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Volumn 5, Issue 8, 1998, Pages 707-713

The crystal structure of flap endonuclease-1 from Methanococcus jannaschii

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DOUBLE STRANDED DNA; ENDONUCLEASE; FLAP ENDONUCLEASE 1; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 0031873411     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/1406     Document Type: Article
Times cited : (150)

References (35)
  • 1
    • 0028335180 scopus 로고
    • Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: Implications for nucleotide excision repair
    • Harrington, J. J. & Lieber, M. R. Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: Implications for nucleotide excision repair. Genes Dev. 8, 1344-1355 (1994).
    • (1994) Genes Dev , vol.8 , pp. 1344-1355
    • Harrington, J.J.1    Lieber, M.R.2
  • 2
    • 0028281443 scopus 로고
    • The characterization of a mammalian structurespecific DNA endonuclease
    • Harrington, J. J. & Lieber, M. R. The characterization of a mammalian structurespecific DNA endonuclease. EMBO J. 13, 1235-1246 (1994).
    • (1994) EMBO J , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 3
    • 0028034508 scopus 로고
    • Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of E. Coli DNA polymerase I
    • Robins, P., Pappin, D., Wood, R. D. & Lindahl, T. Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of E. coli DNA polymerase I. J. Biol. Chem. 269, 28535-28538 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 28535-28538
    • Robins, P.1    Pappin, D.2    Wood, R.D.3    Lindahl, T.4
  • 4
    • 0024270343 scopus 로고
    • Complete enzymatic synthesis of DNA containing the SV40 origin of replication
    • Ishimi, Y., Claude, A., Bullock, P. & Hurwitz, J. Complete enzymatic synthesis of DNA containing the SV40 origin of replication. J. Biol. Chem. 263, 19723-19733 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 19723-19733
    • Ishimi, Y.1    Claude, A.2    Bullock, P.3    Hurwitz, J.4
  • 5
    • 0028363546 scopus 로고
    • Reconstitution of complete SV40 DNA replication using purified proteins
    • Waga, S., Baue, G. & Stillman, B. Reconstitution of complete SV40 DNA replication using purified proteins. J. Biol. Chem. 269, 10923-10934 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 10923-10934
    • Waga, S.1    Baue, G.2    Stillman, B.3
  • 6
    • 0025017971 scopus 로고
    • Discontinuous DNA synthesis by purified mammalian proteins
    • Goulian, M., Richards, S. H., Heard, C. J. & Bigsby, B. M. Discontinuous DNA synthesis by purified mammalian proteins. J. Biol. Chem. 265, 18461-18471 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 18461-18471
    • Goulian, M.1    Richards, S.H.2    Heard, C.J.3    Bigsby, B.M.4
  • 7
    • 0029959104 scopus 로고    scopus 로고
    • Calf RTH1 nuclease can remove initiator RNAs of Okazaki fragments by endonuclease action
    • Murante, R. S., Rumbaugh, J. A., Barnes, C. J., Norton, J. R., Bambara, R. A. Calf RTH1 nuclease can remove initiator RNAs of Okazaki fragments by endonuclease action. J. Biol. Chem. 271, 25888-25897 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 25888-25897
    • Murante, R.S.1    Rumbaugh, J.A.2    Barnes, C.J.3    Norton, J.R.4    Bambara, R.A.5
  • 8
    • 0028947298 scopus 로고
    • Conditional lethality of null mutations in RTH1 that encodes the yeast counterpart of a mammalian 5' - to 3' exonuclease required for lagging strand DNA synthesis in reconstituted systems
    • Sommers, C. H., Miller, E. J., Dujon, B., Prakash, L. & Prakash, S. Conditional lethality of null mutations in RTH1 that encodes the yeast counterpart of a mammalian 5' - to 3' exonuclease required for lagging strand DNA synthesis in reconstituted systems. J. Biol. Chem. 270, 4193-4196 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 4193-4196
    • Sommers, C.H.1    Miller, E.J.2    Dujon, B.3    Prakash, L.4    Prakash, S.5
  • 9
    • 0347526845 scopus 로고
    • Completion of lagging strand DNA replication using purified proteins
    • Turchi, J. J. & Bambara, R. A. Completion of lagging strand DNA replication using purified proteins. J. Biol. Chem. 269, 1191-1196 (1993).
