메뉴 건너뛰기




Volumn 57, Issue , 2003, Pages 487-516

Archaeal DNA Replication: Eukaryal Proteins in a Bacterial Context

Author keywords

Cell cycle; Elongation; Initiation of DNA replication; Nucleic acid metabolism; Origin of replication

Indexed keywords

CELL CYCLE PROTEIN 6; CYCLINE; DEOXYRIBONUCLEASE I; DNA POLYMERASE; DNA PRIMASE; DNA TOPOISOMERASE; DOUBLE STRANDED DNA; HELICASE; MINICHROMOSOME MAINTENANCE PROTEIN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; REPLICATION PROTEIN A; RIBONUCLEASE H; RIBOSOME RNA; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; ARCHAEAL DNA; DNA; DNA BINDING PROTEIN; DNA DIRECTED DNA POLYMERASE; OKAZAKI FRAGMENTS; REPLICATION FACTOR C;

EID: 1542682737     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.57.030502.090709     Document Type: Review
Times cited : (114)

References (168)
  • 1
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam T, Iwata A, Nishimura A, Ueda S, Ishihama A. 1999. Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol. 181:6361-70
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 2
    • 0033485460 scopus 로고    scopus 로고
    • DNA-binding proteins and evolution of transcription regulation in the archaea
    • Aravind L, Koonin EV. 1999. DNA-binding proteins and evolution of transcription regulation in the archaea. Nucleic Acids Res. 27:4658-70
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4658-4670
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 0032530488 scopus 로고    scopus 로고
    • Toprim - A conserved catalytic domain in type Ia and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins
    • Aravind L, Leipe DD, Koonin EV. 1998. Toprim - a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Nucleic Acids Res. 26:4205-13
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4205-4213
    • Aravind, L.1    Leipe, D.D.2    Koonin, E.V.3
  • 4
    • 0035169689 scopus 로고    scopus 로고
    • Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
    • Augustin MA, Huber R, Kaiser JT. 2001. Crystal structure of a DNA-dependent RNA polymerase (DNA primase). Nat. Struct. Biol. 8:57-61
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 57-61
    • Augustin, M.A.1    Huber, R.2    Kaiser, J.T.3
  • 5
    • 0033569403 scopus 로고    scopus 로고
    • Drosophila ORC specifically binds to ACE3, an origin of DNA replication control element
    • Austin RJ, Orr-Weaver TL, Bell SP. 1999. Drosophila ORC specifically binds to ACE3, an origin of DNA replication control element. Genes Dev. 13: 2639-49
    • (1999) Genes Dev. , vol.13 , pp. 2639-2649
    • Austin, R.J.1    Orr-Weaver, T.L.2    Bell, S.P.3
  • 6
    • 0029832927 scopus 로고    scopus 로고
    • Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences
    • Barns SM, Delwiche CF, Palmer JD, Pace NR. 1996. Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences. Proc. Natl. Acad. Sci. USA 93:9188-93
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9188-9193
    • Barns, S.M.1    Delwiche, C.F.2    Palmer, J.D.3    Pace, N.R.4
  • 7
    • 0035067057 scopus 로고    scopus 로고
    • Mechanism and regulation of transcription in archaea
    • Bell SD, Jackson SP. 2001. Mechanism and regulation of transcription in archaea. Curr. Opin. Microbiol. 4:208-13
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 208-213
    • Bell, S.D.1    Jackson, S.P.2
  • 8
    • 0037087587 scopus 로고    scopus 로고
    • The origin recognition complex: From simple origins to complex functions
    • Bell SP. 2002. The origin recognition complex: from simple origins to complex functions. Genes Dev. 16:659-72
    • (2002) Genes Dev. , vol.16 , pp. 659-672
    • Bell, S.P.1
  • 10
    • 0038687976 scopus 로고    scopus 로고
    • The archaeal cell cycle: Current issues
    • Bernander R. 2003. The archaeal cell cycle: current issues. Mol. Microbiol. 48: 599-604
    • (2003) Mol. Microbiol. , vol.48 , pp. 599-604
    • Bernander, R.1
  • 12
  • 13
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): An archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic π
    • Boudsocq F, Iwai S, Hanaoka F, Woodgate R. 2001. Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic π. Nucleic Acids Res. 29:4607-16
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4607-4616
    • Boudsocq, F.1    Iwai, S.2    Hanaoka, F.3    Woodgate, R.4
  • 14
    • 0029987173 scopus 로고    scopus 로고
    • Common structural features of replication origins in all life forms
    • Boulikas T. 1996. Common structural features of replication origins in all life forms. J. Cell Biochem. 60:297-316
    • (1996) J. Cell Biochem. , vol.60 , pp. 297-316
    • Boulikas, T.1
  • 17
    • 0023766613 scopus 로고
    • A model for initiation at origins of DNA replication
    • Bramhill D, Kornberg A. 1988. A model for initiation at origins of DNA replication. Cell 54:915-18
    • (1988) Cell , vol.54 , pp. 915-918
    • Bramhill, D.1    Kornberg, A.2
  • 18
    • 0032745320 scopus 로고    scopus 로고
    • Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea
    • Cann IK, Ishino S, Hayashi I, Komori K, Toh H, et al. 1999. Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea. J. Bacteriol. 181:6591-99
    • (1999) J. Bacteriol. , vol.181 , pp. 6591-6599
    • Cann, I.K.1    Ishino, S.2    Hayashi, I.3    Komori, K.4    Toh, H.5
  • 19
    • 0035093865 scopus 로고    scopus 로고
    • Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus
    • Cann IK, Ishino S, Yuasa M, Daiyasu H, Toh H, Ishino Y. 2001. Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183:2614-23
    • (2001) J. Bacteriol. , vol.183 , pp. 2614-2623
    • Cann, I.K.1    Ishino, S.2    Yuasa, M.3    Daiyasu, H.4    Toh, H.5    Ishino, Y.6
  • 20
    • 0032564361 scopus 로고    scopus 로고
    • A heterodimeric DNA polymerase: Evidence that members of Euryarchaeota possess a distinct DNA polymerase
    • Cann IK, Komori K, Toh H, Kanai S, Ishino Y. 1998. A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase. Proc. Natl. Acad. Sci. USA 95:14250-55
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14250-14255
    • Cann, I.K.1    Komori, K.2    Toh, H.3    Kanai, S.4    Ishino, Y.5
  • 21
    • 0037023748 scopus 로고    scopus 로고
    • Physical and functional interaction between the MCM-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus
    • Carpentieri F, De Felice M, De Falco M, Rossi M, Pisani FM. 2002. Physical and functional interaction between the MCM-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus. J. Biol. Chem. 277:12118-27
    • (2002) J. Biol. Chem. , vol.277 , pp. 12118-12127
    • Carpentieri, F.1    De Felice, M.2    De Falco, M.3    Rossi, M.4    Pisani, F.M.5
  • 22
    • 0037131160 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin
    • Carr KM, Kaguni JM. 2002. Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin. J. Biol. Chem. 277:39815-22
    • (2002) J. Biol. Chem. , vol.277 , pp. 39815-39822
    • Carr, K.M.1    Kaguni, J.M.2
  • 23
    • 0034805756 scopus 로고    scopus 로고
    • Archaeoglobus fulgidus RNase HII in DNA replication: Enzymological functions and activity regulation via metal cofactors
    • Chai Q, Qiu J, Chapados BR, Shen B. 2001. Archaeoglobus fulgidus RNase HII in DNA replication: enzymological functions and activity regulation via metal cofactors. Biochem. Biophys. Res. Commun. 286:1073-81
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 1073-1081
    • Chai, Q.1    Qiu, J.2    Chapados, B.R.3    Shen, B.4
  • 24
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function, and mechanism
    • Champoux JJ. 2001. DNA topoisomerases: structure, function, and mechanism. Annu. Rev. Biochem. 70:369-413
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 25
    • 0035937257 scopus 로고    scopus 로고
    • Structural biochemistry of a type 2 RNase H: RNA primer recognition and removal during DNA replication
    • Chapados BR, Chai Q, Hosfield DJ, Qiu J, Shen B, Tainer JA. 2001. Structural biochemistry of a type 2 RNase H: RNA primer recognition and removal during DNA replication. J. Mol. Biol. 307:541-56
    • (2001) J. Mol. Biol. , vol.307 , pp. 541-556
    • Chapados, B.R.1    Chai, Q.2    Hosfield, D.J.3    Qiu, J.4    Shen, B.5    Tainer, J.A.6
  • 26
    • 0344541947 scopus 로고    scopus 로고
    • Novel homologs of replication protein A in archaea: Implications for the evolution of ssDNA-binding proteins
    • Chedin F, Seitz EM, Kowalczykowski SC. 1998. Novel homologs of replication protein A in archaea: implications for the evolution of ssDNA-binding proteins. Trends Biochem. Sci. 23:273-77
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 273-277
    • Chedin, F.1    Seitz, E.M.2    Kowalczykowski, S.C.3
  • 27
    • 0034652354 scopus 로고    scopus 로고
    • A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase
    • Chong JP, Hayashi MK, Simon MN, Xu RM, Stillman B. 2000. A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase. Proc. Natl. Acad. Sci. USA 97:1530-35
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1530-1535
    • Chong, J.P.1    Hayashi, M.K.2    Simon, M.N.3    Xu, R.M.4    Stillman, B.5
  • 28
    • 0032957449 scopus 로고    scopus 로고
    • DnaA boxes are important elements in setting the initiation mass of Escherichia coli
    • Christensen BB, Atlung T, Hansen FG. 1999. DnaA boxes are important elements in setting the initiation mass of Escherichia coli. J. Bacteriol. 181:2683-88
    • (1999) J. Bacteriol. , vol.181 , pp. 2683-2688
    • Christensen, B.B.1    Atlung, T.2    Hansen, F.G.3
  • 29
    • 0029150469 scopus 로고
    • Characterization of the five replication factor C genes of Saccharomyces cerevisiae
    • Cullmann G, Fien K, Kobayashi R, Stillman B. 1995. Characterization of the five replication factor C genes of Saccharomyces cerevisiae. Mol. Cell Biol. 15:4661-71
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4661-4671
    • Cullmann, G.1    Fien, K.2    Kobayashi, R.3    Stillman, B.4
  • 30
    • 0036180382 scopus 로고    scopus 로고
    • Three proliferating cell nuclear antigen-like proteins found in the hyperthermophilic archaeon Aeropyrum pernix: Interactions with the two DNA polymerases
    • Daimon K, Kawarabayasi Y, Kikuchi H, Sako Y, Ishino Y. 2002. Three proliferating cell nuclear antigen-like proteins found in the hyperthermophilic archaeon Aeropyrum pernix: interactions with the two DNA polymerases. J. Bacteriol. 184:687-94
    • (2002) J. Bacteriol. , vol.184 , pp. 687-694
    • Daimon, K.1    Kawarabayasi, Y.2    Kikuchi, H.3    Sako, Y.4    Ishino, Y.5
  • 32
    • 0344994570 scopus 로고    scopus 로고
    • Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus
    • De Felice M, Sensen CW, Charlebois RL, Rossi M, Pisani FM. 1999. Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus. J. Mol. Biol. 291:47-57
    • (1999) J. Mol. Biol. , vol.291 , pp. 47-57
    • De Felice, M.1    Sensen, C.W.2    Charlebois, R.L.3    Rossi, M.4    Pisani, F.M.5
  • 33
    • 0003060027 scopus 로고    scopus 로고
    • Origins of DNA replication
    • ed. ML DePamphilis, Plainview, NY: Cold Spring Harbor Lab. Press
    • DePamphilis ML. 1996. Origins of DNA replication. In DNA Replication in Eukaryotic Cells, ed. ML DePamphilis, pp. 45-86. Plainview, NY: Cold Spring Harbor Lab. Press
    • (1996) DNA Replication in Eukaryotic Cells , pp. 45-86
    • DePamphilis, M.L.1
  • 34
    • 0032416608 scopus 로고    scopus 로고
    • Initiation of DNA replication in eukaryotic chromosomes
    • DePamphilis ML. 1998. Initiation of DNA replication in eukaryotic chromosomes. J. Cell Biochem. Suppl. 31:8-17
    • (1998) J. Cell Biochem. Suppl. , vol.31 , pp. 8-17
    • DePamphilis, M.L.1
  • 35
    • 0033571525 scopus 로고    scopus 로고
    • Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii
    • Desogus G, Onesti S, Brick P, Rossi M, Pisani FM. 1999. Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii. Nucleic Acids Res. 27:4444-50
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4444-4450
    • Desogus, G.1    Onesti, S.2    Brick, P.3    Rossi, M.4    Pisani, F.M.5
  • 36
    • 0037251411 scopus 로고    scopus 로고
    • A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Dionne I, Nookala R, Jackson SP, Doherty AJ, Bell SD. 2003. A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus. Mol. Cell 11:275-82
    • (2003) Mol. Cell , vol.11 , pp. 275-282
    • Dionne, I.1    Nookala, R.2    Jackson, S.P.3    Doherty, A.J.4    Bell, S.D.5
  • 37
    • 0031587829 scopus 로고    scopus 로고
    • Archaea and the origin(s) of DNA replication proteins
    • Edgell DR, Doolittle WF. 1997. Archaea and the origin(s) of DNA replication proteins. Cell 89:995-98
    • (1997) Cell , vol.89 , pp. 995-998
    • Edgell, D.R.1    Doolittle, W.F.2
  • 38
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: Implications for general mechanisms underlying DNA replication initiation
    • Erzberger JP, Pirruccello MM, Berger JM. 2002. The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 21:4763-73
    • (2002) EMBO J. , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 41
    • 19544370577 scopus 로고    scopus 로고
    • Origin and evolution of DNA and DNA replication machineries
    • ed. L Ribas, In press. Georgetown, TX: Landes Biosci.
    • Forterre P, Filee J, Myllykallio H. 2003. Origin and evolution of DNA and DNA replication machineries. In The Genetic Code and the Origin of Life, ed. L Ribas, pp. In press. Georgetown, TX: Landes Biosci.
