메뉴 건너뛰기




Volumn 5, Issue 3, 2013, Pages

Prokaryotic nucleotide excision repair

Author keywords

[No Author keywords available]

Indexed keywords

CHO PROTEIN, E COLI; DEOXYRIBONUCLEASE; ENDODEOXYRIBONUCLEASE UVRABC; ESCHERICHIA COLI PROTEIN; MULTIPROTEIN COMPLEX; NUCLEOTIDE;

EID: 84874744349     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a012591     Document Type: Article
Times cited : (141)

References (117)
  • 1
    • 0034739530 scopus 로고    scopus 로고
    • A physical interaction of UvrD with nucleotide excision repair protein UvrB
    • Ahn B. 2000. A physical interaction of UvrD with nucleotide excision repair protein UvrB. Mol Cells 10: 592-597.
    • (2000) Mol Cells , vol.10 , pp. 592-597
    • Ahn, B.1
  • 3
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind L, Walker DR, Koonin EV. 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
  • 4
    • 29144437721 scopus 로고    scopus 로고
    • Structural basis for transcription-coupled repair: The N terminus of Mfd resembles UvrB with degenerate ATPase motifs
    • Assenmacher N, Wenig K, Lammens A, Hopfner KP. 2006. Structural basis for transcription-coupled repair: The N terminus of Mfd resembles UvrB with degenerate ATPase motifs. J Mol Biol 355: 675-683.
    • (2006) J Mol Biol , vol.355 , pp. 675-683
    • Assenmacher, N.1    Wenig, K.2    Lammens, A.3    Hopfner, K.P.4
  • 6
    • 0001408659 scopus 로고
    • Release of ultraviolet light-induced thymine dimers from DNA in E
    • Boyce RP, Howard-Flanders P. 1964. Release of ultraviolet light-induced thymine dimers from DNA in E. coli K-12. Proc Natl Acad Sci 51: 293-300.
    • (1964) Coli K-12. Proc Natl Acad Sci , vol.51 , pp. 293-300
    • Boyce, R.P.1    Howard-Flanders, P.2
  • 7
    • 15444357274 scopus 로고    scopus 로고
    • A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo
    • Brosh RM Jr, Matson SW. 1997. A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo. J Biol Chem 272: 572-579.
    • (1997) J Biol Chem , vol.272 , pp. 572-579
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 8
    • 57749188239 scopus 로고    scopus 로고
    • Differential nucleotide excision repair susceptibility of bulky DNA adducts in different sequence contexts: Hierarchies of recognition signals
    • Cai Y, Patel DJ, Geacintov NE, Broyde S. 2009. Differential nucleotide excision repair susceptibility of bulky DNA adducts in different sequence contexts: Hierarchies of recognition signals. J Mol Biol 385: 30-44.
    • (2009) J Mol Biol , vol.385 , pp. 30-44
    • Cai, Y.1    Patel, D.J.2    Geacintov, N.E.3    Broyde, S.4
  • 9
    • 0000134619 scopus 로고
    • UV-radiation from the young sun and oxygen and ozone levels in the prebiological paleoatmosphere
    • Canuto VM, Levine JS, Augustsson TR, Imhoff CL. 1982. UV-radiation from the young sun and oxygen and ozone levels in the prebiological paleoatmosphere. Nature 296: 816-820.
    • (1982) Nature , vol.296 , pp. 816-820
    • Canuto, V.M.1    Levine, J.S.2    Augustsson, T.R.3    Imhoff, C.L.4
  • 10
    • 1842379671 scopus 로고
    • Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the uvrABC protein complex
    • Caron PR, Kushner SR, Grossman L. 1985. Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the uvrABC protein complex. Proc Natl Acad Sci 82: 4925-4929.
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 4925-4929
    • Caron, P.R.1    Kushner, S.R.2    Grossman, L.3
  • 12
    • 79952271901 scopus 로고    scopus 로고
    • New discoveries linking transcription to DNA repair and damage tolerance pathways
    • Cohen SE, Walker GC. 2011. New discoveries linking transcription to DNA repair and damage tolerance pathways. Transcription 2: 37-40.
    • (2011) Transcription , vol.2 , pp. 37-40
    • Cohen, S.E.1    Walker, G.C.2
  • 13
    • 33748749371 scopus 로고    scopus 로고
    • The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding
    • Croteau DL, DellaVecchia MJ, Wang H, Bienstock RJ, Melton MA, Van Houten B. 2006. The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding. J Biol Chem 281: 26370- 26381.
