메뉴 건너뛰기




Volumn 379, Issue 1, 2008, Pages 28-37

Unusual Role of a Cysteine Residue in Substrate Binding and Activity of Human AP-Endonuclease 1

Author keywords

AP endonuclease; DNA base excision repair; DNA binding; human APE1; Ref 1

Indexed keywords

CYSTEINE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; HISTIDINE; MAGNESIUM; SERINE;

EID: 42749086668     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.03.052     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogenous DNA base damage in mammalian cells
    • D.E. Barnes T. Lindahl Repair and genetic consequences of endogenous DNA base damage in mammalian cells Annu. Rev. Genet. 38 2004 445 476
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 2
    • 33847666362 scopus 로고    scopus 로고
    • Intracellular trafficking and regulation of mammalian AP-endonuclease 1 (APE1), an essential DNA repair protein
    • S. Mitra T. Izumi I. Boldogh K.K. Bhakat R. Chattopadhyay B. Szczesny Intracellular trafficking and regulation of mammalian AP-endonuclease 1 (APE1), an essential DNA repair protein DNA Repair (Amst) 6 2007 461 469
    • (2007) DNA Repair (Amst) , vol.6 , pp. 461-469
    • Mitra, S.1    Izumi, T.2    Boldogh, I.3    Bhakat, K.K.4    Chattopadhyay, R.5    Szczesny, B.6
  • 3
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • P.W. Doetsch R.P. Cunningham The enzymology of apurinic/apyrimidinic endonucleases Mutat. Res. 236 1990 173 201
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 4
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: enzymology and biology
    • B. Demple L. Harrison Repair of oxidative damage to DNA: enzymology and biology Annu. Rev. Biochem. 63 1994 915 948
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 5
    • 0032190633 scopus 로고    scopus 로고
    • Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites
    • R.E. Johnson C.A. Torres-Ramos T. Izumi S. Mitra S. Prakash L. Prakash Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites Genes Dev. 12 1998 3137 3143
    • (1998) Genes Dev. , vol.12 , pp. 3137-3143
    • Johnson, R.E.1    Torres-Ramos, C.A.2    Izumi, T.3    Mitra, S.4    Prakash, S.5    Prakash, L.6
  • 6
    • 1242331845 scopus 로고    scopus 로고
    • The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe
    • B. Ribar T. Izumi S. Mitra The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe Nucleic Acids Res. 32 2004 115 126
    • (2004) Nucleic Acids Res. , vol.32 , pp. 115-126
    • Ribar, B.1    Izumi, T.2    Mitra, S.3
  • 7
    • 0035163137 scopus 로고    scopus 로고
    • Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage
    • S. Mitra I. Boldogh T. Izumi T.K. Hazra Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage Environ. Mol. Mutagen. 38 2001 180 190
    • (2001) Environ. Mol. Mutagen. , vol.38 , pp. 180-190
    • Mitra, S.1    Boldogh, I.2    Izumi, T.3    Hazra, T.K.4
  • 8
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase beta
    • S.H. Wilson Mammalian base excision repair and DNA polymerase beta Mutat. Res. 407 1998 203 215
    • (1998) Mutat. Res. , vol.407 , pp. 203-215
    • Wilson, S.H.1
  • 11
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • S. Xanthoudakis G. Miao F. Wang Y.C. Pan T. Curran Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme EMBO J. 11 1992 3323 3335
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 12
    • 14044269479 scopus 로고    scopus 로고
    • The intracellular localization of APE1/Ref-1: more than a passive phenomenon?
    • G. Tell G. Damante D. Caldwell M.R. Kelley The intracellular localization of APE1/Ref-1: more than a passive phenomenon? Antioxid. Redox Signal. 7 2005 367 384
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 367-384
    • Tell, G.1    Damante, G.2    Caldwell, D.3    Kelley, M.R.4
  • 13
    • 0027324056 scopus 로고
    • Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding
    • L.J. Walker C.N. Robson E. Black D. Gillespie I.D. Hickson Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding Mol. Cell. Biol. 13 1993 5370 5376
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5370-5376
    • Walker, L.J.1    Robson, C.N.2    Black, E.3    Gillespie, D.4    Hickson, I.D.5
  • 14
    • 0038655553 scopus 로고    scopus 로고
    • Cysteine 64 of Ref-1 is not essential for redox regulation of AP-1 DNA binding
    • J.M. Ordway D. Eberhart T. Curran Cysteine 64 of Ref-1 is not essential for redox regulation of AP-1 DNA binding Mol. Cell. Biol. 23 2003 4257 4266
