis of structure-function relationship of RNA polymerase in Escherichia coli. Adhya S. Methods in Enzymology. Vol. 273:1996;300-319 Academic Press, San Diego.
    • (1996) Methods in Enzymology , vol.273 , pp. 300-319
    • Jin, D.J.1    Zhou, Y.N.2
  • 62
    • 0023372377 scopus 로고
    • The case for an ancestral genetic system involving simple analogues for the nucleotides
    • Joyce G.F., Schwartz A.W., Miller S.L., Orgel L. The case for an ancestral genetic system involving simple analogues for the nucleotides. Proc. Natl. Acad. Sci. USA. 84:1987;4398-4402.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4398-4402
    • Joyce, G.F.1    Schwartz, A.W.2    Miller, S.L.3    Orgel, L.4
  • 63
    • 0000732090 scopus 로고
    • Evolution of proteins
    • H.N. Munro. New York: Academic Press
    • Jukes T.H., Cantor C.R. Evolution of proteins. Munro H.N. Mammalian Protein Metabolism. Vol. 3:1969;21-132 Academic Press, New York.
    • (1969) Mammalian Protein Metabolism. , vol.3 , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 64
    • 0031451396 scopus 로고    scopus 로고
    • DNA topoisomerases I from thermophilic bacteria: Cloning and sequencing of the DNA topoisomerase I from fervidobacterium islandicum
    • Kaltoum H., Portemer C., Confdalonieri F., Duguet M., Bouthier De La Tour C. DNA topoisomerases I from thermophilic bacteria. cloning and sequencing of the DNA topoisomerase I from fervidobacterium islandicum Syst. Appl. Microbiol. 20:1997;505-512.
    • (1997) Syst. Appl. Microbiol. , vol.20 , pp. 505-512
    • Kaltoum, H.1    Portemer, C.2    Confdalonieri, F.3    Duguet, M.4    Bouthier De La Tour, C.5
  • 65
    • 0001923744 scopus 로고    scopus 로고
    • The early diversification of life and the origin of the three domains: A proposal
    • J. Wiegel, & M.W.W. Adams. Philadelphia: Taylor & Francis
    • Kandler O. The early diversification of life and the origin of the three domains. a proposal Wiegel J., Adams M.W.W. Thermophiles: The Keys to Molecular Evolution and the Origin of Life? 1998;19-31 Taylor & Francis, Philadelphia.
    • (1998) Thermophiles: The Keys to Molecular Evolution and the Origin of Life? , pp. 19-31
    • Kandler, O.1
  • 66
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E.et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5
  • 67
    • 0029609246 scopus 로고
    • Functional map of the alpha subunit of Escherichia coli RNA polymerase: Amino acid substitution within the amino-terminal assembly domain
    • Kimura M., Ishihama A. Functional map of the alpha subunit of Escherichia coli RNA polymerase: amino acid substitution within the amino-terminal assembly domain. J. Mol. Biol. 254:1995;342-349.
    • (1995) J. Mol. Biol. , vol.254 , pp. 342-349
    • Kimura, M.1    Ishihama, A.2
  • 68
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus
    • Klenk H.P., Clayton R.A., Tomb J.F.et al. The complete genome sequence of the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus. Nature. 390:1997;364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3
  • 69
    • 0033838010 scopus 로고    scopus 로고
    • Determining the relative rates of change for prokaryotic and eukaryotic proteins with anciently duplicated paralogs
    • Kollman J.M., Doolittle R.F. Determining the relative rates of change for prokaryotic and eukaryotic proteins with anciently duplicated paralogs. J. Mol. Evol. 51:2000;173-181.
    • (2000) J. Mol. Evol. , vol.51 , pp. 173-181
    • Kollman, J.M.1    Doolittle, R.F.2
  • 70
    • 0031459310 scopus 로고    scopus 로고
    • Prokaryote genomes: The emerging paradigm of genome-based microbiology
    • Koonin E.V., Galperin M.Y. Prokaryote genomes. the emerging paradigm of genome-based microbiology Curr. Opinion Genet. Dev. 7:1997;757-763.
