메뉴 건너뛰기




Volumn 20, Issue , 2014, Pages 58-70

Two steps forward, one step back: Determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers

Author keywords

DNA helicases; DNA repair; FeS cluster; High resolution optical tweezers; Nucleotide excision repair; Single molecule; Total internal reflection fluorescence microscopy (TIRFM)

Indexed keywords

BINDING PROTEIN; CHLR1 HELICASE; DNA; DNA BINDING PROTEIN; DNA HELICASE; DOUBLE STRANDED DNA; FANCJ HELICASE; HELICASE; IRON SULFUR PROTEIN; RPA2 PROTEIN; RTEL1 HELICASE; SF2 HELICASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP D PROTEIN; PROTEIN BINDING;

EID: 84904746173     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.01.013     Document Type: Article
Times cited : (26)

References (102)
  • 1
    • 84873646761 scopus 로고    scopus 로고
    • DNA helicases associated with genetic instability, cancer, and aging
    • Suhasini A.N., Brosh R.M. DNA helicases associated with genetic instability, cancer, and aging. Adv. Exp. Med. Biol. 2013, 767:123-144.
    • (2013) Adv. Exp. Med. Biol. , vol.767 , pp. 123-144
    • Suhasini, A.N.1    Brosh, R.M.2
  • 2
    • 84873653618 scopus 로고    scopus 로고
    • Overview: what are helicases?
    • Wu C.G., Spies M. Overview: what are helicases?. Adv. Exp. Med. Biol. 2013, 767:1-16.
    • (2013) Adv. Exp. Med. Biol. , vol.767 , pp. 1-16
    • Wu, C.G.1    Spies, M.2
  • 3
    • 84873677484 scopus 로고    scopus 로고
    • Roles of DNA helicases in the mediation and regulation of homologous recombination
    • Daley J.M., Niu H., Sung P. Roles of DNA helicases in the mediation and regulation of homologous recombination. Adv. Exp. Med. Biol. 2013, 767:185-202.
    • (2013) Adv. Exp. Med. Biol. , vol.767 , pp. 185-202
    • Daley, J.M.1    Niu, H.2    Sung, P.3
  • 4
    • 0025646391 scopus 로고
    • Spontaneous DNA damage and its significance for the negligible dose controversy in radiation protection
    • Billen D. Spontaneous DNA damage and its significance for the negligible dose controversy in radiation protection. Radiat. Res. 1990, 124:242-245.
    • (1990) Radiat. Res. , vol.124 , pp. 242-245
    • Billen, D.1
  • 5
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia A., Elledge S.J. The DNA damage response: making it safe to play with knives. Mol. Cell 2010, 40:179-204.
    • (2010) Mol. Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 7
    • 0037178722 scopus 로고    scopus 로고
    • Maintenance of genome stability in Saccharomyces cerevisiae
    • Kolodner R.D., Putnam C.D., Myung K. Maintenance of genome stability in Saccharomyces cerevisiae. Science 2002, 297:552-557.
    • (2002) Science , vol.297 , pp. 552-557
    • Kolodner, R.D.1    Putnam, C.D.2    Myung, K.3
  • 8
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D., Weinberg R.A. Hallmarks of cancer: the next generation. Cell 2011, 144:646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 9
    • 0034069237 scopus 로고    scopus 로고
    • Cancer, aging and cellular senescence
    • Campisi J. Cancer, aging and cellular senescence. In Vivo 2000, 14:183-188.
    • (2000) In Vivo , vol.14 , pp. 183-188
    • Campisi, J.1
  • 10
    • 38049136456 scopus 로고    scopus 로고
    • DNA damage-induced cell death: lessons from the central nervous system
    • Borges H.L., Linden R., Wang J.Y. DNA damage-induced cell death: lessons from the central nervous system. Cell Res. 2008, 18:17-26.
    • (2008) Cell Res. , vol.18 , pp. 17-26
    • Borges, H.L.1    Linden, R.2    Wang, J.Y.3
  • 11
    • 33644765799 scopus 로고    scopus 로고
    • Cell biology: ageing nucleus gets out of shape
    • Lans H., Hoeijmakers J.H. Cell biology: ageing nucleus gets out of shape. Nature 2006, 440:32-34.
