메뉴 건너뛰기




Volumn 735, Issue 1-2, 2012, Pages 12-18

Human endonuclease V as a repair enzyme for DNA deamination

Author keywords

Deamination; DNA repair; Endonuclease; Inosine; Nitrosative stress; Xanthosine

Indexed keywords

ADENOSINE; AMINO ACID; COBALT; CYTIDINE; DEOXYADENOSINE; DEOXYINOSINE; DEOXYURIDINE; DNA; ENDONUCLEASE; GUANOSINE; MAGNESIUM; MANGANESE; NICKEL; SINGLE STRANDED DNA; THIOREDOXIN;

EID: 84863002102     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2012.05.003     Document Type: Article
Times cited : (32)

References (48)
  • 1
    • 0020079017 scopus 로고
    • On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme
    • Demple B., Linn S. On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme. J. Biol. Chem. 1982, 257:2848-2855.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2848-2855
    • Demple, B.1    Linn, S.2
  • 2
    • 0017356740 scopus 로고
    • Endonuclease V of Escherichia coli
    • Gates F.T., Linn S. Endonuclease V of Escherichia coli. J. Biol. Chem. 1977, 252:1647-1653.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1647-1653
    • Gates, F.T.1    Linn, S.2
  • 3
    • 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., Kow Y.W. Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3' endonuclease, from Escherichia coli. J. Biol. Chem. 1994, 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
  • 4
    • 1842338079 scopus 로고    scopus 로고
    • Further characterization of Escherichia coli endonuclease V
    • Yao M., Kow Y.W. Further characterization of Escherichia coli endonuclease V. J. Biol. Chem. 1997, 272:30774-30779.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30774-30779
    • Yao, M.1    Kow, Y.W.2
  • 5
    • 12144256802 scopus 로고    scopus 로고
    • Active site plasticity of endonuclease V from Salmonella typhimurium
    • Feng H., Klutz A.M., Cao W. Active site plasticity of endonuclease V from Salmonella typhimurium. Biochemistry 2005, 44:675-683.
    • (2005) Biochemistry , vol.44 , pp. 675-683
    • Feng, H.1    Klutz, A.M.2    Cao, W.3
  • 6
    • 3242875178 scopus 로고    scopus 로고
    • Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V
    • Hitchcock T.M., Gao H., Cao W. Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V. Nucleic Acids Res. 2004, 32:4071-4080.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4071-4080
    • Hitchcock, T.M.1    Gao, H.2    Cao, W.3
  • 7
    • 0035979334 scopus 로고    scopus 로고
    • Multiple cleavage activities of endonuclease V from Thermotoga maritima: recognition and strand nicking mechanism
    • Huang J., Lu J., Barany F., Cao W. Multiple cleavage activities of endonuclease V from Thermotoga maritima: recognition and strand nicking mechanism. Biochemistry 2001, 40:8738-8748.
    • (2001) Biochemistry , vol.40 , pp. 8738-8748
    • Huang, J.1    Lu, J.2    Barany, F.3    Cao, W.4
  • 8
    • 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., Kow Y.W. A deoxyinosine specific endonuclease from hyperthermophile, Archaeoglobus fulgidus: a homolog of Escherichia coli endonuclease V. Mutat. Res. 2000, 461:169-177.
    • (2000) Mutat. Res. , vol.461 , pp. 169-177
    • Liu, J.1    He, B.2    Qing, H.3    Kow, Y.W.4
  • 9
    • 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., Bjoras M., Seeberg E., Rognes T., Klungland A. Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V. Nucleic Acids Res. 2003, 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    Bjoras, M.5    Seeberg, E.6    Rognes, T.7    Klungland, A.8
  • 10
    • 0028032935 scopus 로고
    • Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli
    • Yao M., Kow Y.W. Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli. J. Biol. Chem. 1994, 269:31390-31396.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31390-31396
    • Yao, M.1    Kow, Y.W.2
  • 11
    • 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., Kow Y.W. Cleavage of insertion/deletion mismatches, flap and pseudo-Y DNA structures by deoxyinosine 3'-endonuclease from Escherichia coli. J. Biol. Chem. 1996, 271:30672-30676.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30672-30676