    • (1997) Curr. Opinion Genet. Dev. , vol.7 , pp. 757-763
    • Koonin, E.V.1    Galperin, M.Y.2
  • 72
    • 0032828663 scopus 로고    scopus 로고
    • Universal protein families and the functional content of the last universal common ancestor
    • Kyrpides N., Overbeek R., Ouzounis C. Universal protein families and the functional content of the last universal common ancestor. J. Mol. Evol. 49:1999;413-423.
    • (1999) J. Mol. Evol. , vol.49 , pp. 413-423
    • Kyrpides, N.1    Overbeek, R.2    Ouzounis, C.3
  • 75
    • 0029815789 scopus 로고    scopus 로고
    • Phylogenetic analysis of carbomyl-phosphate genes: Evolution involving multiple gene duplications, gene fusions, and insertions and deletions of surrounding sequences
    • Lawson F.S., Charlebois R.L., Dillon J.A.R. Phylogenetic analysis of carbomyl-phosphate genes. evolution involving multiple gene duplications, gene fusions, and insertions and deletions of surrounding sequences Mol. Biol. Evol. 13:1996;970-977.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 970-977
    • Lawson, F.S.1    Charlebois, R.L.2    Dillon, J.A.R.3
  • 76
    • 0032829506 scopus 로고    scopus 로고
    • On the origin of metabolic pathways
    • Lazcano A., Miller S.L. On the origin of metabolic pathways. J. Mol. Evol. 49:1999;424-431.
    • (1999) J. Mol. Evol. , vol.49 , pp. 424-431
    • Lazcano, A.1    Miller, S.L.2
  • 77
    • 0026487031 scopus 로고
    • On the early emergence of reverse transcriptase: Theoretical basis and experimental evidence
    • Lazcano A., Valverde V., Hernandez G., Gariglio P., Fox G.E., Oro J. On the early emergence of reverse transcriptase. theoretical basis and experimental evidence J. Mol. Evol. 35:1992;524-536.
    • (1992) J. Mol. Evol. , vol.35 , pp. 524-536
    • Lazcano, A.1    Valverde, V.2    Hernandez, G.3    Gariglio, P.4    Fox, G.E.5    Oro, J.6
  • 78
    • 0033199713 scopus 로고    scopus 로고
    • Did DNA replication evolve twice independently?
    • Leipe D.D., Aravind L., Koonin E.V. Did DNA replication evolve twice independently? Nucleic Acids Res. 27:1999;3389-3401.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3389-3401
    • Leipe, D.D.1    Aravind, L.2    Koonin, E.V.3
  • 79
    • 0024523256 scopus 로고
    • Reverse transcriptase-dependent synthesis of a covalently linked, branched DNA-RNA compound in E. coli B
    • Lim D., Maas W.K. Reverse transcriptase-dependent synthesis of a covalently linked, branched DNA-RNA compound in E. coli B. Cell. 56:1989;891-904.
    • (1989) Cell , vol.56 , pp. 891-904
    • Lim, D.1    Maas, W.K.2
  • 80
    • 0032825223 scopus 로고    scopus 로고
    • The root of the tree of life in the light of the covarian model
    • Lopez P., Forterre P., Philippe H. The root of the tree of life in the light of the covarian model. J. Mol. Evol. 49:1999;496-508.
    • (1999) J. Mol. Evol. , vol.49 , pp. 496-508
    • Lopez, P.1    Forterre, P.2    Philippe, H.3
  • 81
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe J., Amos L. Crystal structure of the bacterial cell-division protein FtsZ. Nature. 391:1998;203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.2
  • 82
    • 0030589056 scopus 로고    scopus 로고
    • Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima
    • Macedo-Ribeiro S., Darimont B., Sterner R., Huber R. Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima. Structure. 4:1996;1291-1301.