    • (2006) Nature , vol.440 , pp. 32-34
    • Lans, H.1    Hoeijmakers, J.H.2
  • 14
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton M.R., Dillingham M.S., Wigley D.B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 2007, 76:23-50.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 15
    • 0027182114 scopus 로고
    • Helicases: amino acid sequence comparisons and structure-function relationships
    • Gorbalenya A.E., Koonin E.V. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 1993, 3:419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 16
    • 0034847293 scopus 로고    scopus 로고
    • Biotin-streptavidin-labeled oligonucleotides as probes of helicase mechanisms
    • Morris P.D., Tackett A.J., Raney K.D. Biotin-streptavidin-labeled oligonucleotides as probes of helicase mechanisms. Methods 2001, 23:149-159.
    • (2001) Methods , vol.23 , pp. 149-159
    • Morris, P.D.1    Tackett, A.J.2    Raney, K.D.3
  • 17
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: mechanisms and regulation
    • Lohman T.M., Tomko E.J., Wu C.G. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat. Rev. Mol. Cell Biol. 2008, 9:391-401.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 20
    • 84873408109 scopus 로고    scopus 로고
    • DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH
    • Mathieu N., Kaczmarek N., Ruthemann P., Luch P., Naegeli H. DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH. Curr. Biol. 2013.
    • (2013) Curr. Biol.
    • Mathieu, N.1    Kaczmarek, N.2    Ruthemann, P.3    Luch, P.4    Naegeli, H.5
  • 22
    • 65549113446 scopus 로고    scopus 로고
    • FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange
    • Sommers J.A., Rawtani N., Gupta R., Bugreev D.V., Mazin A.V., Cantor S.B., Brosh R.M. FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange. J. Biol. Chem. 2009, 284:7505-7517.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7505-7517
    • Sommers, J.A.1    Rawtani, N.2    Gupta, R.3    Bugreev, D.V.4    Mazin, A.V.5    Cantor, S.B.6    Brosh, R.M.7
  • 23
    • 44949114282 scopus 로고    scopus 로고
    • FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability
    • Wu Y., Shin-ya K., Brosh R.M. FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability. Mol. Cell. Biol. 2008, 28:4116-4128.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4116-4128
    • Wu, Y.1    Shin-ya, K.2    Brosh, R.M.3
  • 26
    • 0031022335 scopus 로고    scopus 로고
    • Characterization of putative human homologues of the yeast chromosome transmission fidelity gene, CHL1
    • Amann J., Kidd V.J., Lahti J.M. Characterization of putative human homologues of the yeast chromosome transmission fidelity gene, CHL1. J. Biol. Chem. 1997, 272:3823-3832.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3823-3832
    • Amann, J.1    Kidd, V.J.2    Lahti, J.M.3
  • 27
    • 84873694460 scopus 로고    scopus 로고
    • DNA helicases in NER, BER, and MMR
    • Springer, New York, M. Spies (Ed.)
    • Kuper J., Kisker C. DNA helicases in NER, BER, and MMR. DNA Helicases and DNA Motor Proteins 2013, 203-224. Springer, New York. M. Spies (Ed.).
    • (2013) DNA Helicases and DNA Motor Proteins , pp. 203-224
    • Kuper, J.1    Kisker, C.2
  • 32
    • 33845657930 scopus 로고    scopus 로고
    • The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells
    • Parish J.L., Rosa J., Wang X., Lahti J.M., Doxsey S.J., Androphy E.J. The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells. J. Cell Sci. 2006, 119:4857-4865.
    • (2006) J. Cell Sci. , vol.119 , pp. 4857-4865
    • Parish, J.L.1    Rosa, J.2    Wang, X.3    Lahti, J.M.4    Doxsey, S.J.5    Androphy, E.J.6
  • 34
    • 84876807755 scopus 로고    scopus 로고
    • Disease-causing missense mutations in human DNA helicase disorders
    • Suhasini A.N., Brosh R.M. Disease-causing missense mutations in human DNA helicase disorders. Mutat. Res./Rev. Mutat. Res. 2013, 752(2):138-152.
