메뉴 건너뛰기




Volumn 22, Issue 1, 1998, Pages 1-5

Multiprotein reactions in mammalian DNA replication

Author keywords

DNA synthesome; FEN1 RTH1; Junction ribonuclease; Mammalian DNA replication; Okazaki fragment; RNase HI

Indexed keywords

DNA FRAGMENT; DNA SYNTHESOME; PROTEIN; RIBONUCLEASE; RIBONUCLEASE H; UNCLASSIFIED DRUG;

EID: 0031980662     PISSN: 01452126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0145-2126(97)00113-6     Document Type: Note
Times cited : (13)

References (34)
  • 1
    • 0029807797 scopus 로고    scopus 로고
    • Once and only once upon a time: specifying and regulating origins of DNA replication in eukaryotic cells
    • J.F. Diffley Once and only once upon a time: specifying and regulating origins of DNA replication in eukaryotic cells Genes and Development 10 1996 2819
    • (1996) Genes and Development , vol.10 , pp. 2819
    • Diffley, J.F.1
  • 2
    • 0029810269 scopus 로고    scopus 로고
    • Cell cycle control of DNA replication
    • B. Stillman Cell cycle control of DNA replication Science 274 1996 1659
    • (1996) Science , vol.274 , pp. 1659
    • Stillman, B.1
  • 3
    • 0026607331 scopus 로고
    • ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex
    • S.P. Bell B. Stillman ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex Nature 357 1992 128
    • (1992) Nature , vol.357 , pp. 128
    • Bell, S.P.1    Stillman, B.2
  • 4
    • 0031054051 scopus 로고    scopus 로고
    • Enzymes and reactions at the eukaryotic DNA replication fork
    • R.A. Bambara R.S. Murante L.A. Henricksen Enzymes and reactions at the eukaryotic DNA replication fork J. Biol. Chem. 272 1997 4647
    • (1997) J. Biol. Chem. , vol.272 , pp. 4647
    • Bambara, R.A.1    Murante, R.S.2    Henricksen, L.A.3
  • 5
    • 0025826051 scopus 로고
    • Eukaryotic DNA polymerases
    • T.S. Wang Eukaryotic DNA polymerases Annu. Rev. Biochem. 60 1991 513
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 513
    • Wang, T.S.1
  • 6
    • 0028337685 scopus 로고
    • Anatomy of a DNA replication fork revealed by reconstitution of SV40 DNA replication in vitro
    • S. Waga B. Stillman Anatomy of a DNA replication fork revealed by reconstitution of SV40 DNA replication in vitro Nature 369 1994 207
    • (1994) Nature , vol.369 , pp. 207
    • Waga, S.1    Stillman, B.2
  • 7
    • 0025967720 scopus 로고
    • Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase alpha and delta during initiation of leading and lagging strand synthesis
    • T. Tsurimoto B. Stillman Replication factors required for SV40 DNA replication in vitro . II. Switching of DNA polymerase alpha and delta during initiation of leading and lagging strand synthesis J. Biol. Chem. 266 1991 1961
    • (1991) J. Biol. Chem. , vol.266 , pp. 1961
    • Tsurimoto, T.1    Stillman, B.2
  • 8
    • 0025328320 scopus 로고
    • Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin
    • T. Tsurimoto T. Melendy B. Stillman Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin Nature 346 1990 534
    • (1990) Nature , vol.346 , pp. 534
    • Tsurimoto, T.1    Melendy, T.2    Stillman, B.3
  • 9
    • 0028363546 scopus 로고
    • Reconstitution of complete SV40 DNA replication with purified replication factors
    • S. Waga G. Bauer B. Stillman Reconstitution of complete SV40 DNA replication with purified replication factors J. Biol. Chem. 269 1994 10923
    • (1994) J. Biol. Chem. , vol.269 , pp. 10923
    • Waga, S.1    Bauer, G.2    Stillman, B.3
  • 10
    • 0026701992 scopus 로고
    • Assembly of simian virus 40 Okazaki pieces from DNA primers is reversibly arrested by ATP depletion
    • T. Nethanel T. Zlotkin G. Kaufmann Assembly of simian virus 40 Okazaki pieces from DNA primers is reversibly arrested by ATP depletion J. Virol. 66 1992 6634
    • (1992) J. Virol. , vol.66 , pp. 6634
    • Nethanel, T.1    Zlotkin, T.2    Kaufmann, G.3
  • 11
    • 0027937802 scopus 로고
    • Enzymatic completion of mammalian lagging-strand DNA replication
