메뉴 건너뛰기




Volumn 35, Issue 19, 2007, Pages 6672-6680

Retraction: Escherichia coli HU protein has a role in the repair of abasic sites in DNA (Nucleic Acids Research (2007) 35:19 DOI: 10.1093/nar/gkm567);Escherichia coli HU protein has a role in the repair of abasic sites in DNA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; DEOXYRIBOSE; DNA BINDING PROTEIN; HETERODIMER; HU PROTEIN; LYASE; TETRAHYDROFURAN;

EID: 36148980487     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp454     Document Type: Erratum
Times cited : (8)

References (42)
  • 1
    • 0021204627 scopus 로고
    • Isolation and characterization of nucleoid proteins from Escherichia coli
    • Yamazaki,K., Nagata,A., Kano,Y. and Imamoto,F. (1984) Isolation and characterization of nucleoid proteins from Escherichia coli. Mol. Gen. Genet., 196, 217-224.
    • (1984) Mol. Gen. Genet , vol.196 , pp. 217-224
    • Yamazaki, K.1    Nagata, A.2    Kano, Y.3    Imamoto, F.4
  • 2
    • 0024267577 scopus 로고
    • Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli
    • Wada,M., Kano,Y., Ogawa,T., Okazaki,T. and Imamoto,F. (1988) Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli. J. Mal. Biol., 204, 581-591.
    • (1988) J. Mal. Biol , vol.204 , pp. 581-591
    • Wada, M.1    Kano, Y.2    Ogawa, T.3    Okazaki, T.4    Imamoto, F.5
  • 3
    • 85165516911 scopus 로고    scopus 로고
    • Rouviere-Yaniv,J., Yaniv,M. and Germond,J.E. (1979) E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA. Cell, 17, 265-270.
    • Rouviere-Yaniv,J., Yaniv,M. and Germond,J.E. (1979) E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA. Cell, 17, 265-270.
  • 4
    • 0025775961 scopus 로고
    • Participation of the histone-like protein HU and of IHF in minichromosomal maintenance in Escherichia coli
    • Kano,Y., Ogawa,T., Ogura,J., Hiraga,S., Okazaki,T. and Imamoto,F. (1991) Participation of the histone-like protein HU and of IHF in minichromosomal maintenance in Escherichia coli. Gene, 103, 25-30.
    • (1991) Gene , vol.103 , pp. 25-30
    • Kano, Y.1    Ogawa, T.2    Ogura, J.3    Hiraga, S.4    Okazaki, T.5    Imamoto, F.6
  • 5
    • 0031858092 scopus 로고    scopus 로고
    • Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination
    • Li,S. and Waters,R. (1998) Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination. J. Bacteriol., 180, 3750-3756.
    • (1998) J. Bacteriol , vol.180 , pp. 3750-3756
    • Li, S.1    Waters, R.2
  • 6
    • 0033976873 scopus 로고    scopus 로고
    • Histone-like protein HU is required for recA gene-dependent DNA repair and SOS induction pathways in UV-irradiated Escherichia coli
    • Miyabe,I., Zhang,Q.-M., Kano,Y. and Yonei,Y. (2000) Histone-like protein HU is required for recA gene-dependent DNA repair and SOS induction pathways in UV-irradiated Escherichia coli. Int. J. Radiat. Biol., 76, 43-49.
    • (2000) Int. J. Radiat. Biol , vol.76 , pp. 43-49
    • Miyabe, I.1    Zhang, Q.-M.2    Kano, Y.3    Yonei, Y.4
  • 7
    • 0029061514 scopus 로고
    • Increased sensitivity to gamma irradiation in bacteria lacking protein HU
    • Boubrik,F. and Rouviere-Yaniv,J. (1995) Increased sensitivity to gamma irradiation in bacteria lacking protein HU. Proc. Natl Acad. Sci. U.S.A., 92, 3958-3962.
    • (1995) Proc. Natl Acad. Sci. U.S.A , vol.92 , pp. 3958-3962
    • Boubrik, F.1    Rouviere-Yaniv, J.2
  • 9
    • 0030908533 scopus 로고    scopus 로고
    • The Escherichia coli histone-like protein HU affects DNA initiation, chromosome partitionning via MukB, and cell division via MinCDE
    • Jaffé,A., Vinella,D. and D'Ari,R. (1997) The Escherichia coli histone-like protein HU affects DNA initiation, chromosome partitionning via MukB, and cell division via MinCDE. J. Bacteriol., 179, 3494-3499.