    • (2003) The Genetic Code and the Origin of Life
    • Forterre, P.1    Filee, J.2    Myllykallio, H.3
  • 44
    • 0242542133 scopus 로고    scopus 로고
    • Common domains in the initiators of DNA replication in Bacteria, Archaea and Eukarya: Combined structural, functional and phylogenetic perspectives
    • Giraldo R. 2002. Common domains in the initiators of DNA replication in Bacteria, Archaea and Eukarya: combined structural, functional and phylogenetic perspectives. FEBS Microbiol. Rev. 762: 1-22
    • (2002) FEBS Microbiol. Rev. , vol.762 , pp. 1-22
    • Giraldo, R.1
  • 45
    • 0035942258 scopus 로고    scopus 로고
    • Similarities between the DNA replication initiators of Gram-negative bacteria plasmids (RepA) and eukaryotes (Orc4p)/archaea (Cdc6p)
    • Giraldo R, Diaz-Orejas R. 2001. Similarities between the DNA replication initiators of Gram-negative bacteria plasmids (RepA) and eukaryotes (Orc4p)/archaea (Cdc6p). Proc. Natl. Acad. Sci. USA 98: 4938-43
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4938-4943
    • Giraldo, R.1    Diaz-Orejas, R.2
  • 46
    • 0034868902 scopus 로고    scopus 로고
    • Autophosphorylation of the archaeal Cdc6 homologues is regulated by DNA
    • Grabowski B, Kelman Z. 2001. Autophosphorylation of the archaeal Cdc6 homologues is regulated by DNA. J. Bacteriol. 183:5459-64
    • (2001) J. Bacteriol. , vol.183 , pp. 5459-5464
    • Grabowski, B.1    Kelman, Z.2
  • 47
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • Harrington JJ, Lieber MR. 1994. The characterization of a mammalian DNA structure-specific endonuclease. EMBO J. 13:1235-46
    • (1994) EMBO J. , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 48
    • 0031786215 scopus 로고    scopus 로고
    • Gene cloning and characterization of recombinant RNase HII from a hyperthermophilic archaeon
    • Haruki M, Hayashi K, Kochi T, Muroya A, Koga Y, et al. 1998. Gene cloning and characterization of recombinant RNase HII from a hyperthermophilic archaeon. J. Bacteriol. 180:6207-14
    • (1998) J. Bacteriol. , vol.180 , pp. 6207-6214
    • Haruki, M.1    Hayashi, K.2    Kochi, T.3    Muroya, A.4    Koga, Y.5
  • 49
    • 0036015495 scopus 로고    scopus 로고
    • A distinctive single-strand DNA-binding protein from the Archaeon Sulfolobus solfataricus
    • Haseltine CA, Kowalczykoski SC. 2002. A distinctive single-strand DNA-binding protein from the Archaeon Sulfolobus solfataricus. Mol. Microbiol. 43:1505-15
    • (2002) Mol. Microbiol. , vol.43 , pp. 1505-1515
    • Haseltine, C.A.1    Kowalczykoski, S.C.2
  • 50
    • 0035936690 scopus 로고    scopus 로고
    • Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • Hashimoto H, Nishioka M, Fujiwara S, Takagi M, Imanaka T, et al. 2001. Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. J. Mol. Biol. 306:469-77
    • (2001) J. Mol. Biol. , vol.306 , pp. 469-477
    • Hashimoto, H.1    Nishioka, M.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 51
    • 0033572698 scopus 로고    scopus 로고
    • Specific interaction between DNA polymerase II (PolD) and RadB, a Rad51/Dmc1 homolog, in Pyrococcus furiosus
    • Hayashi I, Morikawa K, Ishino Y. 1999. Specific interaction between DNA polymerase II (PolD) and RadB, a Rad51/Dmc1 homolog, in Pyrococcus furiosus. Nucleic Acids Res. 27:4695-702
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4695-4702
    • Hayashi, I.1    Morikawa, K.2    Ishino, Y.3
  • 52
    • 0036430301 scopus 로고    scopus 로고
    • Replication factor C from the hyperthermophilic archaeon Pyrococcus abyssi does not need ATP hydrolysis for clamp-loading and contains a functionally conserved RFC PCNA-binding domain
    • Henneke G, Gueguen Y, Flament D, Azam P, Querellou J, et al. 2002. Replication factor C from the hyperthermophilic archaeon Pyrococcus abyssi does not need ATP hydrolysis for clamp-loading and contains a functionally conserved RFC PCNA-binding domain. J. Mol. Biol. 323:795-810
    • (2002) J. Mol. Biol. , vol.323 , pp. 795-810
    • Henneke, G.1    Gueguen, Y.2    Flament, D.3    Azam, P.4    Querellou, J.5
  • 56
    • 0032538537 scopus 로고    scopus 로고
    • Newly discovered archaebacterial flap endonucleases show a structure-specific mechanism for DNA substrate binding and catalysis resembling human flap endonuclease-1
    • Hosfield DJ, Frank G, Weng Y, Tainer JA, Shen B. 1998. Newly discovered archaebacterial flap endonucleases show a structure-specific mechanism for DNA substrate binding and catalysis resembling human flap endonuclease-1. J. Biol. Chem. 273:27154-61
    • (1998) J. Biol. Chem. , vol.273 , pp. 27154-27161
    • Hosfield, D.J.1    Frank, G.2    Weng, Y.3    Tainer, J.A.4    Shen, B.5
  • 57
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: Coupling DNA and PCNA binding to FEN-1 activity
    • Hosfield DJ, Mol CD, Shen B, Tainer JA. 1998. Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell 95:135-46
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 59
    • 0037007636 scopus 로고    scopus 로고
    • A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont
    • Huber H, Hohn MJ, Rachel R, Fuchs T, Wimmer VC, Stetter KO. 2002. A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont. Nature 417:63-67
    • (2002) Nature , vol.417 , pp. 63-67
    • Huber, H.1    Hohn, M.J.2    Rachel, R.3    Fuchs, T.4    Wimmer, V.C.5    Stetter, K.O.6
  • 60
    • 0035980791 scopus 로고    scopus 로고
    • Replication of the lagging strand: A concert of at least 23 polypeptides
    • Hubscher U, Seo YS. 2001. Replication of the lagging strand: a concert of at least 23 polypeptides. Mol. Cell 12:149-57
    • (2001) Mol. Cell , vol.12 , pp. 149-157
    • Hubscher, U.1    Seo, Y.S.2
  • 61
    • 0031873411 scopus 로고    scopus 로고
    • The crystal structure of flap endonuclease-1 from Methanococcus jannaschii
    • Hwang KY, Baek K, Kim HY, Cho Y. 1998. The crystal structure of flap endonuclease-1 from Methanococcus jannaschii. Nat. Struct. Biol. 5:707-13
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 707-713
    • Hwang, K.Y.1    Baek, K.2    Kim, H.Y.3    Cho, Y.4
  • 63
    • 0030859463 scopus 로고    scopus 로고
    • A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex
    • Erratum. 1998. 273(36): 23616
    • Ishimi Y. 1997. A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex. J. Biol. Chem. 272: 24508-13. Erratum. 1998. 273(36): 23616
    • (1997) J. Biol. Chem. , vol.272 , pp. 24508-24513
    • Ishimi, Y.1
  • 64
    • 0032415809 scopus 로고    scopus 로고
    • The euryarchaeotes, a subdomain of Archaea, survive on a single DNA polymerase: Fact or farce?