    • (2006) J Biol Chem , vol.281 , pp. 26370
    • Croteau, D.L.1    Dellavecchia, M.J.2    Wang, H.3    Bienstock, R.J.4    Melton, M.A.5    van Houten, B.6
  • 14
    • 39149131021 scopus 로고    scopus 로고
    • Cooperative damage recognition by UvrA and UvrB: Identification of UvrA residues that mediate DNA binding
    • Croteau DL, DellaVecchia MJ, Perera L, Van Houten B. 2008. Cooperative damage recognition by UvrA and UvrB: Identification of UvrA residues that mediate DNA binding. DNA Repair (Amst) 7: 392-404.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 392-404
    • Croteau, D.L.1    Dellavecchia, M.J.2    Perera, L.3    van Houten, B.4
  • 16
    • 84857712462 scopus 로고    scopus 로고
    • Nucleotide excision repair (NER) machin-ery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface
    • Deaconescu AM, Sevostyanova A, Artsimovitch I, Grig-orieff N. 2012. Nucleotide excision repair (NER) machin-ery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc Natl Acad Sci 109: 3353-3358.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 3353-3358
    • Deaconescu, A.M.1    Sevostyanova, A.2    Artsimovitch, I.3    Grig-Orieff, N.4
  • 18
    • 79953187302 scopus 로고    scopus 로고
    • Superfamily I helicases as modular components of DNA-processing machines
    • Dillingham MS. 2011. Superfamily I helicases as modular components of DNA-processing machines. Biochem Soc Trans 39: 413-423.
    • (2011) Biochem Soc Trans , vol.39 , pp. 413-423
    • Dillingham, M.S.1
  • 19
    • 0022539339 scopus 로고
    • Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins
    • Doolittle RF, Johnson MS, Husain I, Van Houten B, Thomas DC, Sancar A. 1986. Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins. Nature 323: 451-453.
    • (1986) Nature , vol.323 , pp. 451-453
    • Doolittle, R.F.1    Johnson, M.S.2    Husain, I.3    van Houten, B.4    Thomas, D.C.5    Sancar, A.6
  • 20
    • 84874722387 scopus 로고    scopus 로고
    • DNA damage and transcription elongation: Consequences and RNA integrity
    • (ed. Dreij K, Burns JA, Dimitri A, Nirenstein L, Noujnykh T, Scicchitano DA, Wiley-VCH, Weinheim, Germany
    • Dreij K, Burns JA, Dimitri A, Nirenstein L, Noujnykh T, Scicchitano DA. 2008. DNA damage and transcription elongation: Consequences and RNA integrity. In The chemical biology of DNA damage (ed. Dreij K, Burns JA, Dimitri A, Nirenstein L, Noujnykh T, Scicchitano DA), pp. 399-437. Wiley-VCH, Weinheim, Germany.
    • (2008) The Chemical Biology of DNA Damage , pp. 399-437
    • Dreij, K.1    Burns, J.A.2    Dimitri, A.3    Nirenstein, L.4    Noujnykh, T.5    Scicchitano, D.A.6
  • 22
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA
    • Fischer CJ, Maluf NK, Lohman TM. 2004. Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA. J Mol Biol 344: 1287-1309.
    • (2004) J Mol Biol , vol.344 , pp. 1287-1309
    • Fischer, C.J.1    Maluf, N.K.2    Lohman, T.M.3
  • 23
    • 77952105400 scopus 로고    scopus 로고
    • Scanning the DNA for damage by the nucleotide excision repair machinery
    • Goosen N. 2010. Scanning the DNA for damage by the nucleotide excision repair machinery. DNA Repair (Amst) 9: 593-596.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 593-596
    • Goosen, N.1
  • 25
    • 0025363116 scopus 로고
    • Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems
    • Gorbalenya AE, Koonin EV. 1990. Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems. J Mol Biol 213: 583-591.
    • (1990) J Mol Biol , vol.213 , pp. 583-591
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 26
    • 46449110879 scopus 로고    scopus 로고
    • Key role of Mfd in the development of fluoroquinolone resistance in Campylobacter jejuni
    • Han J, Sahin O, Barton YW, Zhang Q. 2008. Key role of Mfd in the development of fluoroquinolone resistance in Campylobacter jejuni. PLoS Pathog 4: e1000083.
    • (2008) PLoS Pathog , vol.4 , pp. 1000083
    • Han, J.1    Sahin, O.2    Barton, Y.W.3    Zhang, Q.4
  • 27
    • 0033600923 scopus 로고    scopus 로고
    • Oligomerization of the UvrB nucleotide excision repair protein of Escherichia coli
    • Hildebrand EL, Grossman L. 1999. Oligomerization of the UvrB nucleotide excision repair protein of Escherichia coli. J Biol Chem 274: 27885-27890.
    • (1999) J Biol Chem , vol.274 , pp. 27885-27890
    • Hildebrand, E.L.1    Grossman, L.2
  • 28
    • 0037398027 scopus 로고    scopus 로고
    • Rad50/SMC proteins and ABC transporters: Unifying concepts from high-resolution structures
    • Hopfner KP, Tainer JA. 2003. Rad50/SMC proteins and ABC transporters: Unifying concepts from high-resolution structures. Curr Opin Struct Biol 13: 249-255.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 249-255
    • Hopfner, K.P.1    Tainer, J.A.2
  • 30
    • 0028925960 scopus 로고
    • Structure and function of the UvrB protein
    • Hsu DS, Kim ST, Sun Q, Sancar A. 1995. Structure and function of the UvrB protein. J Biol Chem 270: 8319- 8327.