    • (2013) Mutat. Res./Rev. Mutat. Res. , vol.752 , Issue.2 , pp. 138-152
    • Suhasini, A.N.1    Brosh, R.M.2
  • 41
    • 63449109208 scopus 로고    scopus 로고
    • Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins
    • Wu Y., Suhasini A.N., Brosh R.M. Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins. Cell. Mol. Life Sci. 2009, 66:1209-1222.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1209-1222
    • Wu, Y.1    Suhasini, A.N.2    Brosh, R.M.3
  • 42
    • 84861551208 scopus 로고    scopus 로고
    • DNA helicase and helicase/nuclease enzymes with a conserved iron-sulfur cluster
    • Wu Y., Brosh R.M. DNA helicase and helicase/nuclease enzymes with a conserved iron-sulfur cluster. Nucleic Acids Res. 2012, 40:4247-4260.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4247-4260
    • Wu, Y.1    Brosh, R.M.2
  • 43
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf J., Makrantoni V., Ingledew W.J., Stark M.J., White M.F. The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol. Cell 2006, 23:801-808.
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 44
    • 0041344536 scopus 로고    scopus 로고
    • Characterization of the DNA damage-inducible helicase DinG from Escherichia coli
    • Voloshin O.N., Vanevski F., Khil P.P., Camerini-Otero R.D. Characterization of the DNA damage-inducible helicase DinG from Escherichia coli. J. Biol. Chem. 2003, 278:28284-28293.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28284-28293
    • Voloshin, O.N.1    Vanevski, F.2    Khil, P.P.3    Camerini-Otero, R.D.4
  • 45
    • 38349091095 scopus 로고    scopus 로고
    • The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction
    • Pugh R.A., Honda M., Leesley H., Thomas A., Lin Y., Nilges M.J., Cann I.K., Spies M. The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction. J. Biol. Chem. 2008, 283:1732-1743.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1732-1743
    • Pugh, R.A.1    Honda, M.2    Leesley, H.3    Thomas, A.4    Lin, Y.5    Nilges, M.J.6    Cann, I.K.7    Spies, M.8
  • 47
    • 0034651623 scopus 로고    scopus 로고
    • Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase
    • Hirota Y., Lahti J.M. Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase. Nucleic Acids Res. 2000, 28:917-924.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 917-924
    • Hirota, Y.1    Lahti, J.M.2
  • 49
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations
    • Fan L., Fuss J.O., Cheng Q.J., Arvai A.S., Hammel M., Roberts V.A., Cooper P.K., Tainer J.A. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 2008, 133:789-800.
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 51
    • 84857195289 scopus 로고    scopus 로고
    • Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation
    • Kuper J., Wolski S.C., Michels G., Kisker C. Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation. EMBO J. 2012, 31:494-502.
    • (2012) EMBO J. , vol.31 , pp. 494-502
    • Kuper, J.1    Wolski, S.C.2    Michels, G.3    Kisker, C.4
  • 52
    • 84857194573 scopus 로고    scopus 로고
    • Regulation of translocation polarity by helicase domain 1 in SF2B helicases
    • Pugh R.A., Wu C.G., Spies M. Regulation of translocation polarity by helicase domain 1 in SF2B helicases. EMBO J. 2012, 31:503-514.
    • (2012) EMBO J. , vol.31 , pp. 503-514
    • Pugh, R.A.1    Wu, C.G.2    Spies, M.3
  • 53
    • 77950366206 scopus 로고    scopus 로고
    • The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway
    • Rudolf J., Rouillon C., Schwarz-Linek U., White M.F. The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway. Nucleic Acids Res. 2010, 38:931-941.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 931-941
    • Rudolf, J.1    Rouillon, C.2    Schwarz-Linek, U.3    White, M.F.4
  • 54
    • 69749086880 scopus 로고    scopus 로고
    • Single-molecule analysis reveals differential effect of ssDNA-binding proteins on DNA translocation by XPD helicase
    • Honda M., Park J., Pugh R.A., Ha T., Spies M. Single-molecule analysis reveals differential effect of ssDNA-binding proteins on DNA translocation by XPD helicase. Mol. Cell 2009, 35:694-703.
