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Volumn 585, Issue 3, 2011, Pages 452-458

Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii

Author keywords

Binding domain; D family DNA polymerase; DNA replication; Hyperthermophilic archaea; Molecular structure; Pyrococcus

Indexed keywords

ARCHAEAL DNA; DNA DIRECTED DNA POLYMERASE; DNA DIRECTED DNA POLYMERASE D; EXONUCLEASE; UNCLASSIFIED DRUG;

EID: 79551469840     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.040     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0031922356 scopus 로고    scopus 로고
    • A novel DNA polymerase family found in Archaea
    • Y. Ishino, K. Komori, I.K. Cann, and Y. Koga A novel DNA polymerase family found in Archaea J. Bacteriol. 180 1998 2232 2236
    • (1998) J. Bacteriol. , vol.180 , pp. 2232-2236
    • Ishino, Y.1    Komori, K.2    Cann, I.K.3    Koga, Y.4
  • 3
    • 65349186567 scopus 로고    scopus 로고
    • Evolution of DNA polymerases: An inactivated polymerase-exonuclease module in Pol and a chimeric origin of eukaryotic polymerases from two classes of archaeal ancestors
    • T.H. Tahirov, K.S. Makarova, I.B. Rogozin, Y.I. Pavlov, and E.V. Koonin Evolution of DNA polymerases: an inactivated polymerase-exonuclease module in Pol and a chimeric origin of eukaryotic polymerases from two classes of archaeal ancestors Biol. Direct 4 2009 11
    • (2009) Biol. Direct , vol.4 , pp. 11
    • Tahirov, T.H.1    Makarova, K.S.2    Rogozin, I.B.3    Pavlov, Y.I.4    Koonin, E.V.5
  • 4
    • 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
    • Y. Shen, K. Musti, M. Hiramoto, H. Kikuchi, Y. Kawarabayasi, and I. Matsui Invariant Asp-1122 and Asp-1124 are essential residues for polymerization catalysis of family D DNA polymerase from Pyrococcus horikoshii J. Biol. Chem. 276 2001 27376 27383
    • (2001) J. Biol. Chem. , vol.276 , pp. 27376-27383
    • Shen, Y.1    Musti, K.2    Hiramoto, M.3    Kikuchi, H.4    Kawarabayasi, Y.5    Matsui, I.6
  • 5
    • 1242331846 scopus 로고    scopus 로고
    • A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulate its nuclease activity which is Mre-11-like and prefers manganese ion as the cofactor
    • Y. Shen, X. Tang, H. Yokoyama, E. Matsui, and I. Matsui A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulate its nuclease activity which is Mre-11-like and prefers manganese ion as the cofactor Nucleic Acids Res. 32 2004 158 168
    • (2004) Nucleic Acids Res. , vol.32 , pp. 158-168
    • Shen, Y.1    Tang, X.2    Yokoyama, H.3    Matsui, E.4    Matsui, I.5
  • 6
    • 0031196901 scopus 로고    scopus 로고
    • A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: Gene cloning, expression, and characterization
    • T. Uemori, Y. Sato, I. Kato, H. Doi, and Y. Ishino A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: gene cloning, expression, and characterization Genes Cells 2 1997 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
  • 7
    • 0038079801 scopus 로고    scopus 로고
    • Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii
    • Y. Shen, X. Tang, and I. Matsui Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii J. Biol. Chem. 278 2003 21247 21257
    • (2003) J. Biol. Chem. , vol.278 , pp. 21247-21257
    • Shen, Y.1    Tang, X.2    Matsui, I.3
  • 8
    • 0022273106 scopus 로고
    • 15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type
    • 15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type Biochemistry 24 1985 7263 7268
    • (1985) Biochemistry , vol.24 , pp. 7263-7268
    • Lemaster, D.M.1    Richards, F.M.2
  • 9
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 11
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods
    • E. De la Fortelle, and G. Bricogne Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D 50 1994 760 763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 13
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 6 1999 458 463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 15
    • 4644250659 scopus 로고    scopus 로고
    • Domain topology of the DNA polymerase D complex from hyperthermophilic archaeon Pyrococcus horikoshii
    • X. Tang, Y. Shen, E. Matsui, and I. Matsui Domain topology of the DNA polymerase D complex from hyperthermophilic archaeon Pyrococcus horikoshii Biochemistry 43 2004 11818 11827
    • (2004) Biochemistry , vol.43 , pp. 11818-11827
    • Tang, X.1    Shen, Y.2    Matsui, E.3    Matsui, I.4
  • 17
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D 60 2004 2256 2268
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 19
    • 0028959773 scopus 로고
    • Circular dichroism
    • R.W. Woody Circular dichroism Methods Enzymol. 246 1995 34 71
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 20
    • 0001755735 scopus 로고
    • The effect of temperature on the fluorescence of some aromatic amino acids and proteins
    • J.A. Gally, and G.M. Edelman The effect of temperature on the fluorescence of some aromatic amino acids and proteins Biochim. Biophys. Acta 60 1962 499 509
    • (1962) Biochim. Biophys. Acta , vol.60 , pp. 499-509
    • Gally, J.A.1    Edelman, G.M.2
  • 21
    • 0035967930 scopus 로고    scopus 로고
    • The DNA polymerase III holoenzyme: An asymmetric dimeric replicative complex with leading and lagging strand polymerases
    • B.P. Glove, and C.S. McHenry The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases Cell 105 2001 925 934
    • (2001) Cell , vol.105 , pp. 925-934
    • Glove, B.P.1    McHenry, C.S.2
  • 22
    • 0034666148 scopus 로고    scopus 로고
    • Subunit interactions within the Saccharomyces cerevisiae DNA polymerase epsilon (pol epsilon) complex. Demonstration of a dimeric pol epsilon
    • R. Dua, S. Edwards, D.L. Levy, and J.L. Campbell Subunit interactions within the Saccharomyces cerevisiae DNA polymerase epsilon (pol epsilon) complex. Demonstration of a dimeric pol epsilon J. Biol. Chem. 275 2000 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
  • 23
    • 77955268031 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerase
    • K. Yamasaki, Y. Urushibata, T. Yamasaki, F. Arisaka, and I. Matsui Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerase FEBS Lett. 584 2010 3370 3375
    • (2010) FEBS Lett. , vol.584 , pp. 3370-3375
    • Yamasaki, K.1    Urushibata, Y.2    Yamasaki, T.3    Arisaka, F.4    Matsui, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.