    • (1995) J Biol Chem , vol.270 , pp. 8319
    • Hsu, D.S.1    Kim, S.T.2    Sun, Q.3    Sancar, A.4
  • 31
    • 0040581590 scopus 로고
    • Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease
    • Husain I, Van Houten B, Thomas DC, Abdel-Monem M, Sancar A. 1985. Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease. Proc Natl Acad Sci 82: 6774-6778.
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 6774-6778
    • Husain, I.1    van Houten, B.2    Thomas, D.C.3    Abdel-Monem, M.4    Sancar, A.5
  • 32
    • 41849092328 scopus 로고    scopus 로고
    • DNA tandem lesion repair by strand displacement synthesis and nucleotide excision repair
    • Imoto S, Bransfield LA, Croteau DL, Van Houten B, Greenberg MM. 2008. DNA tandem lesion repair by strand displacement synthesis and nucleotide excision repair. Biochemistry 47: 4306-4316.
    • (2008) Biochemistry , vol.47 , pp. 4306-4316
    • Imoto, S.1    Bransfield, L.A.2    Croteau, D.L.3    van Houten, B.4    Greenberg, M.M.5
  • 33
    • 79551624662 scopus 로고    scopus 로고
    • Structure of UvrA nucleotide excision repair protein in complex with modified DNA
    • Jaciuk M, Nowak E, Skowronek K, Tanska A, Nowotny M. 2011. Structure of UvrA nucleotide excision repair protein in complex with modified DNA. Nat Struct Mol Biol 18: 191-197.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 191-197
    • Jaciuk, M.1    Nowak, E.2    Skowronek, K.3    Tanska, A.4    Nowotny, M.5
  • 34
    • 70349774465 scopus 로고    scopus 로고
    • Exploring damage recognition models in prokaryotic nucleotide excision repair with a benzo[a]--pyrene-derived lesion in UvrB
    • Jia L, Kropachev K, Ding S, Van Houten B, Geacintov NE, Broyde S. 2009. Exploring damage recognition models in prokaryotic nucleotide excision repair with a benzo[a]--pyrene-derived lesion in UvrB. Biochemistry 48: 8948- 8957.
    • (2009) Biochemistry , vol.48 , pp. 8948
    • Jia, L.1    Kropachev, K.2    Ding, S.3    van Houten, B.4    Geacintov, N.E.5    Broyde, S.6
  • 35
    • 0035102126 scopus 로고    scopus 로고
    • Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair
    • Junop MS, Obmolova G, Rausch K, Hsieh P, Yang W. 2001. Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair. Mol Cell 7: 1-12.
    • (2001) Mol Cell , vol.7 , pp. 1-12
    • Junop, M.S.1    Obmolova, G.2    Rausch, K.3    Hsieh, P.4    Yang, W.5
  • 36
    • 77649264800 scopus 로고    scopus 로고
    • Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single-molecule imaging of quantum-dot-labeled proteins
    • Kad NM, Wang H, Kennedy GG, Warshaw DM, Van Houten B. 2010. Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single-molecule imaging of quantum-dot-labeled proteins. Mol Cell 37: 702-713.
    • (2010) Mol Cell , vol.37 , pp. 702-713
    • Kad, N.M.1    Wang, H.2    Kennedy, G.G.3    Warshaw, D.M.4    van Houten, B.5
  • 37
    • 33846531362 scopus 로고    scopus 로고
    • Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad
    • Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C. 2007. Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad. EMBO J 26: 613- 622.
    • (2007) EMBO J , vol.26 , pp. 613
    • Karakas, E.1    Truglio, J.J.2    Croteau, D.3    Rhau, B.4    Wang, L.5    van Houten, B.6    Kisker, C.7
  • 38
    • 17044377705 scopus 로고    scopus 로고
    • Variations on the ABC
    • Lebbink JH, Sixma TK. 2005. Variations on the ABC. Structure 13: 498-500.
    • (2005) Structure , vol.13 , pp. 498-500
    • Lebbink, J.H.1    Sixma, T.K.2
  • 39
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee JY, Yang W. 2006. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell 127: 1349- 1360.
    • (2006) Cell , vol.127 , pp. 1349
    • Lee, J.Y.1    Yang, W.2
  • 40
    • 0026722539 scopus 로고
    • Active site of (A)BC excinuclease. I. Evidence for 5 incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466, and His538 residues
    • Lin JJ, Sancar A. 1992. Active site of (A)BC excinuclease. I. Evidence for 5 incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466, and His538 residues. J Biol Chem 267: 17688-17692.