    • (1997) J. Bacteriol , vol.179 , pp. 3494-3499
    • Jaffé, A.1    Vinella, D.2    D'Ari, R.3
  • 10
    • 0031576352 scopus 로고    scopus 로고
    • Variation in HU composition during growth of Escherichia coli: The heterodimer is required for long term survival
    • Claret,L. and Rouviere-Yaniv,J. (1997) Variation in HU composition during growth of Escherichia coli: The heterodimer is required for long term survival. J. Mol. Biol., 273, 93-104.
    • (1997) J. Mol. Biol , vol.273 , pp. 93-104
    • Claret, L.1    Rouviere-Yaniv, J.2
  • 11
    • 0028136642 scopus 로고
    • DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA
    • Bonnefoy,E., Takahashi,M. and Rouviere-Yaniv,J. (1994) DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA. J. Mol. Biol., 242, 116-129.
    • (1994) J. Mol. Biol , vol.242 , pp. 116-129
    • Bonnefoy, E.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 13
    • 0028901705 scopus 로고
    • HU protein of Escherichia cob binds specifically to DNA that contains single-strand breaks or gaps
    • Castaing,B., Zelwer,C., Laval,J. and Boiteux,S. (1995) HU protein of Escherichia cob binds specifically to DNA that contains single-strand breaks or gaps. J. Biol. Chem., 270, 10291-10296.
    • (1995) J. Biol. Chem , vol.270 , pp. 10291-10296
    • Castaing, B.1    Zelwer, C.2    Laval, J.3    Boiteux, S.4
  • 14
    • 0033515646 scopus 로고    scopus 로고
    • Differential binding of the Escherichia cob HU, homodimeric forms and heterodimeric form to linear, gapped and cruciforin DNA
    • Pinson,V., Takahashi,M. and Rouviere-Yaniv,J. (1999) Differential binding of the Escherichia cob HU, homodimeric forms and heterodimeric form to linear, gapped and cruciforin DNA. J. Mol. Biol., 287 485-497.
    • (1999) J. Mol. Biol , vol.287 , pp. 485-497
    • Pinson, V.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 16
    • 36148936224 scopus 로고    scopus 로고
    • Repair of oxidized bases
    • Siede,W, Kow,Y.W. and Doetsch,P.W, eds, Taylor & Francis, New York, London, pp
    • Kow,Y.W. (2006) Repair of oxidized bases. In Siede,W., Kow,Y.W. and Doetsch,P.W. (eds), DNA Damage Recognition. Taylor & Francis, New York, London, pp. 323-338.
    • (2006) DNA Damage Recognition , pp. 323-338
    • Kow, Y.W.1
  • 17
    • 0034429631 scopus 로고    scopus 로고
    • Detection of abasic sites and oxidative DNA base damage using an ELISA-hke assay
    • Kow,Y.W. and Dare,A. (2000) Detection of abasic sites and oxidative DNA base damage using an ELISA-hke assay. Methods, 22, 164-169.
    • (2000) Methods , vol.22 , pp. 164-169
    • Kow, Y.W.1    Dare, A.2
  • 18
    • 0023015325 scopus 로고
    • Mutagenesis by apurinic/apyrimidinic sites
    • Loeb,L.A. and Preston,B.D. (1986) Mutagenesis by apurinic/apyrimidinic sites. Annu. Rev. Genet., 20, 201-230.
    • (1986) Annu. Rev. Genet , vol.20 , pp. 201-230
    • Loeb, L.A.1    Preston, B.D.2
  • 19
    • 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
  • 20
    • 0027236439 scopus 로고
    • Chemically altered apurinic sites in phi X174 DNA give increased mutagenesis in SOS-induced
    • Bockrath,R, Kow,Y.W. and Wallace,S.S. (1993) Chemically altered apurinic sites in phi X174 DNA give increased mutagenesis in SOS-induced. E. coli. Mutat. Res., 288, 207-214.
    • (1993) E. coli. Mutat. Res , vol.288 , pp. 207-214
    • Bockrath, R.1    Kow, Y.W.2    Wallace, S.S.3
  • 21
    • 0042709313 scopus 로고    scopus 로고
    • HU protein of Escherichia coli has a role in the repair of closely opposed lesions in DNA
    • Hashimoto,M., Imhoff,B., Ali,M.M. and Kow,Y.W. (2003) HU protein of Escherichia coli has a role in the repair of closely opposed lesions in DNA. J. Biol. Chem., 278, 28501-28507.
    • (2003) J. Biol. Chem , vol.278 , pp. 28501-28507
    • Hashimoto, M.1    Imhoff, B.2    Ali, M.M.3    Kow, Y.W.4
  • 22
    • 1842338079 scopus 로고    scopus 로고
    • Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA
    • Yao,M. and Kow,Y.W. (1997) Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA. J. Biol. Chem., 272, 30774-30779.