    • Ishino Y, Cann IK. 1998. The euryarchaeotes, a subdomain of Archaea, survive on a single DNA polymerase: fact or farce? Genes Genet. Syst. 73:323-36
    • (1998) Genes Genet. Syst. , vol.73 , pp. 323-336
    • Ishino, Y.1    Cann, I.K.2
  • 65
    • 0031922356 scopus 로고    scopus 로고
    • A novel DNA polymerase family found in Archaea
    • Ishino Y, Komori K, Cann IK, Koga Y. 1998. A novel DNA polymerase family found in Archaea. J. Bacteriol. 180: 2232-36
    • (1998) J. Bacteriol. , vol.180 , pp. 2232-2236
    • Ishino, Y.1    Komori, K.2    Cann, I.K.3    Koga, Y.4
  • 66
    • 0034741835 scopus 로고    scopus 로고
    • Functional interactions of an archaeal sliding clamp with mammalian clamp loader and DNA polymerase δ
    • Ishino Y, Tsurimoto T, Ishino S, Cann IK. 2001. Functional interactions of an archaeal sliding clamp with mammalian clamp loader and DNA polymerase δ. Genes Cell 6:699-706
    • (2001) Genes Cell , vol.6 , pp. 699-706
    • Ishino, Y.1    Tsurimoto, T.2    Ishino, S.3    Cann, I.K.4
  • 67
    • 0035666447 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a DNA primase from hyperthermophilic archaeon Pyrococcus horikoshii
    • Ito N, Nureki O, Shirouzu M, Yokoyama S, Hanaoka F. 2001. Crystallization and preliminary X-ray analysis of a DNA primase from hyperthermophilic archaeon Pyrococcus horikoshii. J. Biochem. (Tokyo) 130:727-30
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 727-730
    • Ito, N.1    Nureki, O.2    Shirouzu, M.3    Yokoyama, S.4    Hanaoka, F.5
  • 70
    • 0033616714 scopus 로고    scopus 로고
    • Horizontal gene transfer among genomes: The complexity hypothesis
    • Jain R, Rivera MC, Lake JA. 1999. Horizontal gene transfer among genomes: the complexity hypothesis. Proc. Natl. Acad. Sci. USA 96:3801-6
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3801-3806
    • Jain, R.1    Rivera, M.C.2    Lake, J.A.3
  • 71
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III
    • Jeruzalmi D, O'Donnell M, Kuriyan J. 2001. Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III. Cell 106:429-41
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 72
    • 0033597786 scopus 로고    scopus 로고
    • A comparison of eubacterial and archaeal structure-specific 5′-exonucleases
    • Kaiser MW, Lyamicheva N, Ma W, Miller C, Neri B, et al. 1999. A comparison of eubacterial and archaeal structure-specific 5′-exonucleases. J. Biol. Chem. 274:21387-94
    • (1999) J. Biol. Chem. , vol.274 , pp. 21387-21394
    • Kaiser, M.W.1    Lyamicheva, N.2    Ma, W.3    Miller, C.4    Neri, B.5
  • 73
    • 0032409981 scopus 로고    scopus 로고
    • Identification and characterization of a single-stranded DNA-binding protein from the archaeon Methanococcus jannaschii
    • Kelly TJ, Simancek P, Brush GS. 1998. Identification and characterization of a single-stranded DNA-binding protein from the archaeon Methanococcus jannaschii. Proc. Natl. Acad. Sci. USA 95:14634-39
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14634-14639
    • Kelly, T.J.1    Simancek, P.2    Brush, G.S.3
  • 74
    • 0038687925 scopus 로고    scopus 로고
    • Archaea: An archetype for replication initiation studies?
    • Kelman LM, Kelman Z. 2003. Archaea: an archetype for replication initiation studies? Mol. Microbiol. 48:605-15
    • (2003) Mol. Microbiol. , vol.48 , pp. 605-615
    • Kelman, L.M.1    Kelman, Z.2
  • 75
    • 0031045565 scopus 로고    scopus 로고
    • PCNA: Structure, functions and interactions
    • Kelman Z. 1997. PCNA: structure, functions and interactions. Oncogene 14: 629-40
    • (1997) Oncogene , vol.14 , pp. 629-640
    • Kelman, Z.1
  • 76
    • 0000024368 scopus 로고    scopus 로고
    • DNA replication in the third domain (of life)
    • Kelman Z. 2000. DNA replication in the third domain (of life). Curr. Protein Peptide Sci. 1:139-54
    • (2000) Curr. Protein Peptide Sci. , vol.1 , pp. 139-154
    • Kelman, Z.1
  • 77
    • 0034327485 scopus 로고    scopus 로고
    • The replication origin of archaea is finally revealed
    • Kelman Z. 2000. The replication origin of archaea is finally revealed. Trends Biochem. Sci. 25:521-23
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 521-523
    • Kelman, Z.1
  • 78
    • 0032126403 scopus 로고    scopus 로고
    • Protein-PCNA interactions: A DNA-scanning mechanism?
    • Kelman Z, Hurwitz J. 1998. Protein-PCNA interactions: a DNA-scanning mechanism? Trends Biochem. Sci. 23: 236-38
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 236-238
    • Kelman, Z.1    Hurwitz, J.2
  • 79
    • 0034629109 scopus 로고    scopus 로고
    • A unique organization of the protein subunits of the DNA polymerase clamp loader in the archaeon Methanobacterium thermoautotrophicum ΔH
    • Kelman Z, Hurwitz J. 2000. A unique organization of the protein subunits of the DNA polymerase clamp loader in the archaeon Methanobacterium thermoautotrophicum ΔH. J. Biol. Chem. 275:7327-36
    • (2000) J. Biol. Chem. , vol.275 , pp. 7327-7336
    • Kelman, Z.1    Hurwitz, J.2
  • 80
    • 0037334907 scopus 로고    scopus 로고
    • Structural lessons in DNA replication from the third domain of life
    • Kelman Z, Hurwitz M. 2003. Structural lessons in DNA replication from the third domain of life. Nat. Struct. Biol. 10:148-50
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 148-150
    • Kelman, Z.1    Hurwitz, M.2
  • 81
    • 0033593053 scopus 로고    scopus 로고
    • The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum ΔH contains DNA helicase activity
    • Kelman Z, Lee JK, Hurwitz J. 1999. The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum ΔH contains DNA helicase activity. Proc. Natl. Acad. Sci. USA 96:14783-88
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14783-14788
    • Kelman, Z.1    Lee, J.K.2    Hurwitz, J.3
  • 82
    • 0029336696 scopus 로고
    • Embryonic PCNA: A missing link?