    • (1992) J Biol Chem , vol.267 , pp. 17688-17692
    • Lin, J.J.1    Sancar, A.2
  • 41
    • 79960372834 scopus 로고    scopus 로고
    • Probing for DNA damage with b-hairpins: Similarities in incision efficiencies of bulky DNA adducts by prokaryotic and human nucleotide excision repair systems in vitro
    • Liu Y, Reeves D, Kropachev K, Cai Y, Ding S, Kolbanovskiy M, Kolbanovskiy A, Bolton JL, Broyde S, Van Houten B, et al. 2011. Probing for DNA damage with b-hairpins: Similarities in incision efficiencies of bulky DNA adducts by prokaryotic and human nucleotide excision repair systems in vitro. DNA Repair (Amst) 10: 684-696.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 684-696
    • Liu, Y.1    Reeves, D.2    Kropachev, K.3    Cai, Y.4    Ding, S.5    Kolbanovskiy, M.6    Kolbanovskiy, A.7    Bolton, J.L.8    Broyde, S.9    van Houten, B.10
  • 42
    • 4143115811 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Locher KP. 2004. Structure and mechanism of ABC transporters. Curr Opin Struct Biol 14: 426-431.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 426-431
    • Locher, K.P.1
  • 43
    • 0032717259 scopus 로고    scopus 로고
    • Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus
    • Machius M, Henry L, Palnitkar M, Deisenhofer J. 1999. Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus. Proc Natl Acad Sci 96: 11717-11722.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 11717-11722
    • Machius, M.1    Henry, L.2    Palnitkar, M.3    Deisenhofer, J.4
  • 44
    • 33644855067 scopus 로고    scopus 로고
    • Base flipping in nucleotide excision repair
    • Malta E, Moolenaar GF, Goosen N. 2006. Base flipping in nucleotide excision repair. J Biol Chem 281: 2184-2194.
    • (2006) J Biol Chem , vol.281 , pp. 2184-2194
    • Malta, E.1    Moolenaar, G.F.2    Goosen, N.3
  • 45
    • 34547797856 scopus 로고    scopus 로고
    • Dynamics of the UvrABC nucleotide excision repair proteins analyzed by fluorescence resonance energy transfer
    • Malta E, Moolenaar GF, Goosen N. 2007. Dynamics of the UvrABC nucleotide excision repair proteins analyzed by fluorescence resonance energy transfer. Biochemistry 46: 9080-9088.
    • (2007) Biochemistry , vol.46 , pp. 9080-9088
    • Malta, E.1    Moolenaar, G.F.2    Goosen, N.3
  • 47
    • 70349881783 scopus 로고    scopus 로고
    • The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair
    • Manelyte L, Guy CP, Smith RM, Dillingham MS, McGlynn P, Savery NJ. 2009. The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair. DNA Repair (Amst) 8: 1300- 1310.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1300
    • Manelyte, L.1    Guy, C.P.2    Smith, R.M.3    Dillingham, M.S.4    McGlynn, P.5    Savery, N.J.6
  • 48
    • 78649968104 scopus 로고    scopus 로고
    • Regulation and rate enhancement during transcription-coupled DNA repair
    • Manelyte L, Kim YI, Smith AJ, Smith RM, Savery NJ. 2010. Regulation and rate enhancement during transcription-coupled DNA repair. Mol Cell 40: 714-724.
    • (2010) Mol Cell , vol.40 , pp. 714-724
    • Manelyte, L.1    Kim, Y.I.2    Smith, A.J.3    Smith, R.M.4    Savery, N.J.5
  • 49
    • 33749120512 scopus 로고    scopus 로고
    • The UvrD helicase and its modulation by the mismatch repair protein MutL
    • Matson SW, Robertson AB. 2006. The UvrD helicase and its modulation by the mismatch repair protein MutL. Nucleic Acids Res 34: 4089-4097.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4089-4097
    • Matson, S.W.1    Robertson, A.B.2
  • 50
    • 84862763199 scopus 로고    scopus 로고
    • The conflict between DNA replication and transcription
    • McGlynn P, Savery N., Dillingham MS. 2012. The conflict between DNA replication and transcription. Mol Microbiol 85: 12-20.
    • (2012) Mol Microbiol , vol.85 , pp. 12-20
    • McGlynn, P.1    Savery, N.2    Dillingham, M.S.3
  • 52
    • 0023665604 scopus 로고
    • Regulation of the Escherichia coli excision repair gene uvrC. Overlap between the uvrC structural gene and the region coding for a 24 kD protein
    • Moolenaar GF, van Sluis CA, Backendorf C, van de Putte P. 1987. Regulation of the Escherichia coli excision repair gene uvrC. Overlap between the uvrC structural gene and the region coding for a 24 kD protein. Nucleic Acids Res 15: 4273-4289.
