메뉴 건너뛰기




Volumn 43, Issue 5, 2015, Pages 2853-2863

A novel endonuclease that may be responsible for damaged DNA base repair in Pyrococcus furiosus

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYINOSINE; ENDONUCLEASE; ENDONUCLEASE Q; HYPOXANTHINE; UNCLASSIFIED DRUG; URACIL; XANTHINE; ARCHAEAL DNA; ARCHAEAL PROTEIN;

EID: 84931285585     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv121     Document Type: Article
Times cited : (41)

References (36)
  • 1
    • 84876016461 scopus 로고    scopus 로고
    • Mammalian base excision repair: The forgotten archangel
    • Dianov, G. L. and Hübscher, U. (2013) Mammalian base excision repair: the forgotten archangel. Nucleic Acids Res., 41, 3483-3490.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3483-3490
    • Dianov, G.L.1    Hübscher, U.2
  • 2
    • 84876730678 scopus 로고    scopus 로고
    • Co-ordination of base excision repair and genome stability
    • Parsons, J. L. and Dianov, G. L. (2013) Co-ordination of base excision repair and genome stability. DNA Repair, 12, 326-333.
    • (2013) DNA Repair , vol.12 , pp. 326-333
    • Parsons, J.L.1    Dianov, G.L.2
  • 3
    • 84857031313 scopus 로고    scopus 로고
    • Damage recognition in nucleotide excision DNA repair
    • Kuper, J. and Kisker, C. (2012) Damage recognition in nucleotide excision DNA repair. Curr. Opin. Struct. Biol., 22, 88-93.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 88-93
    • Kuper, J.1    Kisker, C.2
  • 4
    • 79960350167 scopus 로고    scopus 로고
    • The xeroderma pigmentosum pathway: Decision tree analysis of DNA quality
    • Naegeli, H. and Sugasawa, K. (2011) The xeroderma pigmentosum pathway: decision tree analysis of DNA quality. DNA Repair, 10, 673-683.
    • (2011) DNA Repair , vol.10 , pp. 673-683
    • Naegeli, H.1    Sugasawa, K.2
  • 5
    • 84878930839 scopus 로고    scopus 로고
    • Alternative excision repair pathways
    • Yasui, A. (2013) Alternative excision repair pathways. Cold Spring Harb. Perspect. Biol., 5, a012617.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a012617
    • Yasui, A.1
  • 6
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde, M. L., Hazra, T. K. and Mitra, S. (2008) Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res., 18, 27-47.
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 7
    • 84902119190 scopus 로고    scopus 로고
    • The cutting edges in DNA repair, licensing, and fidelity: DNA and RNA repair nucleases sculpt DNA to measure twice, cut once
    • Tsutakawa, S. E., Lafrance-Vanasse, J. and Tainer, J. A. (2014) The cutting edges in DNA repair, licensing, and fidelity: DNA and RNA repair nucleases sculpt DNA to measure twice, cut once. DNA Repair, 19, 95-107.
    • (2014) DNA Repair , vol.19 , pp. 95-107
    • Tsutakawa, S.E.1    Lafrance-Vanasse, J.2    Tainer, J.A.3
  • 8
    • 0036801346 scopus 로고    scopus 로고
    • Repair of deaminated bases in DNA
    • Kow, Y. W. (2002). Repair of deaminated bases in DNA. Free Radic. Biol. Med., 33, 886-893.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 886-893
    • Kow, Y.W.1
  • 9
    • 84923674774 scopus 로고    scopus 로고
    • Uracil-DNA glycosylases-Structural and functional perspectives on an essential family of DNA repair enzymes
    • Schormann, N., Ricciardi, R. and Chattopadhyay, D. (2014) Uracil-DNA glycosylases-Structural and functional perspectives on an essential family of DNA repair enzymes. Protein Sci., 23, 1667-1685.
    • (2014) Protein Sci. , vol.23 , pp. 1667-1685
    • Schormann, N.1    Ricciardi, R.2    Chattopadhyay, D.3
  • 10
    • 0017356740 scopus 로고
    • Endonuclease V of Escherichia coli
    • Gates, F. T. III and Linn, S. (1977) Endonuclease V of Escherichia coli. J. Biol. Chem., 252, 1647-1653.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1647-1653
    • Gates, F.T.1    Linn, S.2
  • 11
    • 0020079017 scopus 로고
    • On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme
    • Demple, B. and Linn, S. (1982) On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme. J. Biol. Chem., 257, 2848-2855.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2848-2855
    • Demple, B.1    Linn, S.2
  • 12
    • 0028286268 scopus 로고
    • Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3' endonuclease, from Escherichia coli
