메뉴 건너뛰기




Volumn 60, Issue 5, 2015, Pages 755-768

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN; PARP2 PROTEIN, HUMAN;

EID: 84952876742     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2015.10.013     Document Type: Article
Times cited : (247)

References (58)
  • 3
    • 67649888368 scopus 로고    scopus 로고
    • Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
    • Altmeyer M., Messner S., Hassa P.O., Fey M., Hottiger M.O. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites. Nucleic Acids Res. 2009, 37:3723-3738.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3723-3738
    • Altmeyer, M.1    Messner, S.2    Hassa, P.O.3    Fey, M.4    Hottiger, M.O.5
  • 7
    • 0030031666 scopus 로고    scopus 로고
    • Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide
    • Bell C.E., Eisenberg D. Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. Biochemistry 1996, 35:1137-1149.
    • (1996) Biochemistry , vol.35 , pp. 1137-1149
    • Bell, C.E.1    Eisenberg, D.2
  • 8
    • 84875939839 scopus 로고    scopus 로고
    • Mapping PARP-1 auto-ADP-ribosylation sites by liquid chromatography-tandem mass spectrometry
    • Chapman J.D., Gagné J.P., Poirier G.G., Goodlett D.R. Mapping PARP-1 auto-ADP-ribosylation sites by liquid chromatography-tandem mass spectrometry. J. Proteome Res. 2013, 12:1868-1880.
    • (2013) J. Proteome Res. , vol.12 , pp. 1868-1880
    • Chapman, J.D.1    Gagné, J.P.2    Poirier, G.G.3    Goodlett, D.R.4
  • 9
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 1999, 342:249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 11
    • 84861231399 scopus 로고    scopus 로고
    • The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art
    • De Vos M., Schreiber V., Dantzer F. The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art. Biochem. Pharmacol. 2012, 84:137-146.
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 137-146
    • De Vos, M.1    Schreiber, V.2    Dantzer, F.3
  • 12
    • 84898946550 scopus 로고    scopus 로고
    • DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues
    • DeNizio J.E., Elsässer S.J., Black B.E. DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues. Nucleic Acids Res. 2014, 42:4318-4331.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 4318-4331
    • DeNizio, J.E.1    Elsässer, S.J.2    Black, B.E.3
  • 14
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander S.W. Hydrogen exchange and mass spectrometry: A historical perspective. J. Am. Soc. Mass Spectrom. 2006, 17:1481-1489.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 15
    • 79952008439 scopus 로고    scopus 로고
    • The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger
    • Eustermann S., Videler H., Yang J.C., Cole P.T., Gruszka D., Veprintsev D., Neuhaus D. The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger. J. Mol. Biol. 2011, 407:149-170.
    • (2011) J. Mol. Biol. , vol.407 , pp. 149-170
    • Eustermann, S.1    Videler, H.2    Yang, J.C.3    Cole, P.T.4    Gruszka, D.5    Veprintsev, D.6    Neuhaus, D.7
  • 19
    • 84917739517 scopus 로고    scopus 로고
    • ARTD1 (PARP1) activation and NAD(+) in DNA repair and cell death
    • Fouquerel E., Sobol R.W. ARTD1 (PARP1) activation and NAD(+) in DNA repair and cell death. DNA Repair (Amst.) 2014, 23:27-32.
    • (2014) DNA Repair (Amst.) , vol.23 , pp. 27-32
    • Fouquerel, E.1    Sobol, R.W.2
  • 22
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson B.A., Kraus W.L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell Biol. 2012, 13:411-424.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 23
    • 84892616285 scopus 로고    scopus 로고
    • Evaluation and structural basis for the inhibition of tankyrases by PARP inhibitors
    • Haikarainen T., Narwal M., Joensuu P., Lehtiö L. Evaluation and structural basis for the inhibition of tankyrases by PARP inhibitors. ACS Med. Chem. Lett. 2014, 5:18-22.
