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Volumn 32, Issue 8, 2004, Pages 2430-2440

Characterization of the 3′ exonuclease subunit DP1 of Methanococcus jannaschii replicative DNA polymerase D

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; CALCINEURIN; DNA POLYMERASE; EXONUCLEASE; PHOSPHATASE; ARCHAEAL PROTEIN; DEOXYRIBONUCLEASE; DNA DIRECTED DNA POLYMERASE; EXODEOXYRIBONUCLEASE; MAGNESIUM; MRE11 PROTEIN, ARCHAEAL; PROTEIN SUBUNIT;

EID: 2342597828     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh558     Document Type: Article
Times cited : (29)

References (43)
  • 3
    • 0031587829 scopus 로고    scopus 로고
    • Archaea and the origin(s) of DNA replication proteins
    • Edgell,D.R. and Doolittle,W.F. (1997) Archaea and the origin(s) of DNA replication proteins. Cell, 89, 995-998.
    • (1997) Cell , vol.89 , pp. 995-998
    • Edgell, D.R.1    Doolittle, W.F.2
  • 4
    • 0032745320 scopus 로고    scopus 로고
    • Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea
    • Cann,I.K.O., Ishino,S., Hayashi.,I, Komori,K., Toh,H., Morikawa,K. and Ishino,Y. (1999) Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea. J. Bacteriol., 181, 6591-6599.
    • (1999) J. Bacteriol. , vol.181 , pp. 6591-6599
    • Cann, I.K.O.1    Ishino, S.2    Hayashi, I.3    Komori, K.4    Toh, H.5    Morikawa, K.6    Ishino, Y.7
  • 5
    • 1542682737 scopus 로고    scopus 로고
    • Archael DNA replication: Eukaryal proteins in a bacterial context
    • Grabowski,B. and Kelman,Z. (2003) Archael DNA replication: eukaryal proteins in a bacterial context. Annu. Rev. Microbiol., 57, 487-516.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 487-516
    • Grabowski, B.1    Kelman, Z.2
  • 6
    • 0032564361 scopus 로고    scopus 로고
    • A heterodimeric DNA polymerase: Evidence that members of Euryarchaeota possess a distinct DNA polymerase
    • Cann,I.K.O., Komori,K., Toh,H., Kanai,S. and Ishino,Y. (1998) A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase. Proc. Natl Acad. Sci. USA, 95, 14250-14255.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14250-14255
    • Cann, I.K.O.1    Komori, K.2    Toh, H.3    Kanai, S.4    Ishino, Y.5
  • 7
    • 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. and 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
  • 8
    • 0031922356 scopus 로고    scopus 로고
    • A novel DNA polymerase family found in Archaea
    • Ishino,Y., Komori,K., Cann,I.K.O. and Koga,Y. (1998) A novel DNA polymerase family found in Archaea. J. Bacteriol., 180, 2232-2236.
    • (1998) J. Bacteriol. , vol.180 , pp. 2232-2236
    • Ishino, Y.1    Komori, K.2    Cann, I.K.O.3    Koga, Y.4
  • 9
    • 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. and 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, 27376-27383.
    • (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
  • 10
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • Aravind,L. and Koonin,E.V. (1998) Phosphoesterase domains associated with DNA polymerases of diverse origins. Nucleic Acids Res., 26, 3746-3752.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 12
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg,J., Huang,H.B., Kwon,Y.G., Greengard,P., Nairn,A.C. and Kuriyan,J. (1995) Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature, 376, 745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 13
    • 0029645578 scopus 로고
    • Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1
    • Lohse,D.L., Denu,J.M. and Dixon,J.E. (1995) Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1. Structure, 3, 987-990.
    • (1995) Structure , vol.3 , pp. 987-990
    • Lohse, D.L.1    Denu, J.M.2    Dixon, J.E.3
  • 15
    • 0002835799 scopus 로고    scopus 로고
    • Isolation of peptides for microsequencing by in-gel proteolytic digestion
    • Kamp,R.M., Choli-Papadopoulou,T. and Wittmann-Liebold,B. (eds), Springer-Verlag, Heidelberg, Germany
    • Hellman,U. (1997) Isolation of peptides for microsequencing by in-gel proteolytic digestion. In Kamp,R.M., Choli-Papadopoulou,T. and Wittmann-Liebold,B. (eds), Protein Structure Analysis. Preparation, Characterization and Microsequencing. Springer-Verlag, Heidelberg, Germany, pp. 97-104.
    • (1997) Protein Structure Analysis. Preparation, Characterization and Microsequencing , pp. 97-104
    • Hellman, U.1
  • 17
    • 0032415809 scopus 로고    scopus 로고