    • (1996) Structure , vol.4 , pp. 1291-1301
    • Macedo-Ribeiro, S.1    Darimont, B.2    Sterner, R.3    Huber, R.4
  • 83
    • 85025361814 scopus 로고
    • N-formyl-methionyl-sRNA
    • Marcker K., Sanger F. N-formyl-methionyl-sRNA. J. Mol. Biol. 8:1964;835-840.
    • (1964) J. Mol. Biol. , vol.8 , pp. 835-840
    • Marcker, K.1    Sanger, F.2
  • 84
    • 0029864056 scopus 로고    scopus 로고
    • Isolation of an ftsZ homolog from the Archaebacterium Halobacterium salinarium: Implications for the evolution of FtsZ and tubulin
    • Margolin W., Wang R., Kumar M. Isolation of an ftsZ homolog from the Archaebacterium Halobacterium salinarium. implications for the evolution of FtsZ and tubulin J. Bacteriol. 178:1996;1320-1327.
    • (1996) J. Bacteriol. , vol.178 , pp. 1320-1327
    • Margolin, W.1    Wang, R.2    Kumar, M.3
  • 85
    • 0004234377 scopus 로고
    • Boehringer Mannheim Biochemicals, Indianapolis
    • Michal, G., 1978. Biochemical pathways. Boehringer Mannheim Biochemicals, Indianapolis.
    • (1978) Biochemical Pathways
    • Michal, G.1
  • 88
    • 0031113148 scopus 로고    scopus 로고
    • Oparin's "Origin of Life": Sixty years later
    • Miller S.L., Schopf J.W., Lazcano A. Oparin's "Origin of Life" sixty years later J. Mol. Evol. 44:1997;351-353.
    • (1997) J. Mol. Evol. , vol.44 , pp. 351-353
    • Miller, S.L.1    Schopf, J.W.2    Lazcano, A.3
  • 93
    • 0035058292 scopus 로고    scopus 로고
    • Codon reassignment and the evolving code: Problems and pitfalls in post-genome analysis
    • O'Sullivan M.O., Davenport J.B., Tuite M.F. Codon reassignment and the evolving code. problems and pitfalls in post-genome analysis Trends Genet. 17:2001;20-22.
    • (2001) Trends Genet. , vol.17 , pp. 20-22
    • O'Sullivan, M.O.1    Davenport, J.B.2    Tuite, M.F.3
  • 95
    • 0032874259 scopus 로고    scopus 로고
    • The rooting of the universal tree of life is not reliable
    • Philippe H., Forterre P. The rooting of the universal tree of life is not reliable. J. Mol. Evol. 49:1999;509-523.
    • (1999) J. Mol. Evol. , vol.49 , pp. 509-523
    • Philippe, H.1    Forterre, P.2
  • 97
    • 0014192869 scopus 로고
    • Synthesis of sugars in potentially prebiotic conditions
    • Reid C., Orgel L.E. Synthesis of sugars in potentially prebiotic conditions. Nature. 216:1967;455.
    • (1967) Nature , vol.216 , pp. 455
    • Reid, C.1    Orgel, L.E.2
  • 98
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard P. From RNA to DNA, why so many ribonucleotide reductases? Science. 260:1993;1773-1777.
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 99
    • 0031025616 scopus 로고    scopus 로고
    • Ribonucleotide reductase in the archaeon Pyrococcus furiosus: A critical enzyme in the evolution of DNA genomes?
    • Riera J., Robb F.T., Weiss R., Fontecave M. Ribonucleotide reductase in the archaeon Pyrococcus furiosus. a critical enzyme in the evolution of DNA genomes? Proc. Natl. Acad Sci. USA. 94:1997;475-478.