    • (1997) J. Biol. Chem , vol.272 , pp. 30774-30779
    • Yao, M.1    Kow, Y.W.2
  • 23
    • 0019921462 scopus 로고
    • Role of exonuclease III in the base excision repair of uracil-containing DNA
    • Taylor,A.F. and Weiss,B. (1982) Role of exonuclease III in the base excision repair of uracil-containing DNA. J. Bacteriol., 151 351-357.
    • (1982) J. Bacteriol , vol.151 , pp. 351-357
    • Taylor, A.F.1    Weiss, B.2
  • 25
    • 0025789755 scopus 로고
    • Bacteriophage-mediated generalized transduction in Escherichia coli and Salmonella typhimurium
    • Sternberg,N.L. and Maurer,R. (1991) Bacteriophage-mediated generalized transduction in Escherichia coli and Salmonella typhimurium. Methods Enzymol., 204, 18-23.
    • (1991) Methods Enzymol , vol.204 , pp. 18-23
    • Sternberg, N.L.1    Maurer, R.2
  • 26
    • 0029001186 scopus 로고
    • Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA
    • Wilson,D.M.3rd, Takeshita,M., Grollman,A.P. and Demple,B. (1995) Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA. J. Biol. Chem., 270, 16002-16007.
    • (1995) J. Biol. Chem , vol.270 , pp. 16002-16007
    • Wilson 3rd, D.M.1    Takeshita, M.2    Grollman, A.P.3    Demple, B.4
  • 27
    • 0035863849 scopus 로고    scopus 로고
    • Enzymatic processing of DNA containing tandem dihydrouracil by endonucleases III and VIII
    • Venkhataraman,R., Donald,C.D., Roy,R., You,H.J., Doetsch,P.W. and Kow,Y.W. (2001) Enzymatic processing of DNA containing tandem dihydrouracil by endonucleases III and VIII. Nucleic Acids Res., 29, 407-414.
    • (2001) Nucleic Acids Res , vol.29 , pp. 407-414
    • Venkhataraman, R.1    Donald, C.D.2    Roy, R.3    You, H.J.4    Doetsch, P.W.5    Kow, Y.W.6
  • 28
    • 0000247149 scopus 로고    scopus 로고
    • A common mechanism of action for the N-glycosylase activity of DNA N-glycosylase/AP lyases from E. coli and T4
    • Purmal,A.A, Rabow,L.E, Lampman,GW, Cunningham,R.P. and Kow,Y.W. (1996) A common mechanism of action for the N-glycosylase activity of DNA N-glycosylase/AP lyases from E. coli and T4. Mutat. Res., 364 193-207.
    • (1996) Mutat. Res , vol.364 , pp. 193-207
    • Purmal, A.A.1    Rabow, L.E.2    Lampman, G.W.3    Cunningham, R.P.4    Kow, Y.W.5
  • 29
    • 0030991774 scopus 로고    scopus 로고
    • Mechanism of action of base release by Escherichia coli Fpg protein: Role of lysine 155 in catalysis
    • Rabow,L.E. and Kow,Y.W. (1997) Mechanism of action of base release by Escherichia coli Fpg protein: Role of lysine 155 in catalysis. Biochemistry, 36, 5084-5096.
    • (1997) Biochemistry , vol.36 , pp. 5084-5096
    • Rabow, L.E.1    Kow, Y.W.2
  • 30
    • 1342324028 scopus 로고    scopus 로고
    • IHF and HU: Flexible architects of bent DNA
    • Swinger,K.K. and Rice,P.A. (2004) IHF and HU: Flexible architects of bent DNA. Curr. Opin. Struct. Biol., 14, 28-35.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 28-35
    • Swinger, K.K.1    Rice, P.A.2
  • 31
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger,K.K., Lemberg,K.M., Zhang,Y. and Rice,P.A. (2003) Flexible DNA bending in HU-DNA cocrystal structures. EMBO J., 22, 3749-3760.
    • (2003) EMBO J , vol.22 , pp. 3749-3760
    • Swinger, K.K.1    Lemberg, K.M.2    Zhang, Y.3    Rice, P.A.4
  • 32
    • 0037129922 scopus 로고    scopus 로고
    • The role of surface-exposed lysines in wrapping DNA about the bacterial histone-like protein HU
    • Grove,A. and Saavedra,T.C. (2002) The role of surface-exposed lysines in wrapping DNA about the bacterial histone-like protein HU. Biochemistry, 41, 7597-7603.
