메뉴 건너뛰기




Volumn 588, Issue 17, 2014, Pages 3023-3029

Solution phase dynamics of the DNA repair enzyme spore photoproduct lyase as probed by H/D exchange

Author keywords

DNA repair; H D exchange; Mass spectrometry; Radical SAM

Indexed keywords

AMIDE; DOUBLE STRANDED DNA; IRON; LIGAND; LYASE; OLIGONUCLEOTIDE; OXYGEN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTON; S ADENOSYLMETHIONINE; SPORE PHOTOPRODUCT LYASE; SULFUR; UNCLASSIFIED DRUG;

EID: 84906282881     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.06.011     Document Type: Article
Times cited : (4)

References (45)
  • 1
    • 34047126471 scopus 로고    scopus 로고
    • I will survive: DNA protection in bacterial spores
    • P. Setlow I will survive: DNA protection in bacterial spores Trends Microbiol. 15 2007 172 180
    • (2007) Trends Microbiol. , vol.15 , pp. 172-180
    • Setlow, P.1
  • 2
    • 0014934488 scopus 로고
    • 5-Thyminyl-5,6-dihydrothymine from DNA irradiated with ultraviolet light
    • A.J. Varghese 5-Thyminyl-5,6-dihydrothymine from DNA irradiated with ultraviolet light Biochem. Biophys. Res. Commun. 38 1970 484 490
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 484-490
    • Varghese, A.J.1
  • 3
    • 0000454531 scopus 로고
    • Thymine photoproducts but not thymine dimers found in ultraviolet-irradiated bacterial spores
    • J.E. Donnellan, and R.B. Setlow Thymine photoproducts but not thymine dimers found in ultraviolet-irradiated bacterial spores Science 149 1965 308 310
    • (1965) Science , vol.149 , pp. 308-310
    • Donnellan, J.E.1    Setlow, R.B.2
  • 4
    • 0014244318 scopus 로고
    • The ultraviolet photochemistry and photobiology of vegetative cells and spores of Bacillus megaterium
    • J.E. Donnellan Jr., and R.S. Stafford The ultraviolet photochemistry and photobiology of vegetative cells and spores of Bacillus megaterium Biophys. J. 8 1968 17 28
    • (1968) Biophys. J. , vol.8 , pp. 17-28
    • Donnellan, Jr.J.E.1    Stafford, R.S.2
  • 5
    • 0028868465 scopus 로고
    • Mechanisms for the prevention of damage to DNA in spores of Bacillus species
    • P. Setlow Mechanisms for the prevention of damage to DNA in spores of Bacillus species Annu. Rev. Microbiol. 49 1995 29 54
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 29-54
    • Setlow, P.1
  • 8
    • 79954499453 scopus 로고    scopus 로고
    • Structural insights into radical generation by the radical SAM superfamily
    • J.L. Vey, and C.L. Drennan Structural insights into radical generation by the radical SAM superfamily Chem. Rev. 111 2011 2487 2506
    • (2011) Chem. Rev. , vol.111 , pp. 2487-2506
    • Vey, J.L.1    Drennan, C.L.2
  • 10
    • 0033533642 scopus 로고    scopus 로고
    • Mechanistic studies on the repair of a novel DNA photolesion: The spore photoproduct
    • R.A. Mehl, and T.P. Begley Mechanistic studies on the repair of a novel DNA photolesion: the spore photoproduct Org. Lett. 1 1999 1065 1066
    • (1999) Org. Lett. , vol.1 , pp. 1065-1066
    • Mehl, R.A.1    Begley, T.P.2
  • 11
    • 33748756446 scopus 로고    scopus 로고
    • Characterization of an active spore photoproduct lyase, a DNA repair enzyme in the radical S-adenosylmethionine superfamily
    • J.M. Buis, J. Cheek, E. Kalliri, and J.B. Broderick Characterization of an active spore photoproduct lyase, a DNA repair enzyme in the radical S-adenosylmethionine superfamily J. Biol. Chem. 281 2006 25994 26003
    • (2006) J. Biol. Chem. , vol.281 , pp. 25994-26003
    • Buis, J.M.1    Cheek, J.2    Kalliri, E.3    Broderick, J.B.4
  • 12
    • 0037181382 scopus 로고    scopus 로고
    • Direct H atom abstraction from spore photoproduct C-6 Initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: Evidence for a reversibly generated adenosyl radical intermediate
    • J. Cheek, and J.B. Broderick Direct H atom abstraction from spore photoproduct C-6 Initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: evidence for a reversibly generated adenosyl radical intermediate J. Am. Chem. Soc. 124 2002 2860 2861