    • (1997) Proc. Natl. Acad Sci. USA , vol.94 , pp. 475-478
    • Riera, J.1    Robb, F.T.2    Weiss, R.3    Fontecave, M.4
  • 100
    • 0005151689 scopus 로고
    • Biosynthesis of amino acids and related compounds
    • Greenberg, D.M. (Ed.). Academic Press, New York
    • Rodwell, V.W., 1969. Biosynthesis of amino acids and related compounds. In: Greenberg, D.M. (Ed.), Metabolic Pathways, 3rd Edn., Vol. 3. Academic Press, New York, pp. 317-373.
    • (1969) Metabolic Pathways, 3rd Edn. , vol.3 , pp. 317-373
    • Rodwell, V.W.1
  • 101
  • 102
    • 0003337751 scopus 로고    scopus 로고
    • The emergence of life from FeS bubbles at alkaline hot springs in an acid ocean
    • J. Weigel, M.W.W. Adams, Thermophiles London: Taylor and Francis
    • Russell M.J., Daia D.E., Hall A.J. The emergence of life from FeS bubbles at alkaline hot springs in an acid ocean. Weigel J., Adams M.W.W., Thermophiles The Keys to Molecular Evolution and the Origin of Life? 1998;77-126 Taylor and Francis, London.
    • (1998) The Keys to Molecular Evolution and the Origin of Life? , pp. 77-126
    • Russell, M.J.1    Daia, D.E.2    Hall, A.J.3
  • 103
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method. a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 4:1987;406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 104
    • 0028905115 scopus 로고
    • Evolution of tRNA recognition systems and tRNA gene sequences
    • Saks M.E., Sampson J.R. Evolution of tRNA recognition systems and tRNA gene sequences. J. Mol. Evol. 40:1995;509-518.
    • (1995) J. Mol. Evol. , vol.40 , pp. 509-518
    • Saks, M.E.1    Sampson, J.R.2
  • 105
    • 0024285823 scopus 로고
    • Protein biosynthesis in organelles requires misaminoacylation of tRNA
    • Schon A., Kannangara C.G., Gough S., Soll D. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature. 331:1988;187-190.
    • (1988) Nature , vol.331 , pp. 187-190
    • Schon, A.1    Kannangara, C.G.2    Gough, S.3    Soll, D.4
  • 106
    • 0018277518 scopus 로고
    • Origins of prokaryotes, eukaryotes, mitochondria, and chloroplasts
    • Schwarz R.M., Dayhoff M.O. Origins of prokaryotes, eukaryotes, mitochondria, and chloroplasts. Science. 199:1978;395-403.
    • (1978) Science , vol.199 , pp. 395-403
    • Schwarz, R.M.1    Dayhoff, M.O.2
  • 107
    • 0005188193 scopus 로고
    • National Biomedical Research Foundation, Silver Spring
    • Schwarz, R.M., Dayhoff, M.O., 1978b. Atlas of Protein Sequence and Structure, Vol. 5 (Suppl. 3). National Biomedical Research Foundation, Silver Spring, pp. 45-48.
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.SUPPL. 3 , pp. 45-48
    • Schwarz, R.M.1    Dayhoff, M.O.2
  • 108
    • 0024448354 scopus 로고
    • Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaea, eubacteria, and eukaryotes
    • Shimmin L.C., Ramirez C., Metheson A.T., Dennis P.P. Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaea, eubacteria, and eukaryotes. J. Mol. Evol. 29:1989;448-462.
    • (1989) J. Mol. Evol. , vol.29 , pp. 448-462
    • Shimmin, L.C.1    Ramirez, C.2    Metheson, A.T.3    Dennis, P.P.4
  • 109
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: Functional analysis and comparative genomics
    • Smith D.R., Doucette-Stamm L.A., Deloughery C.et al. Complete genome sequence of Methanobacterium thermoautotrophicum ΔH. functional analysis and comparative genomics J. Bacteriol. 179:1997;7135-7155.