    • (1987) Nucleic Acids Res , vol.15 , pp. 4273-4289
    • Moolenaar, G.F.1    van Sluis, C.A.2    Backendorf, C.3    van de Putte, P.4
  • 54
    • 0032567471 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli damage-independent UvrBC endonuclease activity
    • Moolenaar GF, Bazuine M, van Knippenberg IC, Visse R, Goosen N. 1998. Characterization of the Escherichia coli damage-independent UvrBC endonuclease activity. J Biol Chem 273: 34896-34903.
    • (1998) J Biol Chem , vol.273 , pp. 34896-34903
    • Moolenaar, G.F.1    Bazuine, M.2    van Knippenberg, I.C.3    Visse, R.4    Goosen, N.5
  • 56
    • 0035503314 scopus 로고    scopus 로고
    • Clue to damage recognition by UvrB: Residues in the b-hairpin structure prevent binding to non-damaged DNA
    • Moolenaar GF, Höglund L, Goosen N. 2001. Clue to damage recognition by UvrB: Residues in the b-hairpin structure prevent binding to non-damaged DNA. EMBO J 20: 6140-6149.
    • (2001) EMBO J , vol.20 , pp. 6140-6149
    • Moolenaar, G.F.1    Höglund, L.2    Goosen, N.3
  • 58
    • 19344378508 scopus 로고    scopus 로고
    • Binding of the UvrB dimer to non-damaged and damaged DNA: Residues Y92 and Y93 influence the stability of both subunits
    • Moolenaar GF, Schut M, Goosen N. 2005. Binding of the UvrB dimer to non-damaged and damaged DNA: Residues Y92 and Y93 influence the stability of both subunits. DNA Repair (Amst) 4: 699-713.
    • (2005) DNA Repair (Amst) , vol.4 , pp. 699-713
    • Moolenaar, G.F.1    Schut, M.2    Goosen, N.3
  • 59
    • 70350643700 scopus 로고    scopus 로고
    • An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd
    • Murphy MN, Gong P, Ralto K, Manelyte L, Savery N., Theis K. 2009. An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd. Nucleic Acids Res 37: 6042-6053.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6042-6053
    • Murphy, M.N.1    Gong, P.2    Ralto, K.3    Manelyte, L.4    Savery, N.5    Theis, K.6
  • 60
    • 0033376420 scopus 로고    scopus 로고
    • Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair
    • Nakagawa N, Sugahara M, Masui R, Kato R, Fukuyama K, Kuramitsu S. 1999. Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair. J Biochem 126: 986-990.
    • (1999) J Biochem , vol.126 , pp. 986-990
    • Nakagawa, N.1    Sugahara, M.2    Masui, R.3    Kato, R.4    Fukuyama, K.5    Kuramitsu, S.6
  • 62
    • 0024441308 scopus 로고
    • Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in UvrA protein of Escherichia coli
    • Navaratnam S, Myles GM, Strange RW, Sancar A. 1989. Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in UvrA protein of Escherichia coli. J Biol Chem 264: 16067- 16071.
    • (1989) J Biol Chem , vol.264 , pp. 16067
    • Navaratnam, S.1    Myles, G.M.2    Strange, R.W.3    Sancar, A.4
  • 64
    • 0024371067 scopus 로고
    • The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex
    • Orren DK, Sancar A. 1989. The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex. Proc Natl Acad Sci 86: 5237-5241.
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 5237-5241
    • Orren, D.K.1    Sancar, A.2
  • 65
    • 0026595890 scopus 로고
    • Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I
    • Orren DK, Selby CP, Hearst JE, Sancar A. 1992. Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I. J Biol Chem 267: 780-788.
    • (1992) J Biol Chem , vol.267 , pp. 780-788
    • Orren, D.K.1    Selby, C.P.2    Hearst, J.E.3    Sancar, A.4
  • 66
    • 38349057357 scopus 로고    scopus 로고
    • Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding
    • Pakotiprapha D, Inuzuka Y, Bowman BR, Moolenaar GF, Goosen N, Jeruzalmi D, Verdine GL. 2008. Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Mol Cell 29: 122-133.
    • (2008) Mol Cell , vol.29 , pp. 122-133
    • Pakotiprapha, D.1    Inuzuka, Y.2    Bowman, B.R.3    Moolenaar, G.F.4    Goosen, N.5    Jeruzalmi, D.6    Verdine, G.L.7
  • 68
    • 75749150810 scopus 로고    scopus 로고
    • Direct restart of a replication fork stalled by a head-on RNA polymerase
    • Pomerantz RT, O'Donnell M. 2010. Direct restart of a replication fork stalled by a head-on RNA polymerase. Science 327: 590-592.
    • (2010) Science , vol.327 , pp. 590-592
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 69
  • 70
    • 34250177258 scopus 로고    scopus 로고
    • Sequence context- and temperature-dependent nucleotide excision repair of a benzo[a]pyrene diol epoxide-guanine DNA adduct catalyzed by thermophilic UvrABC proteins
    • Ruan Q, Liu T, Kolbanovskiy A, Liu Y, Ren J, Skorvaga M, Zou Y, Lader J, Malkani B, Amin S, et al. 2007. Sequence context- and temperature-dependent nucleotide excision repair of a benzo[a]pyrene diol epoxide-guanine DNA adduct catalyzed by thermophilic UvrABC proteins. Bio-chemistry 46: 7006-7015.