    • Yao, M., Hatahet, Z., Melamede, R. J. and Kow, Y. W. (1994) Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3' endonuclease, from Escherichia coli. J. Biol. Chem., 269, 16260-16268.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16260-16268
    • Yao, M.1    Hatahet, Z.2    Melamede, R.J.3    Kow, Y.W.4
  • 13
    • 0028032935 scopus 로고
    • Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli
    • Yao, M. and Kow, Y. W. (1994) Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli. J. Biol. Chem., 269, 31390-31396.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31390-31396
    • Yao, M.1    Kow, Y.W.2
  • 14
    • 10544239535 scopus 로고    scopus 로고
    • Cleavage of insertion/deletion mismatches, flap and pseudo-Y DNA structures by deoxyinosine 3'-endonuclease from Escherichia coli
    • Yao, M. and Kow, Y. W. (1996) Cleavage of insertion/deletion mismatches, flap and pseudo-Y DNA structures by deoxyinosine 3'-endonuclease from Escherichia coli. J. Biol. Chem., 271, 30672-30676.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30672-30676
    • Yao, M.1    Kow, Y.W.2
  • 15
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind, L., Walker, D. R. and Koonin, E. V. (1999) Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res., 27, 1223-1242.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1223-1242
    • Aravind, L.1    Walker, D.R.2    Koonin, E.V.3
  • 16
    • 84882448985 scopus 로고    scopus 로고
    • Endonuclease V: An unusual enzyme for repair of DNA deamination
    • Cao, W. (2013) Endonuclease V: an unusual enzyme for repair of DNA deamination. Cell. Mol. Life Sci., 70, 3145-3156.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 3145-3156
    • Cao, W.1
  • 17
    • 0242380643 scopus 로고    scopus 로고
    • Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V
    • Moe, A., Ringvoll, J., Nordstrand, L. M., Eide, L., Bjørås, M., Seeberg, E., Rognes, T. and Klungland, A. (2003) Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V. Nucleic Acids Res., 31, 3893-3900.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3893-3900
    • Moe, A.1    Ringvoll, J.2    Nordstrand, L.M.3    Eide, L.4    Bjørås, M.5    Seeberg, E.6    Rognes, T.7    Klungland, A.8
  • 18
  • 19
    • 0034626814 scopus 로고    scopus 로고
    • A deoxyinosine specific endonuclease from hyperthermophile, Archaeoglobus fulgidus: A homolog of Escherichia coli endonuclease V
    • Liu, J., He, B., Qing, H. and Kow, Y. W. (2000) A deoxyinosine specific endonuclease from hyperthermophile, Archaeoglobus fulgidus: a homolog of Escherichia coli endonuclease V. Mutat. Res., 461, 169-177.
    • (2000) Mutat. Res. , vol.461 , pp. 169-177
    • Liu, J.1    He, B.2    Qing, H.3    Kow, Y.W.4
  • 20
    • 14844346741 scopus 로고    scopus 로고
    • A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities
    • Kanugula, S., Pauly, G. T., Moschel, R. C. and Pegg, A. E. (2005) A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities. Proc. Natl. Acad. Sci. U. S. A., 102, 3617-3622.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3617-3622
    • Kanugula, S.1    Pauly, G.T.2    Moschel, R.C.3    Pegg, A.E.4
  • 21
    • 84899793137 scopus 로고    scopus 로고
    • Biochemical characterization of endonuclease V from the hyperthermophilic archaeon, Pyrococcus furiosus
    • Kiyonari, S., Egashira, Y., Ishino, S. and Ishino, Y. (2014) Biochemical characterization of endonuclease V from the hyperthermophilic archaeon, Pyrococcus furiosus. J. Biochem., 153, 325-333.
    • (2014) J. Biochem. , vol.153 , pp. 325-333
    • Kiyonari, S.1    Egashira, Y.2    Ishino, S.3    Ishino, Y.4
  • 22
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • Aravind, L. and Koonin, E. V. (1998) Phosphoesterase domains associated with DNA polymerases of diverse origins. Nucleic Acids Res., 26, 3746-3752.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 23
    • 67649695570 scopus 로고    scopus 로고
    • Hidden reservoir of integrative elements is the major source of recently acquired foreign genes and ORFans in archaeal and bacterial genomes
    • Cortez, D., Forterre, P. and Gribaldo, S. A. (2009) Hidden reservoir of integrative elements is the major source of recently acquired foreign genes and ORFans in archaeal and bacterial genomes. Genome Biol., 10, R65.
    • (2009) Genome Biol. , vol.10 , pp. R65
    • Cortez, D.1    Forterre, P.2    Gribaldo, S.A.3
  • 24
    • 0036425161 scopus 로고    scopus 로고