    • (1997) J. Bacteriol. , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3
  • 111
    • 0345627986 scopus 로고    scopus 로고
    • The structure of iron-sulfur proteins
    • Sticht H., Rosch P. The structure of iron-sulfur proteins. Prog. Biophys. Mol. Biol. 70:1998;95-136.
    • (1998) Prog. Biophys. Mol. Biol. , vol.70 , pp. 95-136
    • Sticht, H.1    Rosch, P.2
  • 112
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe J-A., van der Donck W.A. Protein radicals in enzyme catalysis. Chem. Rev. 98:1998;705-762.
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J-A.1    Van der Donck, W.A.2
  • 113
    • 0344271983 scopus 로고
    • Prokaryotic and eukaryotic RNA polymerase have homologous core subunits
    • Sweetser D., Nonet M., Young R.A. Prokaryotic and eukaryotic RNA polymerase have homologous core subunits. Proc. Natl. Acad. USA. 84:1987;1192-1196.
    • (1987) Proc. Natl. Acad. USA , vol.84 , pp. 1192-1196
    • Sweetser, D.1    Nonet, M.2    Young, R.A.3
  • 114
    • 0030614339 scopus 로고    scopus 로고
    • 12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: An evolutionary solution to the ribonucleotide reductase conundrum
    • 12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila. an evolutionary solution to the ribonucleotide reductase conundrum Proc. Natl. Acad. Sci. USA. 94:1997;53-58.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 53-58
    • Tauer, A.1    Benner, S.A.2
  • 115
    • 0024488958 scopus 로고
    • The code within codes
    • Taylor F.J.R., Coates D. The code within codes. BioSystems. 22:1989;177-187.
    • (1989) BioSystems , vol.22 , pp. 177-187
    • Taylor, F.J.R.1    Coates, D.2
  • 116
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen Heliobacter pylori
    • Tomb J., White O., Kerlavage A., Clayton R., Sutton G.et al. The complete genome sequence of the gastric pathogen Heliobacter pylori. Nature. 388:1997;539-547.
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.1    White, O.2    Kerlavage, A.3    Clayton, R.4    Sutton, G.5
  • 117
    • 0024254814 scopus 로고
    • Before enzymes and templates: Theory of surface metabolism
    • Wachterhauser G. Before enzymes and templates. theory of surface metabolism Microbiol. Rev. 52:1988;452-484.
    • (1988) Microbiol. Rev. , vol.52 , pp. 452-484
    • Wachterhauser, G.1
  • 118
    • 0026444704 scopus 로고
    • Groundworks for an evolutionary biochemistry: The iron-sulphur world
    • Wachterhauser G. Groundworks for an evolutionary biochemistry. the iron-sulphur world Prog. Biophys. Mol. Biol. 58:1992;85-201.
    • (1992) Prog. Biophys. Mol. Biol. , vol.58 , pp. 85-201
    • Wachterhauser, G.1
  • 119
    • 0031582720 scopus 로고    scopus 로고
    • The origin of life and its methodological challenge
    • Wachterhauser G. The origin of life and its methodological challenge. J. Theor. Biol. 187:1997;483-494.
    • (1997) J. Theor. Biol. , vol.187 , pp. 483-494
    • Wachterhauser, G.1
  • 120
    • 0002669597 scopus 로고    scopus 로고
    • The case for a hyperthermophilic, chemolithoautotrophic origin of life in an iron-sulfur world
    • J. Wiegel, & M.W.W. Adams. London: Taylor and Francis
    • Wachterhauser G. The case for a hyperthermophilic, chemolithoautotrophic origin of life in an iron-sulfur world. Wiegel J., Adams M.W.W. Thermophiles: The Keys to Molecular Evolution and the Origin of Life? 1998;47-57 Taylor and Francis, London.
