메뉴 건너뛰기




Volumn 35, Issue 2, 2004, Pages 248-256

Subunit protein-affinity isolation of Drosophila DNA polymerase ε catalytic subunit

Author keywords

Drosophila melanogaster DNA polymerases; Pol. catalytic subunit; Processivity; Proofreading 3 5 exonuclease activity; Protein purification

Indexed keywords

DROSOPHILA MELANOGASTER; MELANOGASTER;

EID: 2642569447     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.02.001     Document Type: Article
Times cited : (62)

References (24)
  • 1
    • 0035985037 scopus 로고    scopus 로고
    • Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme
    • N. Shimazaki, K. Yoshida, T. Kobayashi, S. Toji, K. Tamai, O. Koiwai, Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme, Genes Cells 7 (2002) 639-651.
    • (2002) Genes Cells , vol.7 , pp. 639-651
    • Shimazaki, N.1    Yoshida, K.2    Kobayashi, T.3    Toji, S.4    Tamai, K.5    Koiwai, O.6
  • 2
    • 0037166307 scopus 로고    scopus 로고
    • DNA polymerase lambda from calf thymus preferentially replicates damaged DNA
    • K. Ramadan, I.V. Shevelev, G. Maga, U. Hubscher, DNA polymerase lambda from calf thymus preferentially replicates damaged DNA, J. Biol. Chem. 277 (2002) 18454-18458.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18454-18458
    • Ramadan, K.1    Shevelev, I.V.2    Maga, G.3    Hubscher, U.4
  • 3
    • 2242420935 scopus 로고    scopus 로고
    • Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis
    • G. Maga, G. Villani, K. Ramadan, I. Shevelev, N.T. Le Gac, L. Blanco, G. Blanca, S. Spadari, U. Hubscher, Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis, J. Biol. Chem. 277 (2002) 48434-48440.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48434-48440
    • Maga, G.1    Villani, G.2    Ramadan, K.3    Shevelev, I.4    Le Gac, N.T.5    Blanco, L.6    Blanca, G.7    Spadari, S.8    Hubscher, U.9
  • 5
    • 0033538091 scopus 로고    scopus 로고
    • A new DNA polymerase species from Drosophila melanogaster: A probable mus308 gene product
    • M. Oshige, N. Aoyagi, P.V. Harris, K.C. Burtis, K. Sakaguchi, A new DNA polymerase species from Drosophila melanogaster: a probable mus308 gene product, Mutat. Res. 433 (1999) 183-192.
    • (1999) Mutat. Res. , vol.433 , pp. 183-192
    • Oshige, M.1    Aoyagi, N.2    Harris, P.V.3    Burtis, K.C.4    Sakaguchi, K.5
  • 7
    • 0034705095 scopus 로고    scopus 로고
    • The many faces of DNA polymerases: Strategies for mutagenesis and for mutational avoidance
    • E.C. Friedberg, W.J. Feaver, V.L. Gerlach, The many faces of DNA polymerases: strategies for mutagenesis and for mutational avoidance, Proc. Natl. Acad. Sci. USA 97 (2002) 5681-5683.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5681-5683
    • Friedberg, E.C.1    Feaver, W.J.2    Gerlach, V.L.3
  • 9
    • 0032587610 scopus 로고    scopus 로고
    • DNA polymerase epsilon catalytic domains are dispensable for DNA replication, DNA repair, and cell viability
    • T. Kesti, K. Flick, S. Keranen, J.E. Syvaoja, C. Wittenberg, DNA polymerase epsilon catalytic domains are dispensable for DNA replication, DNA repair, and cell viability, Mol. Cell 3 (1999) 679-685.
    • (1999) Mol. Cell , vol.3 , pp. 679-685
    • Kesti, T.1    Flick, K.2    Keranen, S.3    Syvaoja, J.E.4    Wittenberg, C.5
  • 10
    • 0033529497 scopus 로고    scopus 로고
    • Analysis of the essential functions of the C-terminal protein/protein interaction domain of Saccharomyces cerevisiae pol epsilon and its unexpected ability to support growth in the absence of the DNA polymerase domain
    • R. Dua, D.L. Levy, J.L. Campbell, Analysis of the essential functions of the C-terminal protein/protein interaction domain of Saccharomyces cerevisiae pol epsilon and its unexpected ability to support growth in the absence of the DNA polymerase domain, J. Biol. Chem. 274 (1999) 22283-22288.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22283-22288
    • Dua, R.1    Levy, D.L.2    Campbell, J.L.3
  • 11
    • 0023185816 scopus 로고
    • Isolation and characterization of a photorepair-deficient mutant in Drosophila melanogaster
    • J.B. Boyd, P.V. Harris, Isolation and characterization of a photorepair-deficient mutant in Drosophila melanogaster, Genetics 116 (1987) 233-239.
    • (1987) Genetics , vol.116 , pp. 233-239