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4257-4266
    • Ordway, J.M.1    Eberhart, D.2    Curran, T.3
  • 15
    • 0027985675 scopus 로고
    • A redox factor protein, ref1, is involved in negative gene regulation by extracellular calcium
    • T. Okazaki U. Chung T. Nishishita S. Ebisu S. Usuda S. Mishiro A redox factor protein, ref1, is involved in negative gene regulation by extracellular calcium J. Biol. Chem. 269 1994 27855 27862
    • (1994) J. Biol. Chem. , vol.269 , pp. 27855-27862
    • Okazaki, T.1    Chung, U.2    Nishishita, T.3    Ebisu, S.4    Usuda, S.5    Mishiro, S.6
  • 16
    • 0037331196 scopus 로고    scopus 로고
    • Implication of Ref-1 in the repression of renin gene transcription by intracellular calcium
    • S. Fuchs J. Philippe P. Corvol F. Pinet Implication of Ref-1 in the repression of renin gene transcription by intracellular calcium J. Hypertens. 21 2003 327 335
    • (2003) J. Hypertens. , vol.21 , pp. 327-335
    • Fuchs, S.1    Philippe, J.2    Corvol, P.3    Pinet, F.4
  • 17
    • 0347504848 scopus 로고    scopus 로고
    • Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene
    • K.K. Bhakat T. Izumi S.H. Yang T.K. Hazra S. Mitra Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene EMBO J. 22 2003 6299 6309
    • (2003) EMBO J. , vol.22 , pp. 6299-6309
    • Bhakat, K.K.1    Izumi, T.2    Yang, S.H.3    Hazra, T.K.4    Mitra, S.5
  • 18
    • 0030728449 scopus 로고    scopus 로고
    • The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
    • M.A. Gorman S. Morera D.G. Rothwell E. de La Fortelle C.D. Mol J.A. Tainer The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites EMBO J. 16 1997 6548 6558
    • (1997) EMBO J. , vol.16 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3    de La Fortelle, E.4    Mol, C.D.5    Tainer, J.A.6
  • 19
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]
    • C.D. Mol T. Izumi S. Mitra J.A. Tainer DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected] Nature 403 2000 451 456
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 20
    • 34249905486 scopus 로고    scopus 로고
    • A “moving metal mechanism” for substrate cleavage by the DNA repair endonuclease APE-1
    • N. Oezguen C.H. Schein S.R. Peddi T.D. Power T. Izumi W. Braun A “moving metal mechanism” for substrate cleavage by the DNA repair endonuclease APE-1 Proteins 68 2007 313 323
    • (2007) Proteins , vol.68 , pp. 313-323
    • Oezguen, N.1    Schein, C.H.2    Peddi, S.R.3    Power, T.D.4    Izumi, T.5    Braun, W.6
  • 21
    • 0032515067 scopus 로고    scopus 로고
    • Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium
    • Y. Masuda R.A.O. Bennett B. Demple Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium J. Biol. Chem. 273 1998 30360 30365
    • (1998) J. Biol. Chem. , vol.273 , pp. 30360-30365
    • Masuda, Y.1    Bennett, R.A.O.2    Demple, B.3
  • 22
    • 0034607548 scopus 로고    scopus 로고
    • Mapping the protein–DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease
    • L.H. Nguyen D. Barsky J.P. Erzberger D.M. Wilson III Mapping the protein–DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease J. Mol. Biol. 298 2000 447 459
    • (2000) J. Mol. Biol. , vol.298 , pp. 447-459
    • Nguyen, L.H.1    Barsky, D.2    Erzberger, J.P.3    Wilson, D.M.4
  • 23
  • 24
    • 0032515143 scopus 로고    scopus 로고
    • Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product
    • Y. Masuda R.A.O. Bennett B. Demple Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product J. Biol. Chem. 273 1998 30352 30359
    • (1998) J. Biol. Chem. , vol.273 , pp. 30352-30359
    • Masuda, Y.1    Bennett, R.A.O.2    Demple, B.3
  • 25
    • 0035815108 scopus 로고    scopus 로고
    • Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism
    • P.T. Beernink B.W. Segelke M.Z. Hadi J.P. Erzberger D.M. Wilson III B. Rupp Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism J. Mol. Biol. 307 2001 1023 1034
    • (2001) J. Mol. Biol. , vol.307 , pp. 1023-1034
    • Beernink, P.T.1    Segelke, B.W.2    Hadi, M.Z.3    Erzberger, J.P.4    Wilson, D.M.5    Rupp, B.6
  • 26
    • 0034734377 scopus 로고    scopus 로고
    • Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3′ ends justify the means
    • C.D. Mol D.J. Hosfield J.A. Tainer Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3′ ends justify the means Mutat. Res. 460 2000 211 229
    • (2000) Mutat. Res. , vol.460 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 27