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2860-2861
    • Cheek, J.1    Broderick, J.B.2
  • 13
    • 13844280918 scopus 로고    scopus 로고
    • CC bond formation and cleavage in radical enzymes, a theoretical perspective
    • F. Himo CC bond formation and cleavage in radical enzymes, a theoretical perspective Biochim. Biophys. Acta 1707 2005 24 33
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 24-33
    • Himo, F.1
  • 15
    • 0026654184 scopus 로고
    • Electron microscopic study of (A)BC excinuclease: DNA is sharply bent in the UvrB-DNA complex
    • Q. Shi, R. Thresher, A. Sancar, and J. Griffith Electron microscopic study of (A)BC excinuclease: DNA is sharply bent in the UvrB-DNA complex J. Mol. Biol. 226 1992 425 432
    • (1992) J. Mol. Biol. , vol.226 , pp. 425-432
    • Shi, Q.1    Thresher, R.2    Sancar, A.3    Griffith, J.4
  • 16
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • A. Sancar Structure and function of DNA photolyase Biochemistry 33 1994 2 9
    • (1994) Biochemistry , vol.33 , pp. 2-9
    • Sancar, A.1
  • 17
    • 0038305458 scopus 로고    scopus 로고
    • Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors
    • A. Sancar Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors Chem. Rev. 103 6 2003 2203 2238
    • (2003) Chem. Rev. , vol.103 , Issue.6 , pp. 2203-2238
    • Sancar, A.1
  • 20
  • 21
    • 80051757503 scopus 로고    scopus 로고
    • Crystal structures and repair studies reveal the identity and the base-pairing properties of the UV-induced spore photoproduct DNA lesion
    • K. Heil, A.C. Kneuttinger, S. Schneider, U. Lischke, and T. Carell Crystal structures and repair studies reveal the identity and the base-pairing properties of the UV-induced spore photoproduct DNA lesion Chem. Eur. J. 17 2011 9651 9657
    • (2011) Chem. Eur. J. , vol.17 , pp. 9651-9657
    • Heil, K.1    Kneuttinger, A.C.2    Schneider, S.3    Lischke, U.4    Carell, T.5
  • 22
    • 84866040804 scopus 로고    scopus 로고
    • Structural insights into recognition and repair of UV-DNA damage by Spore Photoproduct Lyase, a radical SAM enzyme
    • A. Benjdia, K. Heil, T.R.M. Barends, T. Carell, and I. Schlichting Structural insights into recognition and repair of UV-DNA damage by Spore Photoproduct Lyase, a radical SAM enzyme Nucleic Acids Res. 40 18 2012 9308 9318
    • (2012) Nucleic Acids Res. , vol.40 , Issue.18 , pp. 9308-9318
    • Benjdia, A.1    Heil, K.2    Barends, T.R.M.3    Carell, T.4    Schlichting, I.5
  • 23
    • 63549096515 scopus 로고    scopus 로고
    • Damage recognition by UV damage endonuclease from Schizosaccharomyces pombe
    • K. Paspaleva, G.F. Moolenaar, and N. Goosen Damage recognition by UV damage endonuclease from Schizosaccharomyces pombe DNA Repair 8 2009 600 611
    • (2009) DNA Repair , vol.8 , pp. 600-611
    • Paspaleva, K.1    Moolenaar, G.F.2    Goosen, N.3
  • 24
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: The modern legacy of Linderstrøm-Lang
    • S. Englander, L. Mayne, Y. Bai, and T. Sosnick Hydrogen exchange: the modern legacy of Linderstrøm-Lang Protein Sci. 6 1997 1101 1109
    • (1997) Protein Sci. , vol.6 , pp. 1101-1109
    • Englander, S.1    Mayne, L.2    Bai, Y.3    Sosnick, T.4
  • 26
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • J.R. Engen Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS Anal. Chem. 81 2009 7870 7875
    • (2009) Anal. Chem. , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 27
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Z. Zhang, and D.L. Smith Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation Protein Sci. 2 1993 522 531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 30
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 13844275460 scopus 로고    scopus 로고
    • Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-SAM" protein superfamily
