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Volumn 14, Issue 13, 2000, Pages 1589-1594

Error-prone bypass of certain DNA lesions by the human DNA polymerase κ

Author keywords

AAF; Abasic site; DINB1; Mutation; Pol ; Sequence context

Indexed keywords

DNA POLYMERASE;

EID: 0034235584     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (274)

References (33)
  • 1
    • 0032703301 scopus 로고    scopus 로고
    • Replication of damaged DNA: Molecular defect in xeroderma pigmentosum variant cells
    • Cordonnier, A.M. and Fuchs, R.P.P. 1999. Replication of damaged DNA: Molecular defect in xeroderma pigmentosum variant cells. Mutat. Res. 435: 111-119.
    • (1999) Mutat. Res. , vol.435 , pp. 111-119
    • Cordonnier, A.M.1    Fuchs, R.P.P.2
  • 2
    • 0033020150 scopus 로고    scopus 로고
    • Impaired translesion synthesis in xeroderma pigmentosum variant extracts
    • Cordonnier, A.M., Lehman, A.R., and Fuchs, R.P.P. 1999. Impaired translesion synthesis in xeroderma pigmentosum variant extracts. Mol. Cell Biol. 19: 2206-2211.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 2206-2211
    • Cordonnier, A.M.1    Lehman, A.R.2    Fuchs, R.P.P.3
  • 3
    • 0030872714 scopus 로고    scopus 로고
    • The high spontaneous mutation rate: Is it a health risk?
    • Crow, J.F. 1997. The high spontaneous mutation rate: Is it a health risk? Proc. Natl. Acad. Sci. 94: 8380-8386.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 8380-8386
    • Crow, J.F.1
  • 4
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase β violates the "A-rule." Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts
    • Efrati, E., Tocco, G., Eritja, R., Wilson, S.H., and Goodman, M.F. 1997. Abasic translesion synthesis by DNA polymerase β violates the "A-rule." Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts. J. Biol. Chem. 272: 2559-2569.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 5
    • 0033588043 scopus 로고    scopus 로고
    • Novel DNA polymerases offer clues to the molecular basis of mutagenesis
    • Friedberg, E.C. and Gerlach, V.L. 1999. Novel DNA polymerases offer clues to the molecular basis of mutagenesis. Cell 98: 413-416.
    • (1999) Cell , vol.98 , pp. 413-416
    • Friedberg, E.C.1    Gerlach, V.L.2
  • 7
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • Fujiwara, Y., Masutani, C., Mizukoshi, T., Kondo, J., Hanaoka, F., and Iwai, S. 1999. Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J. Biol. Chem. 274: 20027-20033.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1    Masutani, C.2    Mizukoshi, T.3    Kondo, J.4    Hanaoka, F.5    Iwai, S.6
  • 8
    • 0032716109 scopus 로고    scopus 로고
    • Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily
    • Gerlach, V.L., Aravind, L., Gotway, G., Schultz, R.A., Koonin, E.V., and Friedberg, E.C. 1999. Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily. Proc. Natl. Acad. Sci. 96: 11922-11927.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 11922-11927
    • Gerlach, V.L.1    Aravind, L.2    Gotway, G.3    Schultz, R.A.4    Koonin, E.V.5    Friedberg, E.C.6
  • 9
    • 0032499748 scopus 로고    scopus 로고
    • A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase ζ
    • Gibbs, P.E.M., McGregor, W.G., Maher, V.M., Nisson, P., and Lawrence, C.W. 1998. A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase ζ. Proc. Natl. Acad. Sci. 95: 6876-6880.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 6876-6880
    • Gibbs, P.E.M.1    McGregor, W.G.2    Maher, V.M.3    Nisson, P.4    Lawrence, C.W.5
  • 10
    • 0029777391 scopus 로고    scopus 로고
    • Synthesis of a phosphoramidite coupling unit of the pyrimidine (6-4) pyrimidone photoproduct and its incorporation into oligodeoxynucleotides
    • Iwai, S., Shimizu, M., Kamiya, H., and Ohtsuka, E. 1996. Synthesis of a phosphoramidite coupling unit of the pyrimidine (6-4) pyrimidone photoproduct and its incorporation into oligodeoxynucleotides. J. Am. Chem. Soc. 118: 7642-7643.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7642-7643
    • Iwai, S.1    Shimizu, M.2    Kamiya, H.3    Ohtsuka, E.4