    • Boyd, J.B.1    Harris, P.V.2
  • 13
    • 0025365165 scopus 로고
    • Mus308 mutants of Drosophila exhibit hypersensitivity to DNA cross-linking agents and are defective in a deoxyribonuclease
    • J.B. Boyd, K. Sakaguchi, P.V. Harris, Mus308 mutants of Drosophila exhibit hypersensitivity to DNA cross-linking agents and are defective in a deoxyribonuclease, Genetics 125 (1990) 813-819.
    • (1990) Genetics , vol.125 , pp. 813-819
    • Boyd, J.B.1    Sakaguchi, K.2    Harris, P.V.3
  • 14
    • 0036714152 scopus 로고    scopus 로고
    • Drosophila damage-specific DNA-binding protein 1 (D-DDB1) is controlled by the DRE/DREF system
    • K. Takata, G. Ishikawa, F. Hirose, K. Sakaguchi, Drosophila damage-specific DNA-binding protein 1 (D-DDB1) is controlled by the DRE/DREF system, Nucleic Acids Res. 30 (2002) 3795-3808.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3795-3808
    • Takata, K.1    Ishikawa, G.2    Hirose, F.3    Sakaguchi, K.4
  • 15
    • 0016023634 scopus 로고
    • Sea urchin nuclear DNA polymerase
    • B.S. Fansler, L.A. Loeb, Sea urchin nuclear DNA polymerase, Methods Enzymol. 29 (1974) 53-70.
    • (1974) Methods Enzymol. , vol.29 , pp. 53-70
    • Fansler, B.S.1    Loeb, L.A.2
  • 16
    • 0028268383 scopus 로고
    • Purification and characterisation of dRP-A: A single-stranded DNA binding protein from Drosophila melanogaster
    • R.F. Marton, P. Thommes, S. Cotterill, Purification and characterisation of dRP-A: a single-stranded DNA binding protein from Drosophila melanogaster, FEBS Lett. 342 (1994) 139-144.
    • (1994) FEBS Lett. , vol.342 , pp. 139-144
    • Marton, R.F.1    Thommes, P.2    Cotterill, S.3
  • 17
    • 0022202529 scopus 로고
    • Purification and characterization of a DNA polymerase beta from Drosophila*
    • K. Sakaguchi, J.B. Boyd, Purification and characterization of a DNA polymerase beta from Drosophila*, J. Biol. Chem. 260 (1985) 10406-10411.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10406-10411
    • Sakaguchi, K.1    Boyd, J.B.2
  • 18
    • 0025635943 scopus 로고
    • Immunoaffinity purification and properties of Drosophila melanogaster DNA polymerase alpha-primase complex
    • K. Kuroda, R. Kagiyama-Takahashi, T. Shinomiya, Immunoaffinity purification and properties of Drosophila melanogaster DNA polymerase alpha-primase complex, J. Biochem. 108 (1990) 926-933.
    • (1990) J. Biochem. , vol.108 , pp. 926-933
    • Kuroda, K.1    Kagiyama-Takahashi, R.2    Shinomiya, T.3
  • 20
    • 0021872030 scopus 로고
    • The mutational specificity of DNA polymerase-beta during in vitro DNA synthesis. Production of frameshift, base substitution, and deletion mutations
    • T.A. Kunkel, The mutational specificity of DNA polymerase-beta during in vitro DNA synthesis. Production of frameshift, base substitution, and deletion mutations, J. Biol. Chem. 260 (1985) 5787-5796.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5787-5796
    • Kunkel, T.A.1
  • 21
    • 0018787427 scopus 로고
    • A high molecular weight DNA polymerase from Drosophila melanogaster embryos. Purification, structure, and partial characterization
    • G.R. Banks, J.A. Boezi, I.R. Lehman, A high molecular weight DNA polymerase from Drosophila melanogaster embryos. Purification, structure, and partial characterization, J. Biol. Chem. 254 (1979) 9886-9892.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9886-9892
    • Banks, G.R.1    Boezi, J.A.2    Lehman, I.R.3
  • 22
    • 0022840351 scopus 로고
    • A mitochondrial DNA polymerase from embryos of Drosophila melanogaster. Purification, subunit structure, and partial characterization
    • C.M. Wernette, L.S. Kaguni, A mitochondrial DNA polymerase from embryos of Drosophila melanogaster. Purification, subunit structure, and partial characterization, J. Biol. Chem. 261 (1986) 14764-14770.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14764-14770
    • Wernette, C.M.1    Kaguni, L.S.2
  • 24
    • 0023181306 scopus 로고
    • Processivity of the DNA polymerase alpha-primase complex from calf thymus
    • K.T. Hohn, F. Grosse, Processivity of the DNA polymerase alpha-primase complex from calf thymus, Biochemistry 26 (1987) 2870-2878.
    • (1987) Biochemistry , vol.26 , pp. 2870-2878
    • Hohn, K.T.1    Grosse, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.