    • Kelman Z, O'Donnell M. 1995. Embryonic PCNA: a missing link?. Curr. Biol. 5:814
    • (1995) Curr. Biol. , vol.5 , pp. 814
    • Kelman, Z.1    O'Donnell, M.2
  • 83
    • 0029163487 scopus 로고
    • Structural and functional similarities of prokaryotic and eukaryotic DNA polymerase sliding clamps
    • Erratum. 1995. 23(23):4938
    • Kelman Z, O'Donnell M. 1995. Structural and functional similarities of prokaryotic and eukaryotic DNA polymerase sliding clamps. Nucleic Acids Res. 23: 3613-20. Erratum. 1995. 23(23):4938
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3613-3620
    • Kelman, Z.1    O'Donnell, M.2
  • 84
    • 0033214481 scopus 로고    scopus 로고
    • Isolation and characterization of a split B-type DNA polymerase from the archaeon Methanobacterium thermoautotrophicum ΔH
    • Kelman Z, Pietrokovski S, Hurwitz J. 1999. Isolation and characterization of a split B-type DNA polymerase from the archaeon Methanobacterium thermoautotrophicum ΔH. J. Biol. Chem. 274:28751-61
    • (1999) J. Biol. Chem. , vol.274 , pp. 28751-28761
    • Kelman, Z.1    Pietrokovski, S.2    Hurwitz, J.3
  • 85
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman Z, Yuzhakov A, Andjelkovic J, O'Donnell M. 1998. Devoted to the lagging strand-the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J. 17:2436-49
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 86
    • 0034767491 scopus 로고    scopus 로고
    • Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence
    • Kennedy SP, Ng WV, Salzberg SL, Hood L, DasSarma S. 2001. Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence. Genome Res. 11:1641-50
    • (2001) Genome Res. , vol.11 , pp. 1641-1650
    • Kennedy, S.P.1    Ng, W.V.2    Salzberg, S.L.3    Hood, L.4    DasSarma, S.5
  • 87
    • 0033564245 scopus 로고    scopus 로고
    • Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology
    • Kirk BW, Kuchta RD. 1999. Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology. Biochemistry 38:7727-36
    • (1999) Biochemistry , vol.38 , pp. 7727-7736
    • Kirk, B.W.1    Kuchta, R.D.2
  • 88
    • 0026661136 scopus 로고
    • Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases
    • Kletzin A. 1992. Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases. Nucleic Acids Res. 20:5389-96
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5389-5396
    • Kletzin, A.1
  • 89
    • 0035854709 scopus 로고    scopus 로고
    • Replication protein A in Pyrococcus furiosus is involved in homologous DNA recombination
    • Komori K, Ishino Y. 2001. Replication protein A in Pyrococcus furiosus is involved in homologous DNA recombination. J. Biol. Chem. 276:25654-60
    • (2001) J. Biol. Chem. , vol.276 , pp. 25654-25660
    • Komori, K.1    Ishino, Y.2
  • 90
    • 0030868589 scopus 로고    scopus 로고
    • Comparison of archaeal and bacterial genomes: Computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for the archaea
    • Koonin EV, Mushegian AR, Galperin MY, Walker DR. 1997. Comparison of archaeal and bacterial genomes: Computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for the archaea. Mol. Microbiol. 25:619-37
    • (1997) Mol. Microbiol. , vol.25 , pp. 619-637
    • Koonin, E.V.1    Mushegian, A.R.2    Galperin, M.Y.3    Walker, D.R.4
  • 92
    • 0034662744 scopus 로고    scopus 로고
    • Crystal structure of archaeal RNase HII: A homologue of human major RNase H
    • Lai L, Yokota H, Hung LW, Kim R, Kim SH. 2000. Crystal structure of archaeal RNase HII: a homologue of human major RNase H. Struct. Fold. Des. 8:897-904
    • (2000) Struct. Fold. Des. , vol.8 , pp. 897-904
    • Lai, L.1    Yokota, H.2    Hung, L.W.3    Kim, R.4    Kim, S.H.5
  • 93
    • 0037219192 scopus 로고    scopus 로고
    • A rotary pumping model for helicase function of MCM proteins at a distance from replication forks
    • Laskey RA, Madine MA. 2003. A rotary pumping model for helicase function of MCM proteins at a distance from replication forks. EMBO Rep. 4:1-5
    • (2003) EMBO Rep. , vol.4 , pp. 1-5
    • Laskey, R.A.1    Madine, M.A.2
  • 94
    • 0034063607 scopus 로고    scopus 로고
    • ATPase switches controlling DNA replication initiation
    • Lee DG, Bell SP. 2000. ATPase switches controlling DNA replication initiation. Curr. Opin. Cell Biol. 12:280-85
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 280-285
    • Lee, D.G.1    Bell, S.P.2
  • 95
    • 0035793113 scopus 로고    scopus 로고
    • Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures
    • Lee J-K, Hurwitz J. 2001. Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures. Proc. Natl. Acad. Sci. USA 98:54-59
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 54-59
    • Lee, J.-K.1    Hurwitz, J.2
  • 96
    • 0030692134 scopus 로고    scopus 로고
    • An interaction between DNA ligase I and proliferating cell nuclear antigen: Implications for Okazaki fragment synthesis and joining
    • Levin DS, Bai W, Yao N, O'Donnell M, Tomkinson AE. 1997. An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining. Proc. Natl. Acad. Sci. USA 94:12863-68
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12863-12868
    • Levin, D.S.1    Bai, W.2    Yao, N.3    O'Donnell, M.4    Tomkinson, A.E.5
  • 97
    • 0029092897 scopus 로고
    • Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen
    • Li X, Li J, Harrington J, Lieber MR, Burgers PM. 1995. Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen. J. Biol. Chem. 270:22109-12
    • (1995) J. Biol. Chem. , vol.270 , pp. 22109-22112
    • Li, X.1    Li, J.2    Harrington, J.3    Lieber, M.R.4    Burgers, P.M.5
  • 99
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM. 2000. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 6:637-48
    • (2000) Mol. Cell , vol.6 , pp. 637-648
    • Liu, J.1    Smith, C.L.2    DeRyckere, D.3    DeAngelis, K.4    Martin, G.S.5    Berger, J.M.6
  • 100
    • 0035976978 scopus 로고    scopus 로고
    • The archaeal DNA primase: Biochemical characterization of the p41-p46 complex from Pyrococcus furiosus
    • Liu L, Komori K, Ishino S, Bocquier AA, Cann IK, et al. 2001. The archaeal DNA primase: biochemical characterization of the p41-p46 complex from Pyrococcus furiosus. J. Biol. Chem. 276:45484-90
    • (2001) J. Biol. Chem. , vol.276 , pp. 45484-45490
    • Liu, L.1    Komori, K.2    Ishino, S.3    Bocquier, A.A.4    Cann, I.K.5
  • 101
    • 0032972657 scopus 로고    scopus 로고
    • Identification of putative chromosomal origins of replication in Archaea
    • Lopez P, Philippe H, Myllykallio H, Forterre P. 1999. Identification of putative chromosomal origins of replication in Archaea. Mol. Microbiol. 32:883-86
    • (1999) Mol. Microbiol. , vol.32 , pp. 883-886
    • Lopez, P.1    Philippe, H.2    Myllykallio, H.3    Forterre, P.4
  • 102
    • 0034999673 scopus 로고    scopus 로고
    • Understanding the enzymology of archaeal DNA replication: Progress in form and function
    • MacNeill SA. 2001. Understanding the enzymology of archaeal DNA replication: progress in form and function. Mol. Microbiol. 40:520-29
    • (2001) Mol. Microbiol. , vol.40 , pp. 520-529
    • MacNeill, S.A.1
  • 103
    • 0036050023 scopus 로고    scopus 로고
    • Chromosome replication patterns in the hyperthermophilic euryarchaea Archaeoglobus fulgidus and Méthanocaldococcus (Methanococcus) jannaschii