  • 11
    • 0033538470 scopus 로고    scopus 로고
    • hRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson, R.E., Kondratick, C.M., Prakash, S., and Prakash, L. 1999a. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science 285: 263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 12
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Polη
    • Johnson, R.E., Prakash, S., and Prakash, L. 1999b. Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Polη. Science 283: 1001-1004.
    • (1999) Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 13
    • 0033522984 scopus 로고    scopus 로고
    • Requirement of DNA polymerase activity of yeast Rad30 protein for its biological function
    • _. 1999c. Requirement of DNA polymerase activity of yeast Rad30 protein for its biological function. J. Biol. Chem. 274: 15975-15977.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15975-15977
  • 14
    • 0033607287 scopus 로고    scopus 로고
    • Bridging the gap: A family of novel DNA polymerases that replicate faulty DNA
    • Johnson, R.E., Washington, M.T., Prakash, S., and Prakash, L. 1999d. Bridging the gap: A family of novel DNA polymerases that replicate faulty DNA. Proc. Natl. Acad. Sci. 96: 12224-12226.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 12224-12226
    • Johnson, R.E.1    Washington, M.T.2    Prakash, S.3    Prakash, L.4
  • 15
    • 0034635953 scopus 로고    scopus 로고
    • The human DINB1 gene encodes the DNA polymerase Polθ
    • Johnson, R.E., Prakash, S., and Prakash, L. 2000. The human DINB1 gene encodes the DNA polymerase Polθ. Proc. Natl. Acad. Sci. 97: 3838-3843.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 3838-3843
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 16
    • 0031443646 scopus 로고    scopus 로고
    • Multiple pathways for SOS-induced mutagenesis in Escherichia coli: An overexpression of dinB/dinP results in strongly enhancing mutagenesis in the absence of any exogenous treatment to damage DNA
    • Kim, S-R., Maenhaut-Michel, G., Yamada, M., Yamamoto, Y., Matsui, K., Sofuni, T., Nohmi, T., and Ohmori, H. 1997. Multiple pathways for SOS-induced mutagenesis in Escherichia coli: An overexpression of dinB/dinP results in strongly enhancing mutagenesis in the absence of any exogenous treatment to damage DNA. Proc. Natl. Acad. Sci. 94: 13792-13797.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 13792-13797
    • Kim, S.-R.1    Maenhaut-Michel, G.2    Yamada, M.3    Yamamoto, Y.4    Matsui, K.5    Sofuni, T.6    Nohmi, T.7    Ohmori, H.8
  • 18
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. 1993. Instability and decay of the primary structure of DNA. Nature 362: 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 19
    • 0033564917 scopus 로고    scopus 로고
    • Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity
    • Masutani, C., Araki, M., Yamada, A., Kusumoto, R., Nogimori, T., Mackawa, T., Iwai, S., and Hanaoka, F. 1999a. Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity. EMBO J. 18: 3491-3501
    • (1999) EMBO J. , vol.18 , pp. 3491-3501
    • Masutani, C.1    Araki, M.2    Yamada, A.3    Kusumoto, R.4    Nogimori, T.5    Mackawa, T.6    Iwai, S.7    Hanaoka, F.8
  • 21
    • 0034660259 scopus 로고    scopus 로고
    • Mechanisms of accurate translesion synthesis by human DNA polymerase η
    • in press
    • Masutani, C., Kusumoto, R., Iwai, S., and Hanaoka, F. 2000. Mechanisms of accurate translesion synthesis by human DNA polymerase η. EMBO J. (in press).
    • (2000) EMBO J.
    • Masutani, C.1    Kusumoto, R.2    Iwai, S.3    Hanaoka, F.4
  • 22
    • 0025667322 scopus 로고
    • Synthesis and characterization of a substrate for T4 endonuclease V containing a phosphorodithioate linkage at the thymine dimer site
    • Murata, T., Iwai, S., and Ohtsuka, E. 1990. Synthesis and characterization of a substrate for T4 endonuclease V containing a phosphorodithioate linkage at the thymine dimer site. Nucleic Acids Res. 18: 7279-7286.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7279-7286
    • Murata, T.1    Iwai, S.2    Ohtsuka, E.3