    • 0034209946 scopus 로고    scopus 로고
    • Substitution of Asp-210 in HAP1 (APE/Ref-1) eliminates endonuclease activity but stabilises substrate binding
    • D.G. Rothwell B. Hang M.A. Gorman P.S. Freemont B. Singer I.D. Hickson Substitution of Asp-210 in HAP1 (APE/Ref-1) eliminates endonuclease activity but stabilises substrate binding Nucleic Acids Res. 28 2000 2207 2213
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2207-2213
    • Rothwell, D.G.1    Hang, B.2    Gorman, M.A.3    Freemont, P.S.4    Singer, B.5    Hickson, I.D.6
  • 28
    • 0042589136 scopus 로고    scopus 로고
    • Total sequence decomposition distinguishes functional modules, “molegos” in apurinic/apyrimidinic endonucleases
    • C.H. Schein N. Ozgun T. Izumi W. Braun Total sequence decomposition distinguishes functional modules, “molegos” in apurinic/apyrimidinic endonucleases BMC Bioinf. 3 2002 37
    • (2002) BMC Bioinf. , vol.3 , pp. 37
    • Schein, C.H.1    Ozgun, N.2    Izumi, T.3    Braun, W.4
  • 29
    • 0034866372 scopus 로고    scopus 로고
    • Redox regulation of the DNA repair function of the human AP endonuclease Ape1/ref-1
    • M.R. Kelley S.H. Parsons Redox regulation of the DNA repair function of the human AP endonuclease Ape1/ref-1 Antioxid. Redox Signal. 3 2001 671 683
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 671-683
    • Kelley, M.R.1    Parsons, S.H.2
  • 31
    • 0029001186 scopus 로고
    • Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA
    • D.M. Wilson III M. Takeshita A.P. Grollman B. Demple Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA J. Biol. Chem. 270 1995 16002 16007
    • (1995) J. Biol. Chem. , vol.270 , pp. 16002-16007
    • Wilson, D.M.1    Takeshita, M.2    Grollman, A.P.3    Demple, B.4
  • 32
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • S. Xanthoudakis T. Curran Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity EMBO J. 11 1992 653 665
    • (1992) EMBO J. , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 33
    • 0242412184 scopus 로고    scopus 로고
    • Origin of endogenous DNA abasic sites in Saccharomyces cerevisiae
    • M. Guillet S. Boiteux Origin of endogenous DNA abasic sites in Saccharomyces cerevisiae Mol. Cell Biol. 23 2003 8386 8394
    • (2003) Mol. Cell Biol. , vol.23 , pp. 8386-8394
    • Guillet, M.1    Boiteux, S.2
  • 34
    • 0024673277 scopus 로고
    • Role of exonuclease III and endonuclease IV in repair of pyrimidine dimers initiated by bacteriophage T4 pyrimidine dimer–DNA glycosylase
    • S.M. Saporito M. Gedenk R.P. Cunningham Role of exonuclease III and endonuclease IV in repair of pyrimidine dimers initiated by bacteriophage T4 pyrimidine dimer–DNA glycosylase J. Bacteriol. 171 1989 2542 2546
    • (1989) J. Bacteriol. , vol.171 , pp. 2542-2546
    • Saporito, S.M.1    Gedenk, M.2    Cunningham, R.P.3
  • 35
    • 1642494900 scopus 로고    scopus 로고
    • Effects of backbone contacts 3′ to the abasic site on the cleavage and the product binding by human apurinic/apyrimidinic endonuclease (APE1)
    • T. Izumi C.H. Schein N. Oezguen Y. Feng W. Braun Effects of backbone contacts 3′ to the abasic site on the cleavage and the product binding by human apurinic/apyrimidinic endonuclease (APE1) Biochemistry 43 2004 684 689
    • (2004) Biochemistry , vol.43 , pp. 684-689
    • Izumi, T.1    Schein, C.H.2    Oezguen, N.3    Feng, Y.4    Braun, W.5
  • 37
    • 0032574770 scopus 로고    scopus 로고
    • Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals
    • C.V. Ramana I. Boldogh T. Izumi S. Mitra Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals Proc. Natl. Acad. Sci. USA 95 1998 5061 5066
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5061-5066
    • Ramana, C.V.1    Boldogh, I.2    Izumi, T.3    Mitra, S.4
  • 39
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen J. Chandrasekhar J.D. Madura Comparison of simple potential functions for simulating liquid water J. Chem. Phys. 79 1983 926 935
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 40
    • 0242443693 scopus 로고    scopus 로고
    • Force fields for protein simulations
    • J.W. Ponder D.A. Case Force fields for protein simulations Adv. Protein Chem. 66 2003 27 85
    • (2003) Adv. Protein Chem. , vol.66 , pp. 27-85
    • Ponder, J.W.1    Case, D.A.2
  • 41
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • R. Koradi M. Billeter K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 1996 51 55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.