    • Maisnier-Patin S, Malandrin L, Birkeland NK, Bernander R. 2002. Chromosome replication patterns in the hyperthermophilic euryarchaea Archaeoglobus fulgidus and Méthanocaldococcus (Methanococcus) jannaschii. Mol. Microbiol. 45:1443-50
    • (2002) Mol. Microbiol. , vol.45 , pp. 1443-1450
    • Maisnier-Patin, S.1    Malandrin, L.2    Birkeland, N.K.3    Bernander, R.4
  • 104
    • 0032766490 scopus 로고    scopus 로고
    • Comparative genomics of the Archaea (Euryarchaeota): Evolution of conserved protein families, the stable core, and the variable shell
    • Makarova KS, Aravind L, Galperin MY, Grishin NV, Tatusov RL, et al. 1999. Comparative genomics of the Archaea (Euryarchaeota): evolution of conserved protein families, the stable core, and the variable shell. Genome Res. 9:608-28
    • (1999) Genome Res. , vol.9 , pp. 608-628
    • Makarova, K.S.1    Aravind, L.2    Galperin, M.Y.3    Grishin, N.V.4    Tatusov, R.L.5
  • 107
    • 0033603350 scopus 로고    scopus 로고
    • Thermostable flap endonuclease from the archaeon, Pyrococcus horikoshii, cleaves the replication fork-like structure endo/exonucleolytically
    • Matsui E, Kawasaki S, Ishida H, Ishikawa K, Kosugi Y, et al. 1999. Thermostable flap endonuclease from the archaeon, Pyrococcus horikoshii, cleaves the replication fork-like structure endo/exonucleolytically. J. Biol. Chem. 274: 18297-309
    • (1999) J. Biol. Chem. , vol.274 , pp. 18297-18309
    • Matsui, E.1    Kawasaki, S.2    Ishida, H.3    Ishikawa, K.4    Kosugi, Y.5
  • 108
    • 0037020251 scopus 로고    scopus 로고
    • Molecular structure and novel DNA binding sites located in loops of flap endonuclease-1 from Pyrococcus horikoshii
    • Matsui E, Musti KV, Abe J, Yamasaki K, Matsui I, Harata K. 2002. Molecular structure and novel DNA binding sites located in loops of flap endonuclease-1 from Pyrococcus horikoshii. J. Biol. Chem. 277:37840-47
    • (2002) J. Biol. Chem. , vol.277 , pp. 37840-37847
    • Matsui, E.1    Musti, K.V.2    Abe, J.3    Yamasaki, K.4    Matsui, I.5    Harata, K.6
  • 109
    • 0036734527 scopus 로고    scopus 로고
    • Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus
    • Matsumiya S, Ishino S, Ishino Y, Morikawa K. 2002. Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus. Genes Cells 7:911-22
    • (2002) Genes Cells , vol.7 , pp. 911-922
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 110
    • 0037377527 scopus 로고    scopus 로고
    • Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA
    • Matsumiya S, Ishino S, Ishino Y, Morikawa K. 2003. Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA. Protein Sci. 12:823-31
    • (2003) Protein Sci. , vol.12 , pp. 823-831
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 111
    • 0035107856 scopus 로고    scopus 로고
    • Crystal structure of an archaeal DNA sliding clamp: Proliferating cell nuclear antigen from Pyrococcus furiosus
    • Matsumiya S, Ishino Y, Morikawa K. 2001. Crystal structure of an archaeal DNA sliding clamp: proliferating cell nuclear antigen from Pyrococcus furiosus. Protein Sci. 10:17-23
    • (2001) Protein Sci. , vol.10 , pp. 17-23
    • Matsumiya, S.1    Ishino, Y.2    Morikawa, K.3
  • 112
    • 0035949506 scopus 로고    scopus 로고
    • In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance protein with the replication origin
    • Matsunaga F, Forterre P, Ishino Y, Myllykallio H. 2001. In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance protein with the replication origin. Proc. Natl. Acad. Sci. USA 98:11152-57
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11152-11157
    • Matsunaga, F.1    Forterre, P.2    Ishino, Y.3    Myllykallio, H.4
  • 113
    • 0037295722 scopus 로고    scopus 로고
    • Identification of short 'eukaryotic' Okazaki fragments synthesized from a prokaryotic replication origin
    • Matsunaga F, Norais C, Forterre P, Myllykallio H. 2003. Identification of short 'eukaryotic' Okazaki fragments synthesized from a prokaryotic replication origin. EMBO Rep. 4:154-58
    • (2003) EMBO Rep. , vol.4 , pp. 154-158
    • Matsunaga, F.1    Norais, C.2    Forterre, P.3    Myllykallio, H.4
  • 114
    • 0035783136 scopus 로고    scopus 로고
    • Three-dimensional electron microscopy of the clamp loader small subunit from Pyrococcus furiosus
    • Mayanagi K, Miyata T, Oyama T, Ishino Y, Morikawa K. 2001. Three-dimensional electron microscopy of the clamp loader small subunit from Pyrococcus furiosus. J. Struct. Biol. 134:35-45
    • (2001) J. Struct. Biol. , vol.134 , pp. 35-45
    • Mayanagi, K.1    Miyata, T.2    Oyama, T.3    Ishino, Y.4    Morikawa, K.5
  • 115
    • 0033792010 scopus 로고    scopus 로고
    • Two different oligomeric states of the RuvB branch migration motor protein as revealed by electron microscopy
    • Miyata T, Yamada K, Iwasaki H, Shinagawa H, Morikawa K, Mayanagi K. 2000. Two different oligomeric states of the RuvB branch migration motor protein as revealed by electron microscopy. J. Struct. Biol. 131:83-89
    • (2000) J. Struct. Biol. , vol.131 , pp. 83-89
    • Miyata, T.1    Yamada, K.2    Iwasaki, H.3    Shinagawa, H.4    Morikawa, K.5    Mayanagi, K.6
  • 116
    • 0033607154 scopus 로고    scopus 로고
    • Identification and reconstitution of the origin recognition complex from Schizosaccharomyces pombe
    • Moon KY, Kong D, Lee JK, Raychaudhuri S, Hurwitz J. 1999. Identification and reconstitution of the origin recognition complex from Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 96: 12367-72
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12367-12372
    • Moon, K.Y.1    Kong, D.2    Lee, J.K.3    Raychaudhuri, S.4    Hurwitz, J.5
  • 117
    • 0037013241 scopus 로고    scopus 로고
    • Elucidation of an archaeal replication protein network to generate enhanced PCR enzymes
    • Motz M, Kober I, Girardot C, Loeser E, Bauer U, et al. 2002. Elucidation of an archaeal replication protein network to generate enhanced PCR enzymes. J. Biol. Chem. 277:16179-88
    • (2002) J. Biol. Chem. , vol.277 , pp. 16179-16188
    • Motz, M.1    Kober, I.2    Girardot, C.3    Loeser, E.4    Bauer, U.5
  • 118
    • 0027479161 scopus 로고
    • OB(oligonucleotide/ oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin AG. 1993. OB(oligonucleotide/ oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12:861-67
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 119
    • 0034541136 scopus 로고    scopus 로고
    • Mapping of a chromosome replication origin in an archaeon: Response
    • Myllykallio H, Forterre P. 2000. Mapping of a chromosome replication origin in an archaeon: response. Trends Microbiol. 8:537-39
    • (2000) Trends Microbiol. , vol.8 , pp. 537-539
    • Myllykallio, H.1    Forterre, P.2
  • 120
    • 0034705420 scopus 로고    scopus 로고
    • Bacterial mode of replication with eukaryotic-like machinery in a hyperthermophilic archaeon
    • Myllykallio H, Lopez P, Lopez-Garcia P, Heilig R, Saurin W, et al. 2000. Bacterial mode of replication with eukaryotic-like machinery in a hyperthermophilic archaeon. Science 288:2212-15
    • (2000) Science , vol.288 , pp. 2212-2215
    • Myllykallio, H.1    Lopez, P.2    Lopez-Garcia, P.3    Heilig, R.4    Saurin, W.5
  • 121
    • 0033764931 scopus 로고    scopus 로고