    • (1993) J. Biol. Chem. , vol.269 , pp. 1191-1196
    • Turchi, J.J.1    Bambara, R.A.2
  • 10
    • 0029092897 scopus 로고
    • Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by PCNA
    • Li, X., Li, J., Harrington, J. J., Lieber, M. R. & Burgers, P. M. J. Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by PCNA. J. Biol. Chem. 270, 22109-22112 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 22109-22112
    • Li, X.1    Li, J.2    Harrington, J.J.3    Lieber, M.R.4    Burgers, P.M.J.5
  • 11
    • 0029885134 scopus 로고    scopus 로고
    • Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA
    • Wu, X., Li, J., Li, X., Hsieh, C-L., Burgers, P. M. J. & Lieber, M. R. Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA. Nuc. Acids Res. 24, 2036-2043 (1996).
    • (1996) Nuc. Acids Res. , vol.24 , pp. 2036-2043
    • Wu, X.1    Li, J.2    Li, X.3    Hsieh, C.-L.4    Burgers, P.M.J.5    Lieber, M.R.6
  • 12
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN-1)
    • Klungland, A. & Lindahl, T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN-1). EMBO J. 16, 3341-3348 (1997).
    • (1997) EMBO J , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 13
    • 0029039868 scopus 로고
    • Requirement of the yeast RTH1 5' to 3' exonuclease for the stability of simple repetitive DNA
    • Johnson, R., Kovvali, G., Prakash, L. & Prakash, S. Requirement of the yeast RTH1 5' to 3' exonuclease for the stability of simple repetitive DNA. Science 269, 238-24 (1995).
    • (1995) Science , vol.269 , pp. 238-324
    • Johnson, R.1    Kovvali, G.2    Prakash, L.3    Prakash, S.4
  • 14
    • 0031442653 scopus 로고    scopus 로고
    • A novel mutation avoidance mechanim dependent on S. Cerevisiae RAD27 is distinct from DNA mismatch repair
    • Tishkoff, D. X., Fisoli, N., Gaida, N., Kolodner, R. D. A novel mutation avoidance mechanim dependent on S. cerevisiae RAD27 is distinct from DNA mismatch repair. Cell 88, 253-263 (1997).
    • (1997) Cell , vol.88 , pp. 253-263
    • Tishkoff, D.X.1    Fisoli, N.2    Gaida, N.3    Kolodner, R.D.4
  • 15
    • 0028813895 scopus 로고
    • Microsatellite instability in inherited and sporadic neoplasms
    • Eshleman, J. R. & Markowitz, S. D. Microsatellite instability in inherited and sporadic neoplasms.Curr. Opin. Oncol. 7, 83–89 (1995).
    • (1995) Curr. Opin. Oncol , vol.7 , pp. 83-89
    • Eshleman, J.R.1    Markowitz, S.D.2
  • 16
    • 0027255962 scopus 로고
    • Complementation of the DNA repair defect in xeroderma pigmentation group G cells by a human cDNA related to yeast RAD2
    • Scherly, D. et al. Complementation of the DNA repair defect in xeroderma pigmentation group G cells by a human cDNA related to yeast RAD2. Nature 363, 182-185 (1993).
    • (1993) Nature , vol.363 , pp. 182-185
    • Scherly, D.1
  • 17
    • 0022635503 scopus 로고
    • Nucleotide sequence, transcript mapping, and regulation of the rad2 gene of Saccharomyces cerevisiae
    • Madura, K., & Prakash, P. Nucleotide sequence, transcript mapping, and regulation of the rad2 gene of Saccharomyces cerevisiae. J. Bacteriol. 166, 914-923 (1986).
    • (1986) J. Bacteriol. , vol.166 , pp. 914-923
    • Madura, K.1    Prakash, P.2
  • 18
    • 0027215222 scopus 로고
    • Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerase
    • Nature Lyamichev, V., Brow, M. A. D. & Dahlberg, J. E. Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerase. Science 260, 778-783 (1993).
    • (1993) Science , vol.260 , pp. 778-783
    • Nature Lyamichev, V.1    Brow, M.A.D.2    Dahlberg, J.E.3
  • 19
    • 0027305444 scopus 로고
    • Conserved sites in the 5'-3' exonuclease domain of Escherichia coli DNA polymerase
    • Gutman, P. D. & Minton, K. W. Conserved sites in the 5'-3' exonuclease domain of Escherichia coli DNA polymerase. Nuc. Acids Res. 21, 4406-4407 (1993).
    • (1993) Nuc. Acids Res. , vol.21 , pp. 4406-4407
    • Gutman, P.D.1    Minton, K.W.2
  • 20
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim, Y et al. Crystal structure of Thermus aquaticus DNA polymerase. Nature 376, 612-616 (1995).