    • (2009) Mol. Cell , vol.35 , pp. 694-703
    • Honda, M.1    Park, J.2    Pugh, R.A.3    Ha, T.4    Spies, M.5
  • 55
    • 84893698747 scopus 로고    scopus 로고
    • Strand specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility
    • Buechner C.N., Heil K., Michels G., Carell T., Kisker C., Tessmer I. Strand specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility. J. Biol. Chem. 2013, 289(6):3613-3624.
    • (2013) J. Biol. Chem. , vol.289 , Issue.6 , pp. 3613-3624
    • Buechner, C.N.1    Heil, K.2    Michels, G.3    Carell, T.4    Kisker, C.5    Tessmer, I.6
  • 56
    • 53549120600 scopus 로고    scopus 로고
    • Ferroplasma acidarmanus RPA2 facilitates efficient unwinding of forked DNA substrates by monomers of FacXPD helicase
    • Pugh R.A., Lin Y., Eller C., Leesley H., Cann I.K., Spies M. Ferroplasma acidarmanus RPA2 facilitates efficient unwinding of forked DNA substrates by monomers of FacXPD helicase. J. Mol. Biol. 2008, 383:982-998.
    • (2008) J. Mol. Biol. , vol.383 , pp. 982-998
    • Pugh, R.A.1    Lin, Y.2    Eller, C.3    Leesley, H.4    Cann, I.K.5    Spies, M.6
  • 57
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay J.A. Iron-sulphur clusters and the problem with oxygen. Mol. Microbiol. 2006, 59:1073-1082.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 58
    • 80054726392 scopus 로고    scopus 로고
    • ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase
    • Mui T.P., Fuss J.O., Ishida J.P., Tainer J.A., Barton J.K. ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase. J. Am. Chem. Soc. 2011, 133:16378-16381.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16378-16381
    • Mui, T.P.1    Fuss, J.O.2    Ishida, J.P.3    Tainer, J.A.4    Barton, J.K.5
  • 59
    • 84857029886 scopus 로고    scopus 로고
    • Iron-sulphur clusters in nucleic acid processing enzymes
    • White M.F., Dillingham M.S. Iron-sulphur clusters in nucleic acid processing enzymes. Curr. Opin. Struct. Biol. 2012, 22:94-100.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 94-100
    • White, M.F.1    Dillingham, M.S.2
  • 61
    • 84871563271 scopus 로고    scopus 로고
    • The mammalian proteins MMS19, MIP18, and ANT2 are involved in cytoplasmic iron-sulfur cluster protein assembly
    • van Wietmarschen N., Moradian A., Morin G.B., Lansdorp P.M., Uringa E.J. The mammalian proteins MMS19, MIP18, and ANT2 are involved in cytoplasmic iron-sulfur cluster protein assembly. J. Biol. Chem. 2012, 287:43351-43358.
    • (2012) J. Biol. Chem. , vol.287 , pp. 43351-43358
    • van Wietmarschen, N.1    Moradian, A.2    Morin, G.B.3    Lansdorp, P.M.4    Uringa, E.J.5
  • 62
    • 77953965074 scopus 로고    scopus 로고
    • Ensemble and single-molecule fluorescence-based assays to monitor DNA binding, translocation, and unwinding by iron-sulfur cluster containing helicases
    • Pugh R.A., Honda M., Spies M. Ensemble and single-molecule fluorescence-based assays to monitor DNA binding, translocation, and unwinding by iron-sulfur cluster containing helicases. Methods 2010, 51(3):313-321.
    • (2010) Methods , vol.51 , Issue.3 , pp. 313-321
    • Pugh, R.A.1    Honda, M.2    Spies, M.3
  • 63
    • 0036176741 scopus 로고    scopus 로고
    • FRET tells us about proximities, distances, orientations and dynamic properties
    • Clegg R.M. FRET tells us about proximities, distances, orientations and dynamic properties. J. Biotechnol. 2002, 82:177-179.