    • (2014) ACS Med. Chem. Lett. , vol.5 , pp. 18-22
    • Haikarainen, T.1    Narwal, M.2    Joensuu, P.3    Lehtiö, L.4
  • 24
    • 0035969987 scopus 로고    scopus 로고
    • Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange
    • Hoofnagle A.N., Resing K.A., Goldsmith E.J., Ahn N.G. Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange. Proc. Natl. Acad. Sci. USA 2001, 98:956-961.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 956-961
    • Hoofnagle, A.N.1    Resing, K.A.2    Goldsmith, E.J.3    Ahn, N.G.4
  • 26
    • 0025640847 scopus 로고
    • The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA
    • Ikejima M., Noguchi S., Yamashita R., Ogura T., Sugimura T., Gill D.M., Miwa M. The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J. Biol. Chem. 1990, 265:21907-21913.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21907-21913
    • Ikejima, M.1    Noguchi, S.2    Yamashita, R.3    Ogura, T.4    Sugimura, T.5    Gill, D.M.6    Miwa, M.7
  • 27
    • 0348147641 scopus 로고    scopus 로고
    • The discovery and synthesis of novel adenosine substituted 2,3-dihydro-1H-isoindol-1-ones: potent inhibitors of poly(ADP-ribose) polymerase-1 (PARP-1)
    • Jagtap P.G., Southan G.J., Baloglu E., Ram S., Mabley J.G., Marton A., Salzman A., Szabó C. The discovery and synthesis of novel adenosine substituted 2,3-dihydro-1H-isoindol-1-ones: potent inhibitors of poly(ADP-ribose) polymerase-1 (PARP-1). Bioorg. Med. Chem. Lett. 2004, 14:81-85.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 81-85
    • Jagtap, P.G.1    Southan, G.J.2    Baloglu, E.3    Ram, S.4    Mabley, J.G.5    Marton, A.6    Salzman, A.7    Szabó, C.8
  • 28
    • 84922361077 scopus 로고    scopus 로고
    • The PDB_REDO server for macromolecular structure model optimization
    • Joosten R.P., Long F., Murshudov G.N., Perrakis A. The PDB_REDO server for macromolecular structure model optimization. IUCrJ 2014, 1:213-220.
    • (2014) IUCrJ , vol.1 , pp. 213-220
    • Joosten, R.P.1    Long, F.2    Murshudov, G.N.3    Perrakis, A.4
  • 30
    • 33646948075 scopus 로고    scopus 로고
    • Genetic and biochemical properties of streptococcal NAD-glycohydrolase inhibitor
    • Kimoto H., Fujii Y., Hirano S., Yokota Y., Taketo A. Genetic and biochemical properties of streptococcal NAD-glycohydrolase inhibitor. J. Biol. Chem. 2006, 281:9181-9189.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9181-9189
    • Kimoto, H.1    Fujii, Y.2    Hirano, S.3    Yokota, Y.4    Taketo, A.5
  • 31
    • 84873524967 scopus 로고    scopus 로고
    • PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
    • Langelier M.F., Pascal J.M. PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis. Curr. Opin. Struct. Biol. 2013, 23:134-143.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 134-143
    • Langelier, M.F.1    Pascal, J.M.2
  • 32
    • 41549108573 scopus 로고    scopus 로고
    • A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation
    • Langelier M.F., Servent K.M., Rogers E.E., Pascal J.M. A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation. J. Biol. Chem. 2008, 283:4105-4114.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4105-4114
    • Langelier, M.F.1    Servent, K.M.2    Rogers, E.E.3    Pascal, J.M.4
  • 33
    • 77953305213 scopus 로고    scopus 로고
    • The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction
    • Langelier M.F., Ruhl D.D., Planck J.L., Kraus W.L., Pascal J.M. The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction. J. Biol. Chem. 2010, 285:18877-18887.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18877-18887
    • Langelier, M.F.1    Ruhl, D.D.2    Planck, J.L.3    Kraus, W.L.4    Pascal, J.M.5
  • 34
    • 79953176276 scopus 로고    scopus 로고
    • Crystal structures of poly(ADP-ribose) polymerase-1 (PARP-1) zinc fingers bound to DNA: structural and functional insights into DNA-dependent PARP-1 activity
    • Langelier M.F., Planck J.L., Roy S., Pascal J.M. Crystal structures of poly(ADP-ribose) polymerase-1 (PARP-1) zinc fingers bound to DNA: structural and functional insights into DNA-dependent PARP-1 activity. J. Biol. Chem. 2011, 286:10690-10701.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10690-10701
    • Langelier, M.F.1    Planck, J.L.2    Roy, S.3    Pascal, J.M.4
  • 35
    • 80054075321 scopus 로고    scopus 로고
    • Purification of human PARP-1 and PARP-1 domains from Escherichia coli for structural and biochemical analysis
    • Langelier M.F., Planck J.L., Servent K.M., Pascal J.M. Purification of human PARP-1 and PARP-1 domains from Escherichia coli for structural and biochemical analysis. Methods Mol. Biol. 2011, 780:209-226.