    • J.J. Turchi L. Huang R.S. Murante Y. Kim R.A. Bambara Enzymatic completion of mammalian lagging-strand DNA replication 5th edn. Proc. Natl. Acad. Sci. U.S.A. 91 1994 9803
    • (1994) , pp. 9803
    • Turchi, J.J.1    Huang, L.2    Murante, R.S.3    Kim, Y.4    Bambara, R.A.5
  • 12
    • 0027201098 scopus 로고
    • Completion of mammalian lagging strand DNA replication using purified proteins
    • J.J. Turchi R.A. Bambara Completion of mammalian lagging strand DNA replication using purified proteins J. Biol. Chem. 268 1993 15136
    • (1993) J. Biol. Chem. , vol.268 , pp. 15136
    • Turchi, J.J.1    Bambara, R.A.2
  • 13
    • 0030929389 scopus 로고    scopus 로고
    • The isolation of a DNA synthesome from human leukemia cells
    • S. Lin R.J. Hickey L.H. Malkas The isolation of a DNA synthesome from human leukemia cells Leuk. Res. 21 1997 501 512
    • (1997) Leuk. Res. , vol.21 , pp. 501-512
    • Lin, S.1    Hickey, R.J.2    Malkas, L.H.3
  • 14
    • 0022400811 scopus 로고
    • Interaction of ribonuclease H from Drosophila melanogaster embryos with DNA polymerase-primase
    • R.A. DiFrancesco I.R. Lehman Interaction of ribonuclease H from Drosophila melanogaster embryos with DNA polymerase-primase J. Biol. Chem. 260 1985 14764
    • (1985) J. Biol. Chem. , vol.260 , pp. 14764
    • DiFrancesco, R.A.1    Lehman, I.R.2
  • 15
    • 0000992952 scopus 로고
    • Physical association of a dNA polymerase stimulating activity with a ribonuclease H purified from yeast
    • R. Karwan H. Blutsch U. Wintersberger Physical association of a dNA polymerase stimulating activity with a ribonuclease H purified from yeast Biochemistry 22 1983 5500
    • (1983) Biochemistry , vol.22 , pp. 5500
    • Karwan, R.1    Blutsch, H.2    Wintersberger, U.3
  • 16
    • 0024380861 scopus 로고
    • A distinct form of ribonuclease H from calf thymus stimulates its homologous DNA-polymerase-alpha-primase complex
    • A. Hagemeier F. Grosse A distinct form of ribonuclease H from calf thymus stimulates its homologous DNA-polymerase-alpha-primase complex European Journal of Biochemistry 185 1989 621
    • (1989) European Journal of Biochemistry , vol.185 , pp. 621
    • Hagemeier, A.1    Grosse, F.2
  • 17
    • 0030999605 scopus 로고    scopus 로고
    • Synthesis of the mammalian telomere lagging strand in vitro
    • P.M. Reveal K.M. Henkels J.J. Turchi Synthesis of the mammalian telomere lagging strand in vitro J. Biol. Chem. 272 1997 11678
    • (1997) J. Biol. Chem. , vol.272 , pp. 11678
    • Reveal, P.M.1    Henkels, K.M.2    Turchi, J.J.3
  • 18
    • 0024270343 scopus 로고
    • Complete enzymatic synthesis of DNA containing the SV40 origin of replication
    • Y. Ishimi A. Claude P. Bullock J. Hurwitz Complete enzymatic synthesis of DNA containing the SV40 origin of replication J. Biol. Chem. 263 1988 19723
    • (1988) J. Biol. Chem. , vol.263 , pp. 19723
    • Ishimi, Y.1    Claude, A.2    Bullock, P.3    Hurwitz, J.4
  • 19
    • 85119805235 scopus 로고
    • R.J. Crouch M.L. Dirksen M. Linn R.J. Roberts Nucleases 1982 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 211
    • (1982) , pp. 211
    • Crouch, R.J.1    Dirksen, M.L.2
  • 20
    • 0025977588 scopus 로고
    • Discrimination between mammalian RNases H-1 and H-2
    • M. Goulian C.J. Heard Discrimination between mammalian RNases H-1 and H-2 Anal. Biochem. 192 1991 398
    • (1991) Anal. Biochem. , vol.192 , pp. 398
    • Goulian, M.1    Heard, C.J.2
  • 21
    • 0027988074 scopus 로고
    • Structure-specific cleavage of the RNA primer from Okazaki fragments by calf thymus RNase HI
    • L. Huang Y. Kim J.J. Turchi R.A. Bambara Structure-specific cleavage of the RNA primer from Okazaki fragments by calf thymus RNase HI J. Biol. Chem. 269 1994 25922
    • (1994) J. Biol. Chem. , vol.269 , pp. 25922
    • Huang, L.1    Kim, Y.2    Turchi, J.J.3    Bambara, R.A.4
  • 22
    • 0027213005 scopus 로고
    • Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA
    • P.S. Eder R.Y. Walder J.A. Walder Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA Biochimie 75 1993 123
    • (1993) Biochimie , vol.75 , pp. 123
    • Eder, P.S.1    Walder, R.Y.2    Walder, J.A.3
  • 23
    • 0026738799 scopus 로고
    • A 5′ to 3′ exonuclease functionally interacts with calf DNA polymerase epsilon
    • G. Siegal J.J. Turchi T.W. Myers R.A. Bambara A 5′ to 3′ exonuclease functionally interacts with calf DNA polymerase epsilon 5th edn. Proc. Natl. Acad. Sci. U.S.A. 89 1992 9377
    • (1992) , pp. 9377
    • Siegal, G.1    Turchi, J.J.2    Myers, T.W.3    Bambara, R.A.4
  • 24
    • 0028034508 scopus 로고
    • Structural and functional homology between mammalian DNase IV and the 5′-nuclease domain of Escherichia coli DNA polymerase I
    • P. Robins D.J. Pappin R.D. Wood T. Lindahl Structural and functional homology between mammalian DNase IV and the 5′-nuclease domain of Escherichia coli DNA polymerase I J. Biol. Chem. 269 1994 28535
    • (1994) J. Biol. Chem. , vol.269 , pp. 28535
    • Robins, P.1    Pappin, D.J.2    Wood, R.D.3    Lindahl, T.4
  • 26
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • J.J. Harrington M.R. Lieber The characterization of a mammalian DNA structure-specific endonuclease EMBO J. 13 1994 1235
    • (1994) EMBO J. , vol.13 , pp. 1235
    • Harrington, J.J.1    Lieber, M.R.2
  • 27
    • 0028089040 scopus 로고
    • The calf 5′- to 3′-exonuclease is also an endonuclease with both activities dependent on primers annealed upstream of the point of cleavage
    • R.S. Murante L. Huang J.J. Turchi R.A. Bambara The calf 5′- to 3′-exonuclease is also an endonuclease with both activities dependent on primers annealed upstream of the point of cleavage J. Biol. Chem. 269 1994 1191
    • (1994) J. Biol. Chem. , vol.269 , pp. 1191
    • Murante, R.S.1    Huang, L.2    Turchi, J.J.3    Bambara, R.A.4
  • 28
    • 0029938728 scopus 로고    scopus 로고
    • Role of calf RTH-1 nuclease in removal of 5′-ribonucleotides during Okazaki fragment processing
    • L. Huang J.A. Rumbaugh R.S. Murante R.J.R. Lin L. Rust R.A. Bambara Role of calf RTH-1 nuclease in removal of 5′-ribonucleotides during Okazaki fragment processing Biochemistry 35 1996 9266
    • (1996) Biochemistry , vol.35 , pp. 9266
    • Huang, L.1    Rumbaugh, J.A.2    Murante, R.S.3    Lin, R.J.R.4    Rust, L.5    Bambara, R.A.6
  • 29
    • 0029616338 scopus 로고
    • Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage
    • R.S. Murante L. Rust R.A. Bambara Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage J. Biol. Chem. 270 1995 30377
    • (1995) J. Biol. Chem. , vol.270 , pp. 30377
    • Murante, R.S.1    Rust, L.2    Bambara, R.A.3
  • 30
  • 31
    • 0029959104 scopus 로고    scopus 로고
    • Calf RTH1 nuclease can remove the initiator RNAs of Okazaki fragments by endonuclease activity
    • R.S. Murante J.A. Rumbaugh C.J. Barnes J.R. Norton R.A. Bambara Calf RTH1 nuclease can remove the initiator RNAs of Okazaki fragments by endonuclease activity J. Biol. Chem. 271 1996 25888
    • (1996) J. Biol. Chem. , vol.271 , pp. 25888
    • Murante, R.S.1    Rumbaugh, J.A.2    Barnes, C.J.3    Norton, J.R.4    Bambara, R.A.5
  • 32
    • 0030002197 scopus 로고    scopus 로고
    • A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease
    • T.A. Ceska J.R. Sayers G. Stier D. Suck A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease Nature 382 1996 90
    • (1996) Nature , vol.382 , pp. 90
    • Ceska, T.A.1    Sayers, J.R.2    Stier, G.3    Suck, D.4
  • 34
    • 0031442653 scopus 로고    scopus 로고
    • A novel mutation avoidance mechanism dependent on S. cerevisiae RAD27 is distinct from DNA mismatch repair
    • D.X. Tishkoff N. Filosi G.M. Gaida R.D. Kolodner A novel mutation avoidance mechanism dependent on S. cerevisiae RAD27 is distinct from DNA mismatch repair Cell 88 1997 253
    • (1997) Cell , vol.88 , pp. 253
    • Tishkoff, D.X.1    Filosi, N.2    Gaida, G.M.3    Kolodner, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.