    • (2002) J. Biotechnol. , vol.82 , pp. 177-179
    • Clegg, R.M.1
  • 64
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy R., Hohng S., Ha T. A practical guide to single-molecule FRET. Nat. Methods 2008, 5:507-516.
    • (2008) Nat. Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 65
    • 84876021636 scopus 로고    scopus 로고
    • Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase
    • Masuda-Ozawa T., Hoang T., Seo Y.-S., Chen L.-F., Spies M. Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase. Nucleic Acids Res. 2013, 41:3576-3587.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3576-3587
    • Masuda-Ozawa, T.1    Hoang, T.2    Seo, Y.-S.3    Chen, L.-F.4    Spies, M.5
  • 66
    • 27644514163 scopus 로고    scopus 로고
    • Repetitive shuttling of a motor protein on DNA
    • Myong S., Rasnik I., Joo C., Lohman T.M., Ha T. Repetitive shuttling of a motor protein on DNA. Nature 2005, 437:1321-1325.
    • (2005) Nature , vol.437 , pp. 1321-1325
    • Myong, S.1    Rasnik, I.2    Joo, C.3    Lohman, T.M.4    Ha, T.5
  • 67
    • 33749146108 scopus 로고    scopus 로고
    • DNA unwinding and protein displacement by superfamily 1 and superfamily 2 helicases
    • Mackintosh S.G., Raney K.D. DNA unwinding and protein displacement by superfamily 1 and superfamily 2 helicases. Nucleic Acids Res. 2006, 34:4154-4159.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4154-4159
    • Mackintosh, S.G.1    Raney, K.D.2
  • 69
    • 44449103347 scopus 로고    scopus 로고
    • High-resolution dual-trap optical tweezers with differential detection, a laboratory manual
    • Bustamante C., Chemla Y.R., Moffitt J.R. High-resolution dual-trap optical tweezers with differential detection, a laboratory manual. Single-Mol. Techn. 2008, 297-324.
    • (2008) Single-Mol. Techn. , pp. 297-324
    • Bustamante, C.1    Chemla, Y.R.2    Moffitt, J.R.3
  • 70
    • 84879040933 scopus 로고    scopus 로고
    • Sequence-dependent base pair stepping dynamics in XPD helicase unwinding
    • Qi Z., Pugh R.A., Spies M., Chemla Y.R. Sequence-dependent base pair stepping dynamics in XPD helicase unwinding. eLife 2013, 2:e00334.
    • (2013) eLife , vol.2
    • Qi, Z.1    Pugh, R.A.2    Spies, M.3    Chemla, Y.R.4
  • 71
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali J.A., Lohman T.M. Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 1997, 275:377-380.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 72
    • 33644793170 scopus 로고    scopus 로고
    • Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase
    • Eoff R.L., Raney K.D. Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase. Nat. Struct. Mol. Biol. 2006, 13:242-249.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 242-249
    • Eoff, R.L.1    Raney, K.D.2
  • 74
    • 33744951869 scopus 로고    scopus 로고
    • Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    • Zhang X.-D., Dou S.-X., Xie P., Hu J.-S., Wang P.-Y., Xi X.G. Escherichia coli RecQ is a rapid, efficient, and monomeric helicase. J. Biol. Chem. 2006, 281:12655-12663.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12655-12663
    • Zhang, X.-D.1    Dou, S.-X.2    Xie, P.3    Hu, J.-S.4    Wang, P.-Y.5    Xi, X.G.6
  • 75
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: "measurement of step size and translocation speed"
    • Dillingham M.S., Wigley D.B., Webb M.R. Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: "measurement of step size and translocation speed". Biochemistry 1999, 39:205-212.
    • (1999) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 76
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee J.Y., Yang W. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell 2006, 127:1349-1360.
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 77
    • 34247602963 scopus 로고    scopus 로고
    • A Nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko E.J., Fischer C.J., Niedziela-Majka A., Lohman T.M. A Nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol. Cell 2007, 26:335-347.