    • C.J. Walsby, D. Ortillo, J. Yang, M.R. Nnyepi, W.E. Broderick, B.M. Hoffman, and J.B. Broderick Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-SAM" protein superfamily Inorg. Chem. 44 2005 727 741
    • (2005) Inorg. Chem. , vol.44 , pp. 727-741
    • Walsby, C.J.1    Ortillo, D.2    Yang, J.3    Nnyepi, M.R.4    Broderick, W.E.5    Hoffman, B.M.6    Broderick, J.B.7
  • 34
    • 0037174377 scopus 로고    scopus 로고
    • An anchoring role for FeS Clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme
    • C.J. Walsby, D. Ortillo, W.E. Broderick, J.B. Broderick, and B.M. Hoffman An anchoring role for FeS Clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme J. Am. Chem. Soc. 124 2002 11270 11271
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 35
    • 11144243217 scopus 로고    scopus 로고
    • Hydrogen exchange and ligand binding: Ligand-dependent and ligand-independent protection in the Src SH3 domain
    • D. Wildes, and S. Marqusee Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain Protein Sci. 14 2005 81 88
    • (2005) Protein Sci. , vol.14 , pp. 81-88
    • Wildes, D.1    Marqusee, S.2
  • 36
    • 0023650526 scopus 로고
    • Binding of E. Coli DNA photolyase to a defined substrate containing a single T<>T dimer
    • I. Husain, and A. Sancar Binding of E. coli DNA photolyase to a defined substrate containing a single T<>T dimer Nucleic Acids Res. 15 1987 1109 1120
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1109-1120
    • Husain, I.1    Sancar, A.2
  • 37
    • 0033754441 scopus 로고    scopus 로고
    • Spore photoproduct (SP) lyase from Bacillus subtilis specifically binds to and cleaves SP (5-thyminyl-5,6-dihydrothymine) but not cyclobutane pyrimidine dimers in UV-irradiated DNA
    • T.A. Slieman, R. Rebeil, and W.L. Nicholson Spore photoproduct (SP) lyase from Bacillus subtilis specifically binds to and cleaves SP (5-thyminyl-5,6-dihydrothymine) but not cyclobutane pyrimidine dimers in UV-irradiated DNA J. Bacteriol. 182 2000 6412 6417
    • (2000) J. Bacteriol. , vol.182 , pp. 6412-6417
    • Slieman, T.A.1    Rebeil, R.2    Nicholson, W.L.3
  • 38
    • 80455155015 scopus 로고    scopus 로고
    • Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA
    • S. Kiontke, Y. Geisselbrecht, R. Pokorny, T. Carell, A. Batschauer, and L.-O. Essen Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA EMBO J. 30 2011 4437 4449
    • (2011) EMBO J. , vol.30 , pp. 4437-4449
    • Kiontke, S.1    Geisselbrecht, Y.2    Pokorny, R.3    Carell, T.4    Batschauer, A.5    Essen, L.-O.6
  • 39
    • 10044280323 scopus 로고    scopus 로고
    • Crystal structure of a photolyase bound to a CPD-Like DNA lesion after in situ repair
    • A. Mees, T. Klar, P. Gnau, U. Hennecke, A.P.M. Eker, T. Carell, and L.-O. Essen Crystal structure of a photolyase bound to a CPD-Like DNA lesion after in situ repair Science 306 2004 1789 1793
    • (2004) Science , vol.306 , pp. 1789-1793
    • Mees, A.1    Klar, T.2    Gnau, P.3    Hennecke, U.4    Eker, A.P.M.5    Carell, T.6    Essen, L.-O.7
  • 41
    • 84870393908 scopus 로고    scopus 로고
    • DNA photolyases and SP lyase: Structure and mechanism of light-dependent and independent DNA lyases
    • A. Benjdia DNA photolyases and SP lyase: structure and mechanism of light-dependent and independent DNA lyases Curr. Opin. Struct. Biol. 22 2012 711 720
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 711-720
    • Benjdia, A.1
  • 45
    • 79952328235 scopus 로고    scopus 로고
    • Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification
    • M. Kato, Y. Araiso, A. Noma, A. Nagao, T. Suzuki, R. Ishitani, and O. Nureki Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification Nucleic Acids Res. 39 2011 1576 1585
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1576-1585
    • Kato, M.1    Araiso, Y.2    Noma, A.3    Nagao, A.4    Suzuki, T.5    Ishitani, R.6    Nureki, O.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.