    • (2007) Bio-chemistry , vol.46 , pp. 7006-7015
    • Ruan, Q.1    Liu, T.2    Kolbanovskiy, A.3    Liu, Y.4    Ren, J.5    Skorvaga, M.6    Zou, Y.7    Lader, J.8    Malkani, B.9    Amin, S.10
  • 72
    • 0025127419 scopus 로고
    • Escherichia coli helicase II (UvrD) protein initiates DNA unwinding at nicks and blunt ends
    • Runyon GT, Bear DG, Lohman TM. 1990. Escherichia coli helicase II (UvrD) protein initiates DNA unwinding at nicks and blunt ends. Proc Natl Acad Sci 87: 6383-6387.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 6383-6387
    • Runyon, G.T.1    Bear, D.G.2    Lohman, T.M.3
  • 74
    • 0020641572 scopus 로고
    • A novel repair enzyme: UVRABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged region
    • Sancar A, Rupp WD. 1983. A novel repair enzyme: UVRABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged region. Cell 33: 249-260.
    • (1983) Cell , vol.33 , pp. 249-260
    • Sancar, A.1    Rupp, W.D.2
  • 76
    • 0038434901 scopus 로고
    • Escherichia coli DNA photolyase stimulates uvrABC excision nuclease in vitro
    • Sancar A, Franklin KA, Sancar GB. 1984. Escherichia coli DNA photolyase stimulates uvrABC excision nuclease in vitro. Proc Natl Acad Sci 81: 7397-7401.
    • (1984) Proc Natl Acad Sci , vol.81 , pp. 7397-7401
    • Sancar, A.1    Franklin, K.A.2    Sancar, G.B.3
  • 77
    • 34347332162 scopus 로고    scopus 로고
    • The molecular mechanism of transcription-coupled DNA repair
    • Savery NJ. 2007. The molecular mechanism of transcription-coupled DNA repair. Trends Microbiol 15: 326-333.
    • (2007) Trends Microbiol , vol.15 , pp. 326-333
    • Savery, N.J.1
  • 78
    • 79960329985 scopus 로고    scopus 로고
    • Prioritizing the repair of DNA damage that is encountered by RNA polymerase
    • Savery N. 2011. Prioritizing the repair of DNA damage that is encountered by RNA polymerase. Transcription 2: 168-172.
    • (2011) Transcription , vol.2 , pp. 168-172
    • Savery, N.1
  • 79
    • 78651191735 scopus 로고
    • The disappearance of thymine dimers from DNA: An error-correcting mechanism
    • Setlow RB, Carrier WL. 1964. The disappearance of thymine dimers from DNA: An error-correcting mechanism. Proc Natl Acad Sci 51: 226-231.
    • (1964) Proc Natl Acad Sci , vol.51 , pp. 226-231
    • Setlow, R.B.1    Carrier, W.L.2
  • 80
    • 0034661711 scopus 로고    scopus 로고
    • Common fold in helix-hairpin-helix proteins
    • Shao X, Grishin NV. 2000. Common fold in helix-hairpin-helix proteins. Nucleic Acids Res 28: 2643-2650.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2643-2650
    • Shao, X.1    Grishin, N.V.2
  • 81
    • 0026654184 scopus 로고
    • Electron mi-croscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex
    • Shi Q, Thresher R, Sancar A, Griffith J. 1992. Electron mi-croscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex. J Mol Biol 226: 425- 432.
    • (1992) J Mol Biol , vol.226 , pp. 425
    • Shi, Q.1    Thresher, R.2    Sancar, A.3    Griffith, J.4
  • 83
    • 0037059785 scopus 로고    scopus 로고
    • The b-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions
    • Skorvaga M, Theis K, Mandavilli BS, Kisker C, Van Hou-ten B. 2002. The b-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. J Biol Chem 277: 1553-1559.
    • (2002) J Biol Chem , vol.277 , pp. 1553-1559
    • Skorvaga, M.1    Theis, K.2    Mandavilli, B.S.3    Kisker, C.4    Van Hou-ten, B.5
  • 85
    • 52049097060 scopus 로고    scopus 로고
    • Effects of the bacterial transcription-repair coupling factor during transcription of DNA containing non-bulky lesions
    • Smith AJ, Savery NJ. 2008. Effects of the bacterial transcription-repair coupling factor during transcription of DNA containing non-bulky lesions. DNA Repair (Amst) 7: 1670-1679.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1670-1679
    • Smith, A.J.1    Savery, N.J.2
  • 86
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith PC, Karpowich N, Millen L, Moody JE, Rosen J, Thomas PJ, Hunt JF. 2002. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10: 139-149.