    • The euryarchaeotes, a subdomain of Archaea, survive on a single DNA polymerase: Fact or farce?
    • Ishino,Y. and Cann,I.K.O. (1998) The euryarchaeotes, a subdomain of Archaea, survive on a single DNA polymerase: fact or farce? Genes Genet. Syst., 73, 323-336.
    • (1998) Genes Genet. Syst. , vol.73 , pp. 323-336
    • Ishino, Y.1    Cann, I.K.O.2
  • 18
    • 0035906860 scopus 로고    scopus 로고
    • Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase
    • Hopfner,K.-P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and Tainer,J.A. (2001) Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Cell, 105, 473-485.
    • (2001) Cell , vol.105 , pp. 473-485
    • Hopfner, K.-P.1    Karcher, A.2    Craig, L.3    Woo, T.T.4    Carney, J.P.5    Tainer, J.A.6
  • 19
    • 0032931844 scopus 로고    scopus 로고
    • The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance
    • Moreau,S., Ferguson,J.R. and Symington,L.S. (1999) The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance. Mol. Cell. Biol., 19, 556-566.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 556-566
    • Moreau, S.1    Ferguson, J.R.2    Symington, L.S.3
  • 20
  • 21
    • 0032747634 scopus 로고    scopus 로고
    • Molecular architecture of the mouse DNA polymerase alpha-primase complex
    • Mizuno,T., Yamagishi,K., Miyazawa,H. and Hanaoka,F. (1999) Molecular architecture of the mouse DNA polymerase alpha-primase complex. Mol. Cell. Biol., 19, 7886-7896.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7886-7896
    • Mizuno, T.1    Yamagishi, K.2    Miyazawa, H.3    Hanaoka, F.4
  • 22
    • 0037063331 scopus 로고    scopus 로고
    • Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180
    • Smith,R.W.P. and Nasheuer,H.-P. (2002) Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180. FEBS Lett., 527, 143-146.
    • (2002) FEBS Lett. , vol.527 , pp. 143-146
    • Smith, R.W.P.1    Nasheuer, H.-P.2
  • 23
    • 0030814759 scopus 로고    scopus 로고
    • Involvement of the yeast DNA polymerase δ in DNA repair in vivo
    • Giot,L., Chanet,R., Simon,M., Facca,C. and Faye,G. (1997) Involvement of the yeast DNA polymerase δ in DNA repair in vivo. Genetics, 146, 1239-1251.
    • (1997) Genetics , vol.146 , pp. 1239-1251
    • Giot, L.1    Chanet, R.2    Simon, M.3    Facca, C.4    Faye, G.5
  • 24
    • 0032491540 scopus 로고    scopus 로고
    • Role of the putative zinc finger domain of Saccharomyces cerevisiae DNA polymerase E in DNA replication and the S/M checkpoint pathway
    • Dua,R., Levy,D.L. and Campbell,J.L. (1998) Role of the putative zinc finger domain of Saccharomyces cerevisiae DNA polymerase E in DNA replication and the S/M checkpoint pathway. J. Biol. Chem., 273, 30046-30055.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30046-30055
    • Dua, R.1    Levy, D.L.2    Campbell, J.L.3
  • 25
    • 0034666148 scopus 로고    scopus 로고
    • Subunit interactions within the Saccharomyces cerevisiae DNA polymerase E (pol E) complex. Demonstration of a dimeric pol E
    • Dua,R., Edwards,S., Levy,D.L. and Campbell,J.L. (2000) Subunit interactions within the Saccharomyces cerevisiae DNA polymerase E (pol E) complex. Demonstration of a dimeric pol E. J. Biol. Chem., 275, 28816-28825.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28816-28825
    • Dua, R.1    Edwards, S.2    Levy, D.L.3    Campbell, J.L.4
  • 26
    • 0038079801 scopus 로고    scopus 로고
    • Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii
    • Shen,Y., Tang,X.-F. and Matsui,I. (2003) Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii. J. Biol. Chem., 278, 21247-21257.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21247-21257
    • Shen, Y.1    Tang, X.-F.2    Matsui, I.3
  • 28
    • 1242331846 scopus 로고    scopus 로고
    • A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulates its nuclease activity which is Mre11-like and prefers manganese ion as the cofactor
    • Shen,Y., Tang,X.-F., Yokoyama,H., Matsui,E. and Matsui,I. (2004) A 21-amino acid peptide from the cysteine. cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulates its nuclease activity which is Mre11-like and prefers manganese ion as the cofactor. Nucleic Acids Res., 32, 158-168.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 158-168
    • Shen, Y.1    Tang, X.-F.2    Yokoyama, H.3    Matsui, E.4    Matsui, I.5
  • 29
    • 0032476658 scopus 로고    scopus 로고
    • Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination
    • Furuse,M., Nagase,Y., Tsubouchi,H., Murakami-Murofushi,K., Shibata,T. and Ohta,K. (1998) Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination. EMBO J., 17, 6412-6425.
    • (1998) EMBO J. , vol.17 , pp. 6412-6425
    • Furuse, M.1    Nagase, Y.2    Tsubouchi, H.3    Murakami-Murofushi, K.4    Shibata, T.5    Ohta, K.6
  • 30
    • 0032555480 scopus 로고    scopus 로고
    • Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11 and p95
    • Trujillo,K.M., Yuan,S.-S.F., Lee,E.Y.-H.P. and Sung,P. (1998) Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11 and p95. J. Biol. Chem., 273, 21447-21450.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21447-21450
    • Trujillo, K.M.1    Yuan, S.-S.F.2    Lee, E.Y.-H.P.3    Sung, P.4
  • 31
    • 0030756165 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of the SbcCD protein from Eschericia coli
    • Connelly,J.C., de Leau,E.S., Okely,E.A. and Leach,D.R.F. (1997) Overexpression, purification and characterization of the SbcCD protein from Eschericia coli. J. Biol. Chem., 272, 19819-19826.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19819-19826
    • Connelly, J.C.1    de Leau, E.S.2    Okely, E.A.3    Leach, D.R.F.4
  • 32
    • 0033759543 scopus 로고    scopus 로고
    • Mre11 and Rad50 from Pyrococcus furiosus: Cloning and biochemical characterization reveal an evolutionary conserved multiprotein machinery
    • Hopfner,K.-P., Karcher,A., Shin,D., Fairley,C., Tainer,J.A. and Carney,J.P. (2000) Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionary conserved multiprotein machinery. J. Bacteriol., 182, 6036-6041.
    • (2000) J. Bacteriol. , vol.182 , pp. 6036-6041
    • Hopfner, K.-P.1    Karcher, A.2    Shin, D.3    Fairley, C.4    Tainer, J.A.5    Carney, J.P.6
  • 33
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker,J.P. (1991) Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem., 42, 1-76.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 34
    • 0024290491 scopus 로고
    • Exonucleolytic proofreading
    • Kunkel,T.A. (1988) Exonucleolytic proofreading. Cell, 53, 837-840.
    • (1988) Cell , vol.53 , pp. 837-840
    • Kunkel, T.A.1
  • 35
    • 0038690166 scopus 로고    scopus 로고
    • Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1
    • Wilson,D.M,3rd (2003) Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1. J. Mol. Biol., 330, 1027-1037.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1027-1037
    • Wilson III, D.M.1
  • 36
    • 0029794521 scopus 로고    scopus 로고
    • Kinetic mechanism of the 3′ → 5′ proofreading exonuclease of DNA polymerase III. Analysis by steady state and pre-steady state methods
    • Miller,H. and Perrino,F.W. (1996) Kinetic mechanism of the 3′ → 5′ proofreading exonuclease of DNA polymerase III. Analysis by steady state and pre-steady state methods. Biochemistry, 35, 12919-12925.
    • (1996) Biochemistry , vol.35 , pp. 12919-12925
    • Miller, H.1    Perrino, F.W.2
  • 37
    • 0033199713 scopus 로고    scopus 로고
    • Did DNA replication evolve twice independently?
    • Leipe,D.D., Aravind,L. and Koonin,E.V. (1999) Did DNA replication evolve twice independently? Nucleic Acids Res., 27, 3389-3401.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3389-3401
    • Leipe, D.D.1    Aravind, L.2    Koonin, E.V.3
  • 38
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin,A.G. (1993) OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 39
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: A snapshot of the evolution of sequence, structure and function
    • Arcus,V. (2002) OB-fold domains: a snapshot of the evolution of sequence, structure and function. Curr. Opin. Struct. Biol., 12, 794-801.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 794-801
    • Arcus, V.1
  • 40
    • 0038473989 scopus 로고    scopus 로고
    • OB-fold: Growing bigger with functional consistency
    • Agrawal,V. and Kishan,K.V.R. (2003) OB-fold: growing bigger with functional consistency. Curr. Protein Pept. Sci.,. 4, 195-206.
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 195-206
    • Agrawal, V.1    Kishan, K.V.R.2
  • 43
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • 127-128
    • Evans,S.V. (1993) SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph., 11, 134-138, 127-128.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1


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