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1
  • 21
    • 0030002197 scopus 로고    scopus 로고
    • A helical arch allowing singlestranded DNA to thread through T5 5' exonuclease
    • Ceska, T. A., Sayers, J. R., Stier, G. & Suck, D. A helical arch allowing singlestranded DNA to thread through T5 5' exonuclease. Nature 382, 90-93 (1996).
    • (1996) Nature , vol.382 , pp. 90-93
    • Ceska, T.A.1    Sayers, J.R.2    Stier, G.3    Suck, D.4
  • 22
    • 0026030641 scopus 로고
    • Data base of homology derived protein structures and the structural meaning of sequence alignment
    • Sander, C. and Schneider, R. Data base of homology derived protein structures and the structural meaning of sequence alignment. Proteins Struct. Funct. Genet. 9, 56-68 (1991).
    • (1991) Proteins Struct. Funct. Genet. , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 23
    • 2142860722 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic protein
    • Mueser, T.C., Nossal, N.G. and Hyde, C. C. Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic protein. Cell 95, 1101-1112 (1996).
    • (1996) Cell , vol.95 , pp. 1101-1112
    • Mueser, T.C.1    Nossal, N.G.2    Hyde, C.C.3
  • 24
    • 0030666337 scopus 로고    scopus 로고
    • Prokaryotic 5'-3' exonucleases share a common core structure with gamma-delta resolvase
    • Artymiuk, P. J., Ceska, T. A., Suck, D. & Sayers, J. R. Prokaryotic 5'-3' exonucleases share a common core structure with gamma-delta resolvase. Nucleic Acids Res 25, 4224-4229 (1997).
    • (1997) Nucleic Acids Res , vol.25 , pp. 4224-4229
    • Artymiuk, P.J.1    Ceska, T.A.2    Suck, D.3    Sayers, J.R.4
  • 25
    • 0030872252 scopus 로고    scopus 로고
    • Functional analysis of point mutations in human flap endonuclease-1 active site
    • Shen, B., Nolan, J. P., Sklar, L. A. & Park, M. S. Functional analysis of point mutations in human flap endonuclease-1 active site. Nucleic Acids Res. 25, 3332-3338 (1997).
    • (1997) Nucleic Acids Res , vol.25 , pp. 3332-3338
    • Shen, B.1    Nolan, J.P.2    Sklar, L.A.3    Park, M.S.4
  • 26
    • 0026019625 scopus 로고
    • Structural basis for the 3'-5' exonuclease activity of Escherichia coli polymerase I: A two metal ion mechanism
    • Beese, L. S. & Steitz, T. A. Structural basis for the 3'-5' exonuclease activity of Escherichia coli polymerase I: a two metal ion mechanism. EMBO J. 10. 25-33 (1991).
    • (1991) EMBO J , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 27
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • Mol, C. D., Kuo, C. F., Thayer, M. M., Cunningham, R. P. & Tainer, J. A. Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature 374, 381-386 (1995).
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 28
    • 0029128447 scopus 로고
    • Identification of critical active site residues in the multifunctional human DNA repair enzyme HAP1
    • Barzilay, G. et al., Identification of critical active site residues in the multifunctional human DNA repair enzyme HAP1. Nature Struct Biol. 2, 562-567 (1995).
    • (1995) Nature Struct Biol , vol.2 , pp. 562-567
    • Barzilay, G.1
  • 29
    • 0029616338 scopus 로고
    • Calf 5' to 3' exoendonuclease must slide from 5' end of the substarte to perform structure-specific cleavage
    • Murante, R. S., Rust, L & Bambara, R. A. Calf 5' to 3' exoendonuclease must slide from 5' end of the substarte to perform structure-specific cleavage. J. Biol. Chem., 270, 30377-30383 (1995)
    • (1995) J. Biol. Chem. , vol.270 , pp. 30377-30383
    • Murante, R.S.1    Rust, L.2    Bambara, R.A.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z & Minor, W. Processing of x-ray diffraction data collected in oscillation mode. Meth. Enz. 276, 307-326 (1997).
    • (1997) Meth. Enz. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0028103275 scopus 로고
    • The CCP4 Suite: Program for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 Suite: Program for protein crystallography. Acta. Crystallogr. D50, 760-763 (1994).
    • (1994) Acta. Crystallogr. , vol.D50 , pp. 760-763
  • 32
    • 0000082544 scopus 로고
    • CHAIN: A crystallographic modelling program
    • Sack, J. S. CHAIN: a crystallographic modelling program. J. Molec. Graphics 6, 224-225 (1988).
    • (1988) J. Molec. Graphics , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 34
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0026319199 scopus 로고
    • Protein folding and association: Insight from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.