    • (2007) Mol. Cell , vol.26 , pp. 335-347
    • Tomko, E.J.1    Fischer, C.J.2    Niedziela-Majka, A.3    Lohman, T.M.4
  • 78
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
    • Dumont S., Cheng W., Serebrov V., Beran R.K., Tinoco I., Pyle A.M., Bustamante C. RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP. Nature 2006, 439:105-108.
    • (2006) Nature , vol.439 , pp. 105-108
    • Dumont, S.1    Cheng, W.2    Serebrov, V.3    Beran, R.K.4    Tinoco, I.5    Pyle, A.M.6    Bustamante, C.7
  • 79
    • 80053144268 scopus 로고    scopus 로고
    • Single-base pair unwinding and asynchronous RNA release by the hepatitis C virus NS3 helicase
    • Cheng W., Arunajadai S.G., Moffitt J.R., Tinoco I., Bustamante C. Single-base pair unwinding and asynchronous RNA release by the hepatitis C virus NS3 helicase. Science 2011, 333:1746-1749.
    • (2011) Science , vol.333 , pp. 1746-1749
    • Cheng, W.1    Arunajadai, S.G.2    Moffitt, J.R.3    Tinoco, I.4    Bustamante, C.5
  • 80
    • 34547595373 scopus 로고    scopus 로고
    • Spring-loaded mechanism of DNA unwinding by hepatitis C virus NS3 helicase
    • Myong S., Bruno M.M., Pyle A.M., Ha T. Spring-loaded mechanism of DNA unwinding by hepatitis C virus NS3 helicase. Science 2007, 317:513-516.
    • (2007) Science , vol.317 , pp. 513-516
    • Myong, S.1    Bruno, M.M.2    Pyle, A.M.3    Ha, T.4
  • 82
    • 41349092240 scopus 로고    scopus 로고
    • Opening of nucleic-acid double strands by helicases: active versus passive opening
    • Betterton M.D., Jülicher F. Opening of nucleic-acid double strands by helicases: active versus passive opening. Phys. Rev. E 2005, 71:011904.
    • (2005) Phys. Rev. E , vol.71 , pp. 011904
    • Betterton, M.D.1    Jülicher, F.2
  • 83
    • 27744507840 scopus 로고    scopus 로고
    • Velocity and processivity of helicase unwinding of double-stranded nucleic acids
    • Betterton M.D., Julicher F. Velocity and processivity of helicase unwinding of double-stranded nucleic acids. J. Phys.: Condens. Matter 2005, 17:S3851-S3869.
    • (2005) J. Phys.: Condens. Matter , vol.17
    • Betterton, M.D.1    Julicher, F.2
  • 84
    • 0036880196 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines Part I: structures and properties of isolated helicases
    • Delagoutte E., von Hippel P.H. Helicase mechanisms and the coupling of helicases within macromolecular machines Part I: structures and properties of isolated helicases. Q. Rev. Biophys. 2002, 35:431-478.
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 431-478
    • Delagoutte, E.1    von Hippel, P.H.2
  • 85
    • 77957785417 scopus 로고    scopus 로고
    • Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor
    • Wu C.G., Bradford C., Lohman T.M. Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor. Nat. Struct. Mol. Biol. 2010, 17:1210-1217.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1210-1217
    • Wu, C.G.1    Bradford, C.2    Lohman, T.M.3
  • 88
    • 33747881750 scopus 로고    scopus 로고
    • The general transcription machinery and general cofactors
    • Thomas M.C., Chiang C.M. The general transcription machinery and general cofactors. Crit. Rev. Biochem. Mol. Biol. 2006, 41:105-178.
    • (2006) Crit. Rev. Biochem. Mol. Biol. , vol.41 , pp. 105-178
    • Thomas, M.C.1    Chiang, C.M.2
  • 89
    • 84875613843 scopus 로고    scopus 로고
    • Structural visualization of key steps in human transcription initiation
    • He Y., Fang J., Taatjes D.J., Nogales E. Structural visualization of key steps in human transcription initiation. Nature 2013, 495:481-486.