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 87
    • 34247859353 scopus 로고    scopus 로고
    • Controlling the motor activity of a transcription-repair coupling factor: Autoinhibition and the role of RNA polymerase
    • Smith AJ, Szczelkun MD, Savery NJ. 2007. Controlling the motor activity of a transcription-repair coupling factor: Autoinhibition and the role of RNA polymerase. Nucleic Acids Res 35: 1802-1811.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1802-1811
    • Smith, A.J.1    Szczelkun, M.D.2    Savery, N.J.3
  • 89
    • 0033573066 scopus 로고    scopus 로고
    • Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
    • Theis K, Chen PJ, Skorvaga M, Van Houten B, Kisker C. 1999. Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair. EMBO J 18: 6899-6907.
    • (1999) EMBO J , vol.18 , pp. 6899-6907
    • Theis, K.1    Chen, P.J.2    Skorvaga, M.3    van Houten, B.4    Kisker, C.5
  • 90
    • 0034734379 scopus 로고    scopus 로고
    • The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch
    • Theis K, Skorvaga M, Machius M, Nakagawa N, Van Houten B, Kisker C. 2000. The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch. Mutat Res 460: 277-300.
    • (2000) Mutat Res , vol.460 , pp. 277-300
    • Theis, K.1    Skorvaga, M.2    Machius, M.3    Nakagawa, N.4    van Houten, B.5    Kisker, C.6
  • 91
    • 0021847980 scopus 로고
    • Amplification and purification of UvrA, UvrB, and UvrC proteins of Escherichia coli
    • Thomas DC, Levy M, Sancar A. 1985. Amplification and purification of UvrA, UvrB, and UvrC proteins of Escherichia coli. J Biol Chem 260: 9875-9883.
    • (1985) J Biol Chem , vol.260 , pp. 9875-9883
    • Thomas, D.C.1    Levy, M.2    Sancar, A.3
  • 92
    • 64349111954 scopus 로고    scopus 로고
    • Structural and mutational analyses of Deinococcus radiodurans UvrA2 provide insight into DNA binding and damage recognition by UvrAs
    • Timmins J, Gordon E, Caria S, Leonard G, Acajjaoui S, Kuo MS, Monchois V, McSweeney S. 2009. Structural and mutational analyses of Deinococcus radiodurans UvrA2 provide insight into DNA binding and damage recognition by UvrAs. Structure 17: 547-558.
    • (2009) Structure , vol.17 , pp. 547-558
    • Timmins, J.1    Gordon, E.2    Caria, S.3    Leonard, G.4    Acajjaoui, S.5    Kuo, M.S.6    Monchois, V.7    McSweeney, S.8
  • 95
    • 33644619706 scopus 로고    scopus 로고
    • Prokaryotic nucleotide excision repair: The UvrABC system
    • Truglio JJ, Croteau DL, Van Houten B, Kisker C. 2006. Prokaryotic nucleotide excision repair: The UvrABC system. Chem Rev 106: 233-252.
    • (2006) Chem Rev , vol.106 , pp. 233-252
    • Truglio, J.J.1    Croteau, D.L.2    van Houten, B.3    Kisker, C.4
  • 97
    • 0025054962 scopus 로고
    • Nucleotide excision repair in Escherichia coli
    • Van Houten B. 1990. Nucleotide excision repair in Escherichia coli. Microbiol Rev 54: 18-51.
    • (1990) Microbiol Rev , vol.54 , pp. 18-51
    • van Houten, B.1
  • 98
    • 0027350849 scopus 로고
    • Mechanism of action of the Escherichia coli UvrABC nuclease: Clues to the damage recognition problem
    • Van Houten B, Snowden A. 1993. Mechanism of action of the Escherichia coli UvrABC nuclease: Clues to the damage recognition problem. Bioessays 15: 51-59.
    • (1993) Bioessays , vol.15 , pp. 51-59
    • van Houten, B.1    Snowden, A.2
  • 100
    • 0023701421 scopus 로고
    • Analysis of sequential steps of nucleotide excision repair in Escherichia coli using synthetic substrates containing single psoralen adducts
    • Van Houten B, Gamper H, Hearst JE, Sancar A. 1988. Analysis of sequential steps of nucleotide excision repair in Escherichia coli using synthetic substrates containing single psoralen adducts. J Biol Chem 263: 16553-16560.
    • (1988) J Biol Chem , vol.263 , pp. 16553-16560
    • van Houten, B.1    Gamper, H.2    Hearst, J.E.3    Sancar, A.4
  • 101
    • 0037022654 scopus 로고    scopus 로고
    • A cut above: Discovery of an alternative excision repair pathway in bacteria
    • Van Houten B, Eisen JA, Hanawalt PC. 2002. A cut above: Discovery of an alternative excision repair pathway in bacteria. Proc Natl Acad Sci 99: 2581-2583.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 2581-2583
    • van Houten, B.1    Eisen, J.A.2    Hanawalt, P.C.3
  • 102
  • 104
    • 0035254673 scopus 로고    scopus 로고
    • Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition
    • Verhoeven EE, Wyman C, Moolenaar GF, Hoeijmakers JH, Goosen N. 2001. Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition. EMBO J 20: 601-611.