    • (2011) Methods Mol. Biol. , vol.780 , pp. 209-226
    • Langelier, M.F.1    Planck, J.L.2    Servent, K.M.3    Pascal, J.M.4
  • 36
    • 84860806404 scopus 로고    scopus 로고
    • Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1
    • Langelier M.F., Planck J.L., Roy S., Pascal J.M. Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1. Science 2012, 336:728-732.
    • (2012) Science , vol.336 , pp. 728-732
    • Langelier, M.F.1    Planck, J.L.2    Roy, S.3    Pascal, J.M.4
  • 37
    • 84903977632 scopus 로고    scopus 로고
    • PARP-2 and PARP-3 are selectively activated by 5' phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1
    • Langelier M.F., Riccio A.A., Pascal J.M. PARP-2 and PARP-3 are selectively activated by 5' phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1. Nucleic Acids Res. 2014, 42:7762-7775.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 7762-7775
    • Langelier, M.F.1    Riccio, A.A.2    Pascal, J.M.3
  • 40
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 2007, 63:32-41.
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 42
    • 33646377649 scopus 로고    scopus 로고
    • Enhancement of streptolysin O activity and intrinsic cytotoxic effects of the group A streptococcal toxin, NAD-glycohydrolase
    • Michos A., Gryllos I., Håkansson A., Srivastava A., Kokkotou E., Wessels M.R. Enhancement of streptolysin O activity and intrinsic cytotoxic effects of the group A streptococcal toxin, NAD-glycohydrolase. J. Biol. Chem. 2006, 281:8216-8223.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8216-8223
    • Michos, A.1    Gryllos, I.2    Håkansson, A.3    Srivastava, A.4    Kokkotou, E.5    Wessels, M.R.6
  • 45
    • 84856879500 scopus 로고    scopus 로고
    • Structural basis of selective inhibition of human tankyrases
    • Narwal M., Venkannagari H., Lehtiö L. Structural basis of selective inhibition of human tankyrases. J. Med. Chem. 2012, 55:1360-1367.
    • (2012) J. Med. Chem. , vol.55 , pp. 1360-1367
    • Narwal, M.1    Venkannagari, H.2    Lehtiö, L.3
  • 46
    • 0142063409 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 dimerizes at a 5' recessed DNA end in vitro: a fluorescence study
    • Pion E., Bombarda E., Stiegler P., Ullmann G.M., Mély Y., de Murcia G., Gérard D. Poly(ADP-ribose) polymerase-1 dimerizes at a 5' recessed DNA end in vitro: a fluorescence study. Biochemistry 2003, 42:12409-12417.
    • (2003) Biochemistry , vol.42 , pp. 12409-12417
    • Pion, E.1    Bombarda, E.2    Stiegler, P.3    Ullmann, G.M.4    Mély, Y.5    de Murcia, G.6    Gérard, D.7
  • 48
    • 84925815358 scopus 로고    scopus 로고
    • New facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases
    • Ryu K.W., Kim D.S., Kraus W.L. New facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases. Chem. Rev. 2015, 115:2453-2481.
    • (2015) Chem. Rev. , vol.115 , pp. 2453-2481
    • Ryu, K.W.1    Kim, D.S.2    Kraus, W.L.3
  • 55
    • 44349083744 scopus 로고    scopus 로고
    • Domain C of human poly(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif
    • Tao Z., Gao P., Hoffman D.W., Liu H.W. Domain C of human poly(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif. Biochemistry 2008, 47:5804-5813.
    • (2008) Biochemistry , vol.47 , pp. 5804-5813
    • Tao, Z.1    Gao, P.2    Hoffman, D.W.3    Liu, H.W.4
  • 57
    • 84882437564 scopus 로고    scopus 로고
    • A systematic analysis of the PARP protein family identifies new functions critical for cell physiology
    • Vyas S., Chesarone-Cataldo M., Todorova T., Huang Y.H., Chang P. A systematic analysis of the PARP protein family identifies new functions critical for cell physiology. Nat. Commun. 2013, 4:2240.
    • (2013) Nat. Commun. , vol.4 , pp. 2240
    • Vyas, S.1    Chesarone-Cataldo, M.2    Todorova, T.3    Huang, Y.H.4    Chang, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.