    • Yao, M.1    Kow, Y.W.2
  • 12
    • 0001773702 scopus 로고
    • Damage to DNA caused by hydrolysis
    • Plenum Press, New York, E. Seeberg, K. Kleppe (Eds.)
    • Shapiro R. Damage to DNA caused by hydrolysis. Chromosome Damage and Repair 1981, 3-18. Plenum Press, New York. E. Seeberg, K. Kleppe (Eds.).
    • (1981) Chromosome Damage and Repair , pp. 3-18
    • Shapiro, R.1
  • 13
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature 1993, 362:709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 14
    • 0033603420 scopus 로고    scopus 로고
    • Efficient nitroso group transfer from N-nitrosoindoles to nucleotides and 2'-deoxyguanosine at physiological pH. A new pathway for N- nitrosocompounds to exert genotoxicity
    • Lucas L.T., Gatehouse D., Shuker D.E. Efficient nitroso group transfer from N-nitrosoindoles to nucleotides and 2'-deoxyguanosine at physiological pH. A new pathway for N- nitrosocompounds to exert genotoxicity. J. Biol. Chem. 1999, 274:18319-18326.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18319-18326
    • Lucas, L.T.1    Gatehouse, D.2    Shuker, D.E.3
  • 15
    • 0029989276 scopus 로고    scopus 로고
    • Isolation and characterization of a novel product, 2'-deoxyoxanosine, from 2'-deoxyguanosine, oligodeoxynucleotide and calf thymus DNA treated by nitrous-acid and nitric-oxide
    • Suzuki T., Yamaoka R., Nishi M., Ide H., Makino K. Isolation and characterization of a novel product, 2'-deoxyoxanosine, from 2'-deoxyguanosine, oligodeoxynucleotide and calf thymus DNA treated by nitrous-acid and nitric-oxide. J. Am. Chem. Soc. 1996, 118:2515-2516.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2515-2516
    • Suzuki, T.1    Yamaoka, R.2    Nishi, M.3    Ide, H.4    Makino, K.5
  • 16
    • 0028148977 scopus 로고
    • Deoxyinosine 3' endonuclease, a novel deoxyinosine-specific endonuclease from Escherichia coli
    • Yao M., Hatahet Z., Melamede R.J., Kow Y.W. Deoxyinosine 3' endonuclease, a novel deoxyinosine-specific endonuclease from Escherichia coli. Ann. N. Y. Acad. Sci. 1994, 726:315-316.
    • (1994) Ann. N. Y. Acad. Sci. , vol.726 , pp. 315-316
    • Yao, M.1    Hatahet, Z.2    Melamede, R.J.3    Kow, Y.W.4
  • 17
    • 23944524787 scopus 로고    scopus 로고
    • Defining amino acid residues involved in DNA-protein interactions and revelation of 3'-exonuclease activity in endonuclease V
    • Feng H., Dong L., Klutz A.M., Aghaebrahim N., Cao W. Defining amino acid residues involved in DNA-protein interactions and revelation of 3'-exonuclease activity in endonuclease V. Biochemistry 2005, 44:11486-11495.
    • (2005) Biochemistry , vol.44 , pp. 11486-11495
    • Feng, H.1    Dong, L.2    Klutz, A.M.3    Aghaebrahim, N.4    Cao, W.5
  • 18
    • 0034689567 scopus 로고    scopus 로고
    • Deoxyxanthosine in DNA is repaired by Escherichia coli endonuclease V
    • He B., Qing H., Kow Y.W. Deoxyxanthosine in DNA is repaired by Escherichia coli endonuclease V. Mutat. Res. 2000, 459:109-114.
    • (2000) Mutat. Res. , vol.459 , pp. 109-114
    • He, B.1    Qing, H.2    Kow, Y.W.3
  • 19
    • 31744431923 scopus 로고    scopus 로고
    • Development of enzymatic probes of oxidative and nitrosative DNA damage caused by reactive nitrogen species
    • Dong M., Vongchampa V., Gingipalli L., Cloutier J.F., Kow Y.W., O'Connor T., Dedon P.C. Development of enzymatic probes of oxidative and nitrosative DNA damage caused by reactive nitrogen species. Mutat. Res. 2006, 594:120-134.
    • (2006) Mutat. Res. , vol.594 , pp. 120-134
    • Dong, M.1    Vongchampa, V.2    Gingipalli, L.3    Cloutier, J.F.4    Kow, Y.W.5    O'Connor, T.6    Dedon, P.C.7
  • 20
    • 0031033040 scopus 로고    scopus 로고
    • Nfi, the gene for endonuclease V in Escherichia coli K-12
    • Guo G., Ding Y., Weiss B. nfi, the gene for endonuclease V in Escherichia coli K-12. J. Bacteriol. 1997, 179:310-316.
    • (1997) J. Bacteriol. , vol.179 , pp. 310-316
    • Guo, G.1    Ding, Y.2    Weiss, B.3
  • 21
    • 0038304303 scopus 로고    scopus 로고