    • (2001) EMBO J , vol.20 , pp. 601-611
    • Verhoeven, E.E.1    Wyman, C.2    Moolenaar, G.F.3    Hoeijmakers, J.H.4    Goosen, N.5
  • 106
    • 0036682613 scopus 로고    scopus 로고
    • The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands
    • Verhoeven EE, Wyman C, Moolenaar GF, Goosen N. 2002b. The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands. EMBO J 21: 4196-4205.
    • (2002) EMBO J , vol.21 , pp. 4196-4205
    • Verhoeven, E.E.1    Wyman, C.2    Moolenaar, G.F.3    Goosen, N.4
  • 107
    • 0027515237 scopus 로고
    • The first zinc-binding domain of UvrA is not essential for UvrABC-mediated DNA excision repair
    • Visse R, de Ruijter M, Ubbink M, Brandsma JA, van de Putte P. 1993. The first zinc-binding domain of UvrA is not essential for UvrABC-mediated DNA excision repair. Mutat Res 294: 263-274.
    • (1993) Mutat Res , vol.294 , pp. 263-274
    • Visse, R.1    de Ruijter, M.2    Ubbink, M.3    Brandsma, J.A.4    van de Putte, P.5
  • 108
    • 0028307439 scopus 로고
    • A mutational study of the C-terminal zinc-finger motif of the Escherichia coli UvrA protein
    • Wang J, Mueller KL, Grossman L. 1994. A mutational study of the C-terminal zinc-finger motif of the Escherichia coli UvrA protein. J Biol Chem 269: 10771-10775.
    • (1994) J Biol Chem , vol.269 , pp. 10771-10775
    • Wang, J.1    Mueller, K.L.2    Grossman, L.3
  • 109
  • 110
    • 48449106541 scopus 로고    scopus 로고
    • Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot
    • Wang H, Tessmer I, Croteau DL, Erie DA, Van Houten B. 2008. Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot. Nano Lett 8: 1631-1637.
    • (2008) Nano Lett , vol.8 , pp. 1631-1637
    • Wang, H.1    Tessmer, I.2    Croteau, D.L.3    Erie, D.A.4    van Houten, B.5
  • 111
    • 69149100489 scopus 로고    scopus 로고
    • DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway
    • Wang H, Lu M, Tang MS, Van Houten B, Ross JB, Weinfeld M, Le XC. 2009. DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway. Proc Natl Acad Sci 106: 12849-12854.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 12849-12854
    • Wang, H.1    Lu, M.2    Tang, M.S.3    van Houten, B.4    Ross, J.B.5    Weinfeld, M.6    Le, X.C.7
  • 112
    • 33750970284 scopus 로고    scopus 로고
    • Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA
    • Waters TR, Eryilmaz J, Geddes S, Barrett TE. 2006. Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA. FEBS Lett 580: 6423-6427.
    • (2006) FEBS Lett , vol.580 , pp. 6423-6427
    • Waters, T.R.1    Eryilmaz, J.2    Geddes, S.3    Barrett, T.E.4
  • 113
    • 84866949254 scopus 로고    scopus 로고
    • Crystal structure of the UvrB dimer: In-sights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes
    • Webster MP, Jukes R, Zamfir VS, Kay CW, Bagneris C, Barrett T. 2012. Crystal structure of the UvrB dimer: In-sights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes. Nucleic Acids Res 40: 8743-8758.
    • (2012) Nucleic Acids Res , vol.40 , pp. 8743-8758
    • Webster, M.P.1    Jukes, R.2    Zamfir, V.S.3    Kay, C.W.4    Bagneris, C.5    Barrett, T.6
  • 115
    • 1842308735 scopus 로고
    • Enzymatic properties of purified Escherichia coli uvrABC proteins
    • Yeung AT, Mattes WB, Oh EY, Grossman L. 1983. Enzymatic properties of purified Escherichia coli uvrABC proteins. Proc Natl Acad Sci 80: 6157-6161.
    • (1983) Proc Natl Acad Sci , vol.80 , pp. 6157-6161
    • Yeung, A.T.1    Mattes, W.B.2    Oh, E.Y.3    Grossman, L.4
  • 116
    • 0033199492 scopus 로고    scopus 로고
    • 2 B complex allows dynamic recognition of DNA damage
    • 2 B complex allows dynamic recognition of DNA damage. EMBO J 18: 4889-4901.
    • (1999) EMBO J , vol.18 , pp. 4889-4901
    • Zou, Y.1    van Houten, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.