    • A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity
    • Nakatani M, Ezaki S, Atomi H, Imanaka T. 2000. A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity. J. Bacteriol. 182:6424-33
    • (2000) J. Bacteriol. , vol.182 , pp. 6424-6433
    • Nakatani, M.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 122
    • 0036159475 scopus 로고    scopus 로고
    • Substrate recognition and fidelity of strand joining by an archaeal DNA ligase
    • Nakatani M, Ezaki S, Atomi H, Imanaka T. 2002. Substrate recognition and fidelity of strand joining by an archaeal DNA ligase. Eur. J. Biochem. 269:650-56
    • (2002) Eur. J. Biochem. , vol.269 , pp. 650-656
    • Nakatani, M.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 123
    • 0034572821 scopus 로고    scopus 로고
    • Towards understanding the first genome sequence of a crenarchaeon by genome annotation using clusters of orthologous groups of proteins (COGs)
    • Natale DA, Shankavaram UT, Galperin MY, Wolf YI, Aravind L, Koonin EV. 2000. Towards understanding the first genome sequence of a crenarchaeon by genome annotation using clusters of orthologous groups of proteins (COGs). Genome Biol. 1:1-19
    • (2000) Genome Biol. , vol.1 , pp. 1-19
    • Natale, D.A.1    Shankavaram, U.T.2    Galperin, M.Y.3    Wolf, Y.I.4    Aravind, L.5    Koonin, E.V.6
  • 124
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 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
  • 125
    • 0033229826 scopus 로고    scopus 로고
    • Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11
    • Nichols MD, DeAngelis K, Keck JL, Berger JM. 1999. Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11. EMBO J. 18:6177-88
    • (1999) EMBO J. , vol.18 , pp. 6177-6188
    • Nichols, M.D.1    Deangelis, K.2    Keck, J.L.3    Berger, J.M.4
  • 126
    • 0035856473 scopus 로고    scopus 로고
    • Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC
    • O'Donnell M, Jeruzalmi D, Kuriyan J. 2001. Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC. Curr. Biol. 11:R935-46
    • (2001) Curr. Biol. , vol.11
    • O'Donnell, M.1    Jeruzalmi, D.2    Kuriyan, J.3
  • 127
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure-diverse function
    • + superfamily ATPases: common structure-diverse function. Genes Cells 6:575-97
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 130
    • 0034840471 scopus 로고    scopus 로고
    • Atomic structure of the clamp loader small subunit from Pyrococcus furiosus
    • Oyama T, Ishino Y, Cann IK, Ishino S, Morikawa K. 2001. Atomic structure of the clamp loader small subunit from Pyrococcus furiosus. Mol. Cell 8:455-63
    • (2001) Mol. Cell , vol.8 , pp. 455-463
    • Oyama, T.1    Ishino, Y.2    Cann, I.K.3    Ishino, S.4    Morikawa, K.5
  • 131
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel SS, Picha KM. 2000. Structure and function of hexameric helicases. Annu. Rev. Biochem. 69:651-97
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 133
    • 0032785122 scopus 로고    scopus 로고
    • The nature of the last universal common ancestor
    • Penny D, Poole A. 1999. The nature of the last universal common ancestor. Curr. Opin. Genet. Dev. 9:672-77
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 672-677
    • Penny, D.1    Poole, A.2
  • 135
    • 0034604383 scopus 로고    scopus 로고
    • Biochemical characterization of a clamp-loader complex homologous to eukaryotic replication factor C from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Pisani FM, De Felice M, Carpentieri F, Rossi M. 2000. Biochemical characterization of a clamp-loader complex homologous to eukaryotic replication factor C from the hyperthermophilic archaeon Sulfolobus solfataricus. J. Mol. Biol. 301:61-73
    • (2000) J. Mol. Biol. , vol.301 , pp. 61-73
    • Pisani, F.M.1    De Felice, M.2    Carpentieri, F.3    Rossi, M.4
  • 136
    • 0035965990 scopus 로고    scopus 로고
    • The zinc finger domain of the archaeal minichromosome maintenance protein is required for helicase activity
    • Poplawski A, Grabowski B, Long SE, Kelman Z. 2001. The zinc finger domain of the archaeal minichromosome maintenance protein is required for helicase activity. J. Biol. Chem. 276:49371-77
    • (2001) J. Biol. Chem. , vol.276 , pp. 49371-49377
    • Poplawski, A.1    Grabowski, B.2    Long, S.E.3    Kelman, Z.4
  • 137
    • 0031690990 scopus 로고    scopus 로고
    • Methanococcus jannaschii flap endonuclease: Expression, purification, and substrate requirements
    • Rao HG, Rosenfeld A, Wetmur JG. 1998. Methanococcus jannaschii flap endonuclease: expression, purification, and substrate requirements. J. Bacteriol. 180:5406-12
    • (1998) J. Bacteriol. , vol.180 , pp. 5406-5412
    • Rao, H.G.1    Rosenfeld, A.2    Wetmur, J.G.3
  • 138
    • 0034703051 scopus 로고    scopus 로고
    • The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9
    • Rauen M, Burtelow MA, Dufault VM, Karnitz LM. 2000. The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. J. Biol. Chem. 275:29767-71
    • (2000) J. Biol. Chem. , vol.275 , pp. 29767-29771
    • Rauen, M.1    Burtelow, M.A.2    Dufault, V.M.3    Karnitz, L.M.4
  • 139
    • 0038575389 scopus 로고    scopus 로고
    • Archaeal chromatin and transcription
    • Reeve JN. 2003. Archaeal chromatin and transcription. Mol. Microbiol. 48:587-98
    • (2003) Mol. Microbiol. , vol.48 , pp. 587-598
    • Reeve, J.N.1
  • 140
    • 0034595517 scopus 로고    scopus 로고
    • Crystal structure of a pol α family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9°N-7
    • Rodriguez AC, Park HW, Mao C, Beese LS. 2000. Crystal structure of a pol α family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9°N-7. J. Mol. Biol. 299:447-62
    • (2000) J. Mol. Biol. , vol.299 , pp. 447-462
    • Rodriguez, A.C.1    Park, H.W.2    Mao, C.3    Beese, L.S.4
  • 141
    • 0036470564 scopus 로고    scopus 로고
    • Crystal structure of reverse gyrase: Insights into the positive supercoiling of DNA
    • Rodriguez AC, Stock D. 2002. Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA. EMBO J. 21:418-26
    • (2002) EMBO J. , vol.21 , pp. 418-426
    • Rodriguez, A.C.1    Stock, D.2
  • 142
    • 0031897521 scopus 로고    scopus 로고
    • High-affinity binding sites for the initiator protein DnaA on the chromosome of Escherichia coli
    • Roth A, Messer W. 1998. High-affinity binding sites for the initiator protein DnaA on the chromosome of Escherichia coli. Mol. Microbiol. 28:395-401
    • (1998) Mol. Microbiol. , vol.28 , pp. 395-401
    • Roth, A.1    Messer, W.2
  • 143
    • 0034011209 scopus 로고    scopus 로고
    • Structure and functional relationships of archaeal and eukaryal histones and nucleosomes
    • Sandman K, Reeve JN. 2000. Structure and functional relationships of archaeal and eukaryal histones and nucleosomes. Arch. Microbiol. 173:165-69
    • (2000) Arch. Microbiol. , vol.173 , pp. 165-169
    • Sandman, K.1    Reeve, J.N.2
  • 145
    • 0035930346 scopus 로고    scopus 로고
    • Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication
    • Schwacha A, Bell SP. 2001. Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication. Mol. Cell 8:1093-104
    • (2001) Mol. Cell , vol.8 , pp. 1093-1104
    • Schwacha, A.1    Bell, S.P.2
  • 147
    • 0037109208 scopus 로고    scopus 로고
    • Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus
    • Seybert A, Scott DJ, Scaife S, Singleton MR, Wigley DB. 2002. Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus. Nucleic Acids Res. 30:4329-38
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4329-4338
    • Seybert, A.1    Scott, D.J.2    Scaife, S.3    Singleton, M.R.4    Wigley, D.B.5
  • 148
    • 0034686021 scopus 로고    scopus 로고
    • The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum ΔH minichromosome maintenance protein
    • Shechter DF, Ying CY, Gautier J. 2000. The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum ΔH minichromosome maintenance protein. J. Biol. Chem. 275:15049-59
    • (2000) J. Biol. Chem. , vol.275 , pp. 15049-15059
    • Shechter, D.F.1    Ying, C.Y.2    Gautier, J.3
  • 149
    • 0032077438 scopus 로고    scopus 로고
    • Flap endonuclease homologs in archaebacteria exist as independent proteins
    • Shen B, Qiu J, Hosfield D, Tainer JA. 1998. Flap endonuclease homologs in archaebacteria exist as independent proteins. Trends Biochem. Sci. 23:171-73
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 171-173
    • Shen, B.1    Qiu, J.2    Hosfield, D.3    Tainer, J.A.4
  • 150
    • 0035920137 scopus 로고    scopus 로고
    • Invariant Asp-1122 and Asp-1124 are essential residues for polymerization catalysis of family D DNA polymerase from Pyrococcus horikoshii
    • Shen Y, Musti K, Hiramoto M, Kikuchi H, Kawarabayashi Y, Matsui I. 2001. Invariant Asp-1122 and Asp-1124 are essential residues for polymerization catalysis of family D DNA polymerase from Pyrococcus horikoshii. J. Biol. Chem. 276:27376-83
    • (2001) J. Biol. Chem. , vol.276 , pp. 27376-27383
    • Shen, Y.1    Musti, K.2    Hiramoto, M.3    Kikuchi, H.4    Kawarabayashi, Y.5    Matsui, I.6
  • 151
    • 0034209827 scopus 로고    scopus 로고
    • Characterization of an ATP-dependent DNA ligase from the thermophilic archaeon Methanobacterium thermoautotrophicum
    • Sriskanda V, Kelman Z, Hurwitz J, Shuman S. 2000. Characterization of an ATP-dependent DNA ligase from the thermophilic archaeon Methanobacterium thermoautotrophicum. Nucleic Acids Res. 28:2221-28
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2221-2228
    • Sriskanda, V.1    Kelman, Z.2    Hurwitz, J.3    Shuman, S.4
  • 152
    • 0032881250 scopus 로고    scopus 로고
    • MCM proteins in DNA replication
    • Tye BK. 1999. MCM proteins in DNA replication. Annu. Rev. Biochem. 68:649-86
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 649-686
    • Tye, B.K.1
  • 153
    • 0031196901 scopus 로고    scopus 로고
    • A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: Gene cloning, expression, and characterization
    • Uemori T, Sato Y, Kato I, Doi H, Ishino Y. 1997. A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: gene cloning, expression, and characterization. Genes Cells 2:499-512
    • (1997) Genes Cells , vol.2 , pp. 499-512
    • Uemori, T.1    Sato, Y.2    Kato, I.3    Doi, H.4    Ishino, Y.5
  • 154
    • 0034235463 scopus 로고    scopus 로고
    • Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes
    • Venclovas C, Thelen MP. 2000. Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes. Nucleic Acids Res. 28:2481-93
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2481-2493
    • Venclovas, C.1    Thelen, M.P.2
  • 155
    • 0037523309 scopus 로고    scopus 로고
    • The diverse spectrum of sliding clamp interacting proteins
    • In press
    • Vivona JB, Kelman Z. 2003. The diverse spectrum of sliding clamp interacting proteins. FEBS Lett. In press
    • (2003) FEBS Lett.
    • Vivona, J.B.1    Kelman, Z.2
  • 156
    • 0035865799 scopus 로고    scopus 로고
    • Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus
    • Wadsworth RI, White MF. 2001. Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus. Nucleic Acids Res. 29:914-20
    • (2001) Nucleic Acids Res. , vol.29 , pp. 914-920
    • Wadsworth, R.I.1    White, M.F.2
  • 157
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69
    • Wang J, Sattar AK, Wang CC, Karam JD, Konigsberg WH, Steitz TA. 1997. Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69. Cell 89:1087-99
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 159
  • 160
    • 0001271789 scopus 로고
    • Phylogenetic structure of the prokaryotic domain: The primary kingdoms
    • Woese CR, Fox GE. 1977. Phylogenetic structure of the prokaryotic domain: the primary kingdoms. Proc. Natl. Acad. Sci. USA 74:5088-90
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5088-5090
    • Woese, C.R.1    Fox, G.E.2
  • 161
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese CR, Kandler O, Wheelis ML. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. USA 87:4576-79
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 162
    • 0029678248 scopus 로고    scopus 로고
    • Clamp loading, unloading and intrinsic stability of the PCNA, β and gp45 sliding clamps of human, E. coli and T4 replicases
    • Yao N, Turner J, Kelman Z, Stukenberg PT, Dean F, et al. 1996. Clamp loading, unloading and intrinsic stability of the PCNA, β and gp45 sliding clamps of human, E. coli and T4 replicases. Genes Cells 1:101-13
    • (1996) Genes Cells , vol.1 , pp. 101-113
    • Yao, N.1    Turner, J.2    Kelman, Z.3    Stukenberg, P.T.4    Dean, F.5
  • 163
    • 0036668640 scopus 로고    scopus 로고
    • The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings
    • Yu X, VanLoock MS, Poplawski A, Kelman Z, Xiang T, et al. 2002. The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings. EMBO Rep. 3:792-97
    • (2002) EMBO Rep. , vol.3 , pp. 792-797
    • Yu, X.1    VanLoock, M.S.2    Poplawski, A.3    Kelman, Z.4    Xiang, T.5
  • 164
    • 0033230401 scopus 로고    scopus 로고
    • Multiple competition reactions for RPA order the assembly of the DNA polymerase δ holoenzyme
    • Yuzhakov A, Kelman Z, Hurwitz J, O'Donnell M. 1999. Multiple competition reactions for RPA order the assembly of the DNA polymerase δ holoenzyme. EMBO J. 18:6189-99
    • (1999) EMBO J. , vol.18 , pp. 6189-6199
    • Yuzhakov, A.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4
  • 165
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA - A three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov A, Kelman Z, O'Donnell M. 1999. Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96:153-63
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 166
    • 0037459196 scopus 로고    scopus 로고
    • Multiple replication origins of the archaeon Halobacterium species NRC-1
    • Zhang R, Zhang C-T. 2003. Multiple replication origins of the archaeon Halobacterium species NRC-1. Biochem. Biophys. Res. Comm. 302:728-34
    • (2003) Biochem. Biophys. Res. Comm. , vol.302 , pp. 728-734
    • Zhang, R.1    Zhang, C.-T.2
  • 168
    • 0036567231 scopus 로고    scopus 로고
    • Pyrococcus genome comparison evidences chromosome shuffling-driven evolution
    • Zivanovic Y, Lopez P, Philippe H, Forterre P. 2002. Pyrococcus genome comparison evidences chromosome shuffling-driven evolution. Nucleic Acids Res. 30:1902-10
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1902-1910
    • Zivanovic, Y.1    Lopez, P.2    Philippe, H.3    Forterre, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.