    • (1998) Thermophiles: The Keys to Molecular Evolution and the Origin of Life? , pp. 47-57
    • Wachterhauser, G.1
  • 121
    • 0003080768 scopus 로고
    • Amino acid sequence of a ferredoxin from thermoacidophilic archaebacteria, Thermoplasma acidophilum
    • Wakabayashi S., Fujimoto N., Wada K., Matsubara H., Kerscher L., Oesterhelt D. Amino acid sequence of a ferredoxin from thermoacidophilic archaebacteria, Thermoplasma acidophilum. FEBS Lett. 162:1983;21-24.
    • (1983) FEBS Lett. , vol.162 , pp. 21-24
    • Wakabayashi, S.1    Fujimoto, N.2    Wada, K.3    Matsubara, H.4    Kerscher, L.5    Oesterhelt, D.6
  • 122
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Richardson, C.C., et al. (Eds.). Annual Reviews Inc., Palo Alto
    • Wang, J.C., 1996. DNA topoisomerases. In: Richardson, C.C., et al. (Eds.), Ann. Rev. Biochem. Annual Reviews Inc., Palo Alto, pp. 635-692.
    • (1996) Ann. Rev. Biochem. , pp. 635-692
    • Wang, J.C.1
  • 123
    • 0019792825 scopus 로고
    • Reasons for the occurrence of the twenty coded protein amino acids
    • Weber A.L., Miller S.L. Reasons for the occurrence of the twenty coded protein amino acids. J. Mol. Evol. 17:1981;273-284.
    • (1981) J. Mol. Evol. , vol.17 , pp. 273-284
    • Weber, A.L.1    Miller, S.L.2
  • 124
    • 0031557397 scopus 로고    scopus 로고
    • Selenoprotein synthesis in Archaea: Identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion
    • Wilting R., Schorling S., Persson B.C., Bock A. Selenoprotein synthesis in Archaea. identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion J. Mol. Biol. 266:1997;637-641.
    • (1997) J. Mol. Biol. , vol.266 , pp. 637-641
    • Wilting, R.1    Schorling, S.2    Persson, B.C.3    Bock, A.4
  • 125
    • 0014324873 scopus 로고
    • Transfer RNA as a cofactor coupling amino acid synthesis with that of protein
    • Wilcox M., Nirenberg M. Transfer RNA as a cofactor coupling amino acid synthesis with that of protein. Proc. Natl. Acad. Sci. USA. 61:1968;229-236.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 229-236
    • Wilcox, M.1    Nirenberg, M.2
  • 127
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese C.R. Bacterial evolution. Microbiol. Rev. 51:1987;221-271.
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 129
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process
    • Woese C.R., Olsen G.J., Ibba M., Soll D. Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol. Mol. Biol. Rev. 64:2000;202-236.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 202-236
    • Woese, C.R.1    Olsen, G.J.2    Ibba, M.3    Soll, D.4
  • 130
    • 0001155613 scopus 로고
    • A coevolution theory of the genetic code
    • Wong J.T-F. A coevolution theory of the genetic code. Proc. Natl. Acad. Sci. USA. 72:1975;1909-1912.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1909-1912
    • Wong, J.T-F.1
  • 131
    • 0025006614 scopus 로고
    • Origin and evolution of retroelements based upon their reverse transcriptase sequences
    • Xiong Y., Eickbush T.H. Origin and evolution of retroelements based upon their reverse transcriptase sequences. EMBO J. 9:1990;3353-3362.
    • (1990) EMBO J. , vol.9 , pp. 3353-3362
    • Xiong, Y.1    Eickbush, T.H.2
  • 132
    • 0001479540 scopus 로고    scopus 로고
    • Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: Role of the cluster-coordinating aspartate in physiological electron transfer reactions
    • Zhou Z.H., Adams M.W.W. Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus. role of the cluster-coordinating aspartate in physiological electron transfer reactions Biochemistry. 36:1997;10892-10900.
    • (1997) Biochemistry , vol.36 , pp. 10892-10900
    • Zhou, Z.H.1    Adams, M.W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.