    • (2002) Biochemistry , vol.41 , pp. 7597-7603
    • Grove, A.1    Saavedra, T.C.2
  • 33
    • 23944475592 scopus 로고    scopus 로고
    • Surface salt bridges modulate the DNA site size of bacterial histone-like HU proteins
    • Kamau,E., Tsihlis,N.D., Simmons,L.A. and Grove,A. (2005) Surface salt bridges modulate the DNA site size of bacterial histone-like HU proteins. Biochem. J., 390, 49-55.
    • (2005) Biochem. J , vol.390 , pp. 49-55
    • Kamau, E.1    Tsihlis, N.D.2    Simmons, L.A.3    Grove, A.4
  • 34
    • 0031052180 scopus 로고    scopus 로고
    • Making DNA do a U-turn: IHF and related proteins
    • Rice,P.A. (1997) Making DNA do a U-turn: IHF and related proteins. Curr. Opin. Struct. Biol., 7, 86-93.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 86-93
    • Rice, P.A.1
  • 35
    • 0027327311 scopus 로고    scopus 로고
    • (0000) Genetic and biochemical analysis of the integration host factor of Escherichia coli
    • Mengeritsky,G., Goldenberg,D., Mendelson,I., Giladi,H. and Oppenheim,A.B. (0000) Genetic and biochemical analysis of the integration host factor of Escherichia coli. J. Mol. Biol., 231 646-657.
    • J. Mol. Biol , vol.231 , pp. 646-657
    • Mengeritsky, G.1    Goldenberg, D.2    Mendelson, I.3    Giladi, H.4    Oppenheim, A.B.5
  • 36
    • 0000247149 scopus 로고    scopus 로고
    • A common mechanism of action for the N-glycosylase activity of DNA N-glycosylase/AP lyases from E. coli and T4
    • Purmal,A.A., Rabow,L.E., Lampman,GW., Cunningham,R.P. and Kow,Y.W. (1996) A common mechanism of action for the N-glycosylase activity of DNA N-glycosylase/AP lyases from E. coli and T4. Mutat. Res., 364, 193-207.
    • (1996) Mutat. Res , vol.364 , pp. 193-207
    • Purmal, A.A.1    Rabow, L.E.2    Lampman, G.W.3    Cunningham, R.P.4    Kow, Y.W.5
  • 37
    • 0026101901 scopus 로고
    • Stereochemical studies of the beta-eliminatibn reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichi a coli, sodium hydroxide, and Lys-Trp-Lys
    • Mazumder,A., Gerlt,J.A., Absalon,M.J., Stubbe,J., Cunningham,R.P., Withka,J. and Bolton,P.H. (1991) Stereochemical studies of the beta-eliminatibn reactions at aldehydic abasic sites in DNA: endonuclease III from Escherichi a coli, sodium hydroxide, and Lys-Trp-Lys. Biochemistry, 30, 1119-1126.
    • (1991) Biochemistry , vol.30 , pp. 1119-1126
    • Mazumder, A.1    Gerlt, J.A.2    Absalon, M.J.3    Stubbe, J.4    Cunningham, R.P.5    Withka, J.6    Bolton, P.H.7
  • 40
    • 0034416406 scopus 로고    scopus 로고
    • The histone-like protein HU binds specifically to DNA recombination and repair intermediates
    • Kamashev,D. and Rouviere-Yaniv,J. (2000) The histone-like protein HU binds specifically to DNA recombination and repair intermediates. EMBO J., 19, 6527-6535.
    • (2000) EMBO J , vol.19 , pp. 6527-6535
    • Kamashev, D.1    Rouviere-Yaniv, J.2
  • 41
    • 0020200025 scopus 로고
    • A shuttle mechanism for DNA-protein interactions. The regulation of poly(ADP-ribose) polymerase
    • Zahradka,P. and Ebisuzaki,K. (1982) A shuttle mechanism for DNA-protein interactions. The regulation of poly(ADP-ribose) polymerase. Eur. J. Biochem., 127, 579-585.
    • (1982) Eur. J. Biochem , vol.127 , pp. 579-585
    • Zahradka, P.1    Ebisuzaki, K.2
  • 42
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase beta -mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis
    • Prasad,R., Lavrik,O.I., Kim,S.J., Kedar,P., Yang,X.P., Vande Berg,B.J. and Wilson,S.H. (2001) DNA polymerase beta -mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem., 276, 2411-32414.
    • (2001) J. Biol. Chem , vol.276 , pp. 2411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6    Wilson, S.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.