    • Repair system for noncanonical purines in Escherichia coli
    • Burgis N.E., Brucker J.J., Cunningham R.P. Repair system for noncanonical purines in Escherichia coli. J. Bacteriol. 2003, 185:3101-3110.
    • (2003) J. Bacteriol. , vol.185 , pp. 3101-3110
    • Burgis, N.E.1    Brucker, J.J.2    Cunningham, R.P.3
  • 22
    • 0031963104 scopus 로고    scopus 로고
    • Endonuclease V (nfi) mutant of Escherichia coli K-12
    • Guo G., Weiss B. Endonuclease V (nfi) mutant of Escherichia coli K-12. J. Bacteriol. 1998, 180:46-51.
    • (1998) J. Bacteriol. , vol.180 , pp. 46-51
    • Guo, G.1    Weiss, B.2
  • 23
    • 0035808729 scopus 로고    scopus 로고
    • Endonuclease V of Escherichia coli prevents mutations from nitrosative deamination during nitrate/nitrite respiration
    • Weiss B. Endonuclease V of Escherichia coli prevents mutations from nitrosative deamination during nitrate/nitrite respiration. Mutat. Res. 2001, 461:301-309.
    • (2001) Mutat. Res. , vol.461 , pp. 301-309
    • Weiss, B.1
  • 24
    • 33846682789 scopus 로고    scopus 로고
    • Switching base preferences of mismatch cleavage in endonuclease V: an improved method for scanning point mutations
    • Gao H., Huang J., Barany F., Cao W. Switching base preferences of mismatch cleavage in endonuclease V: an improved method for scanning point mutations. Nucleic Acids Res. 2007, 35:e2.
    • (2007) Nucleic Acids Res. , vol.35
    • Gao, H.1    Huang, J.2    Barany, F.3    Cao, W.4
  • 26
    • 3042779520 scopus 로고    scopus 로고
    • Harmonized microarray/mutation scanning analysis of TP53 mutations in undissected colorectal tumors
    • Favis R., Huang J., Gerry N.P., Culliford A., Paty P., Soussi T., Barany F. Harmonized microarray/mutation scanning analysis of TP53 mutations in undissected colorectal tumors. Hum. Mutat. 2004, 24:63-75.
    • (2004) Hum. Mutat. , vol.24 , pp. 63-75
    • Favis, R.1    Huang, J.2    Gerry, N.P.3    Culliford, A.4    Paty, P.5    Soussi, T.6    Barany, F.7
  • 28
    • 85047698770 scopus 로고    scopus 로고
    • An endonuclease/ligase based mutation scanning method especially suited for analysis of neoplastic tissue
    • Huang J., Kirk B., Favis R., Soussi T., Paty P., Cao W., Barany F. An endonuclease/ligase based mutation scanning method especially suited for analysis of neoplastic tissue. Oncogene 2002, 21:1909-1921.
    • (2002) Oncogene , vol.21 , pp. 1909-1921
    • Huang, J.1    Kirk, B.2    Favis, R.3    Soussi, T.4    Paty, P.5    Cao, W.6    Barany, F.7
  • 29
    • 0037008086 scopus 로고    scopus 로고
    • Mutational analysis of endonuclease V from Thermotoga maritima
    • Huang J., Lu J., Barany F., Cao W. Mutational analysis of endonuclease V from Thermotoga maritima. Biochemistry 2002, 41:8342-8350.
    • (2002) Biochemistry , vol.41 , pp. 8342-8350
    • Huang, J.1    Lu, J.2    Barany, F.3    Cao, W.4
  • 32
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K.A., Wanner B.L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 34
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymease chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymease chain reaction. Gene 1989, 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 36
    • 0034675927 scopus 로고    scopus 로고
    • Repair of chromosomal abasic sites in vivo involves at least three different repair pathways
    • Otterlei M., Kavli B., Standal R., Skjelbred C., Bharati S., Krokan H.E. Repair of chromosomal abasic sites in vivo involves at least three different repair pathways. EMBO J. 2000, 19:5542-5551.
    • (2000) EMBO J. , vol.19 , pp. 5542-5551
    • Otterlei, M.1    Kavli, B.2    Standal, R.3    Skjelbred, C.4    Bharati, S.5    Krokan, H.E.6
  • 37
    • 0028845857 scopus 로고
    • Interaction of deoxyinosine 3'-endonuclease from Escherichia coli with DNA containing deoxyinosine
    • Yao M., Kow Y.W. Interaction of deoxyinosine 3'-endonuclease from Escherichia coli with DNA containing deoxyinosine. J. Biol. Chem. 1995, 270:28609-28616.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28609-28616
    • Yao, M.1    Kow, Y.W.2
  • 38