  • 23
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson, J.R., Lawrence, C.W., and Hinkle, D.C. 1996a. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 382: 729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 24
    • 0029952294 scopus 로고    scopus 로고
    • Thymine-thymine dimer bypass by yeast DNA polymerase ζ
    • Nelson, J.R., Lawrence, C.W., and Hinkle, D.C. 1996b. Thymine-thymine dimer bypass by yeast DNA polymerase ζ. Science 272: 1646-1649.
    • (1996) Science , vol.272 , pp. 1646-1649
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 25
    • 0033387531 scopus 로고    scopus 로고
    • Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein DinB
    • Ogi, T., Kato, Jr., T., Kato, T., and Ohmori, H. 1999. Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein DinB. Genes Cells 4: 607-618.
    • (1999) Genes Cells , vol.4 , pp. 607-618
    • Ogi, T.1    Kato T., Jr.2    Kato, T.3    Ohmori, H.4
  • 26
    • 0028979213 scopus 로고
    • dinP, a new gene in Escherichia coli, whose product shows similarities to UmuC and its homologues
    • Ohmori, H., Hatada, E., Qaio, Y., Tsuji, M., and Fukuda, R. 1995. dinP, a new gene in Escherichia coli, whose product shows similarities to UmuC and its homologues. Mutat. Res. 347: 1-7.
    • (1995) Mutat. Res. , vol.347 , pp. 1-7
    • Ohmori, H.1    Hatada, E.2    Qaio, Y.3    Tsuji, M.4    Fukuda, R.5
  • 27
    • 0033527533 scopus 로고    scopus 로고
    • The mutagenesis protein UmuC is a DNA polymerase activated by UmuD′, RecA, and SSB and is specialized for translesion replication
    • Reuven, N.B., Arad, G., Maor-Shoshani, A., and Livneh, Z. 1999. The mutagenesis protein UmuC is a DNA polymerase activated by UmuD′, RecA, and SSB and is specialized for translesion replication. J. Biol. Chem. 274: 31763-31766.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31763-31766
    • Reuven, N.B.1    Arad, G.2    Maor-Shoshani, A.3    Livneh, Z.4
  • 28
    • 0030971099 scopus 로고    scopus 로고
    • Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the "A rule"
    • Shibutani, S., Takeshita, M., and Grollman, A.P. 1997. Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the "A rule". J. Biol. Chem. 272: 13916-13922.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13916-13922
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 29
    • 0032168923 scopus 로고    scopus 로고
    • Mutagenic specificity of (Acetylamino)fluorene-derived DNA adducts in mammalian cells
    • Shibutani, S., Suzuki, N., and Grollman, A.P. 1998. Mutagenic specificity of (Acetylamino)fluorene-derived DNA adducts in mammalian cells. Biochemistry 37: 12034-12041.
    • (1998) Biochemistry , vol.37 , pp. 12034-12041
    • Shibutani, S.1    Suzuki, N.2    Grollman, A.P.3
  • 31
    • 0027170187 scopus 로고
    • Evidence for a repair enzyme complex involving ERCC1 and complementing activities of ERCC4, ERCC11 and xeroderma pigmentosum group F
    • van Vuuren, A.J., Appeldoorn, E., Odijk, H., Yasui, A., Jaspers, N.G., Bootsma, D., and Hoeijmakers, J.H. 1993. Evidence for a repair enzyme complex involving ERCC1 and complementing activities of ERCC4, ERCC11 and xeroderma pigmentosum group F. EMBO. J. 12: 3693-3701.
    • (1993) EMBO J. , vol.12 , pp. 3693-3701
    • Van Vuuren, A.J.1    Appeldoorn, E.2    Odijk, H.3    Yasui, A.4    Jaspers, N.G.5    Bootsma, D.6    Hoeijmakers, J.H.7
  • 32
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis
    • Wagner, J., Gruz, P., Kim, S-R., Yamada, M., Matsui, K., Fuchs, R.P.P., and Nohmi, T. 1999. The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis. Mol. Cell 4: 281-286.
    • (1999) Mol. Cell , vol.4 , pp. 281-286
    • Wagner, J.1    Gruz, P.2    Kim, S.-R.3    Yamada, M.4    Matsui, K.5    Fuchs, R.P.P.6    Nohmi, T.7
  • 33
    • 0033200360 scopus 로고    scopus 로고
    • A plethora of lesion-replicating DNA polymerases
    • Woodgate, R. 1999. A plethora of lesion-replicating DNA polymerases. Genes & Dev. 13: 2191-2195.
    • (1999) Genes & Dev. , vol.13 , pp. 2191-2195
    • Woodgate, R.1


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