    • The ICESt1 element of Streptococcus thermophilus belongs to a large family of integrative and conjugative elements that exchange modules and change their specificity of integration
    • Burrus, V., Pavlovic, G., Decaris, B. and Guedon, G. (2002) The ICESt1 element of Streptococcus thermophilus belongs to a large family of integrative and conjugative elements that exchange modules and change their specificity of integration. Plasmid, 48, 77-97.
    • (2002) Plasmid , vol.48 , pp. 77-97
    • Burrus, V.1    Pavlovic, G.2    Decaris, B.3    Guedon, G.4
  • 25
    • 0037439997 scopus 로고    scopus 로고
    • Structural classification of zinc fingers: Survey and summary
    • Krishna, S. S., Majumdar, I. and Grishin, N. V. (2003) Structural classification of zinc fingers: survey and summary. Nucleic Acids Res., 31, 532-550.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 532-550
    • Krishna, S.S.1    Majumdar, I.2    Grishin, N.V.3
  • 26
    • 79951678159 scopus 로고    scopus 로고
    • Nucleases: Diversity of structure, function and mechanism
    • Yang, W. (2011) Nucleases: diversity of structure, function and mechanism. Q. Rev. Biophys., 44, 1-93.
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 1-93
    • Yang, W.1
  • 28
    • 13844320315 scopus 로고    scopus 로고
    • A recombinant exonuclease III homologue of the thermophilic archaeon Methanothermobacter thermautotrophicus
    • Pfeifer, S. and Greiner-Stöffele, T. (2005) A recombinant exonuclease III homologue of the thermophilic archaeon Methanothermobacter thermautotrophicus. DNA Repair, 4, 433-444.
    • (2005) DNA Repair , vol.4 , pp. 433-444
    • Pfeifer, S.1    Greiner-Stöffele, T.2
  • 29
    • 65549119732 scopus 로고    scopus 로고
    • DNA uracil repair initiated by the archaeal ExoIII homologue Mth212 via direct strand incision
    • Schomacher, L., Chong, J. P., McDermott, P., Kramer, W. and Fritz, H.-J. (2009) DNA uracil repair initiated by the archaeal ExoIII homologue Mth212 via direct strand incision. Nucleic Acids Res. 37, 2283-2293.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 2283-2293
    • Schomacher, L.1    Chong, J.P.2    McDermott, P.3    Kramer, W.4    Fritz, H.-J.5
  • 30
    • 53049086145 scopus 로고    scopus 로고
    • Physical and functional interactions between uracil-DNA glycosylase and proliferating cell nuclear antigen from the euryarchaeon Pyrococcus furiosus
    • Kiyonari, S., Uchimura, M., Shirai, T. and Ishino, Y. (2008) Physical and functional interactions between uracil-DNA glycosylase and proliferating cell nuclear antigen from the euryarchaeon Pyrococcus furiosus. J. Biol. Chem., 283, 24185-24193.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24185-24193
    • Kiyonari, S.1    Uchimura, M.2    Shirai, T.3    Ishino, Y.4
  • 31
    • 70449687206 scopus 로고    scopus 로고
    • Biochemical properties and base excision repair complex formation of apurinic/apyrimidinic endonuclease from Pyrococcus furiosus
    • Kiyonari, S., Tahara, S., Shirai, T., Iwai, S., Ishino, S. and Ishino, Y. (2009) Biochemical properties and base excision repair complex formation of apurinic/apyrimidinic endonuclease from Pyrococcus furiosus. Nucleic Acids Res., 37, 6439-6453.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6439-6453
    • Kiyonari, S.1    Tahara, S.2    Shirai, T.3    Iwai, S.4    Ishino, S.5    Ishino, Y.6
  • 32
    • 39049171187 scopus 로고    scopus 로고
    • Repair of UV damage in bacteria
    • Goosen, N. and Moolenaar, G. F. (2008) Repair of UV damage in bacteria. DNA Repair, 7, 353-379.
    • (2008) DNA Repair , vol.7 , pp. 353-379
    • Goosen, N.1    Moolenaar, G.F.2
  • 35
    • 0037215528 scopus 로고    scopus 로고
    • Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Sato, T., Fukui, T., Atomi, H. and Imanaka, T. (2003) Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol., 185, 210-220.
    • (2003) J. Bacteriol. , vol.185 , pp. 210-220
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 36
    • 22144443201 scopus 로고    scopus 로고
    • Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Sato, T., Fukui, T., Atomi, H. and Imanaka, T. (2005) Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis. Appl. Environ. Microbiol., 71, 3889-3899.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 3889-3899
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.