    • 0036801346 scopus 로고    scopus 로고
    • Repair of deaminated bases in DNA
    • Kow Y.W. Repair of deaminated bases in DNA. Free Radic. Biol. Med. 2002, 33:886-893.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 886-893
    • Kow, Y.W.1
  • 39
    • 0032806424 scopus 로고    scopus 로고
    • Endonuclease V protects Escherichia coli against specific mutations caused by nitrous acid
    • Schouten K.A., Weiss B. Endonuclease V protects Escherichia coli against specific mutations caused by nitrous acid. Mutat. Res. 1999, 435:245-254.
    • (1999) Mutat. Res. , vol.435 , pp. 245-254
    • Schouten, K.A.1    Weiss, B.2
  • 40
    • 0028231020 scopus 로고
    • Studies on the base pairing properties of deoxyinosine by solid phase hybridisation to oligonucleotides
    • Case-Green S.C., Southern E.M. Studies on the base pairing properties of deoxyinosine by solid phase hybridisation to oligonucleotides. Nucleic Acids Res. 1994, 22:131-136.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 131-136
    • Case-Green, S.C.1    Southern, E.M.2
  • 41
    • 0022429804 scopus 로고
    • Base pairing involving deoxyinosine: implications for probe design
    • Martin F.H., Castro M.M., Aboul-ela F., Tinoco I. Base pairing involving deoxyinosine: implications for probe design. Nucleic Acids Res. 1985, 13:8927-8938.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8927-8938
    • Martin, F.H.1    Castro, M.M.2    Aboul-ela, F.3    Tinoco, I.4
  • 42
    • 28544447850 scopus 로고    scopus 로고
    • Nearest-neighbor thermodynamics of deoxyinosine pairs in DNA duplexes
    • Watkins N.E., SantaLucia J. Nearest-neighbor thermodynamics of deoxyinosine pairs in DNA duplexes. Nucleic Acids Res. 2005, 33:6258-6267.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6258-6267
    • Watkins, N.E.1    SantaLucia, J.2
  • 43
    • 0035918230 scopus 로고    scopus 로고
    • Base excision and DNA binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion
    • Abner C.W., Lau A.Y., Ellenberger T., Bloom L.B. Base excision and DNA binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion. J. Biol. Chem. 2001, 276:13379-13387.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13379-13387
    • Abner, C.W.1    Lau, A.Y.2    Ellenberger, T.3    Bloom, L.B.4
  • 44
    • 0025800612 scopus 로고
    • Preferential recognition of I.T. base-pairs in the initiation of excision-repair by hypoxanthine-DNA glycosylase
    • Dianov G., Lindahl T. Preferential recognition of I.T. base-pairs in the initiation of excision-repair by hypoxanthine-DNA glycosylase. Nucleic Acids Res. 1991, 19:3829-3833.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3829-3833
    • Dianov, G.1    Lindahl, T.2
  • 45
    • 0034653288 scopus 로고    scopus 로고
    • Interactions of the human, rat. Saccharomyces cerevisiae and Escherichia coli 3-methyladenine-DNA glycosylases with DNA containing dIMP residues
    • Saparbaev M., Mani J.C., Laval J. Interactions of the human, rat. Saccharomyces cerevisiae and Escherichia coli 3-methyladenine-DNA glycosylases with DNA containing dIMP residues. Nucleic Acids Res. 2000, 28:1332-1339.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1332-1339
    • Saparbaev, M.1    Mani, J.C.2    Laval, J.3
  • 46
    • 0034118395 scopus 로고    scopus 로고
    • Influence of DNA structure on hypoxanthine and 1,N(6)-ethenoadenine removal by murine 3-methyladenine DNA glycosylase
    • Wyatt M.D., Samson L.D. Influence of DNA structure on hypoxanthine and 1,N(6)-ethenoadenine removal by murine 3-methyladenine DNA glycosylase. Carcinogenesis 2000, 21:901-908.
    • (2000) Carcinogenesis , vol.21 , pp. 901-908
    • Wyatt, M.D.1    Samson, L.D.2
  • 47
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • Saparbaev M., Laval J. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:5873-5877.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 48
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • Dou H., Mitra S., Hazra T.K. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 2003, 278:49679-49684.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.