    • (2013) Nature , vol.495 , pp. 481-486
    • He, Y.1    Fang, J.2    Taatjes, D.J.3    Nogales, E.4
  • 90
    • 78149399844 scopus 로고    scopus 로고
    • The XPD subunit of TFIIH is required for transcription-associated but not DNA double-strand break-induced recombination in mammalian cells
    • Savolainen L., Cassel T., Helleday T. The XPD subunit of TFIIH is required for transcription-associated but not DNA double-strand break-induced recombination in mammalian cells. Mutagenesis 2010, 25:623-629.
    • (2010) Mutagenesis , vol.25 , pp. 623-629
    • Savolainen, L.1    Cassel, T.2    Helleday, T.3
  • 93
    • 0038157142 scopus 로고    scopus 로고
    • Xpd/Ercc2 regulates CAK activity and mitotic progression
    • Chen J., Larochelle S., Li X., Suter B. Xpd/Ercc2 regulates CAK activity and mitotic progression. Nature 2003, 424:228-232.
    • (2003) Nature , vol.424 , pp. 228-232
    • Chen, J.1    Larochelle, S.2    Li, X.3    Suter, B.4
  • 94
    • 38049029649 scopus 로고    scopus 로고
    • Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase
    • Rajagopal V., Patel S.S. Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase. J. Mol. Biol. 2008, 376:69-79.
    • (2008) J. Mol. Biol. , vol.376 , pp. 69-79
    • Rajagopal, V.1    Patel, S.S.2
  • 95
    • 77953570622 scopus 로고    scopus 로고
    • Inching over hurdles: how DNA helicases move on crowded lattices
    • Spies M., Ha T. Inching over hurdles: how DNA helicases move on crowded lattices. Cell Cycle 2010, 9:1742-1749.
    • (2010) Cell Cycle , vol.9 , pp. 1742-1749
    • Spies, M.1    Ha, T.2
  • 96
    • 0037526104 scopus 로고    scopus 로고
    • Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein
    • Kerr I.D., Wadsworth R.I., Cubeddu L., Blankenfeldt W., Naismith J.H., White M.F. Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein. EMBO J. 2003, 22:2561-2570.
    • (2003) EMBO J. , vol.22 , pp. 2561-2570
    • Kerr, I.D.1    Wadsworth, R.I.2    Cubeddu, L.3    Blankenfeldt, W.4    Naismith, J.H.5    White, M.F.6
  • 97
    • 0033575671 scopus 로고    scopus 로고
    • The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding
    • Bochkarev A., Bochkareva E., Frappier L., Edwards A.M. The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. EMBO J. 1999, 18:4498-4504.
    • (1999) EMBO J. , vol.18 , pp. 4498-4504
    • Bochkarev, A.1    Bochkareva, E.2    Frappier, L.3    Edwards, A.M.4
  • 98
    • 77950366206 scopus 로고    scopus 로고
    • The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway
    • Rudolf J., Rouillon C., Schwarz-Linek U., White M.F. The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway. Nucleic Acids Res. 2010, 38(3):931-941.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.3 , pp. 931-941
    • Rudolf, J.1    Rouillon, C.2    Schwarz-Linek, U.3    White, M.F.4
  • 99
    • 0029899062 scopus 로고    scopus 로고
    • Xeroderma pigmentosum and molecular cloning of DNA repair genes
    • Boulikas T. Xeroderma pigmentosum and molecular cloning of DNA repair genes. Anticancer Res. 1996, 16:693-708.
    • (1996) Anticancer Res. , vol.16 , pp. 693-708
    • Boulikas, T.1
  • 100
    • 70350491426 scopus 로고    scopus 로고
    • Multiple human single-stranded DNA binding proteins function in genome maintenance: structural, biochemical and functional analysis
    • Richard D.J., Bolderson E., Khanna K.K. Multiple human single-stranded DNA binding proteins function in genome maintenance: structural, biochemical and functional analysis. Crit. Rev. Biochem. Mol. Biol. 2009, 44:98-116.
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 98-116
    • Richard, D.J.1    Bolderson, E.2    Khanna, K.K.3
  • 101
    • 77954588476 scopus 로고    scopus 로고
    • The XPD helicase: XPanDing archaeal XPD structures to get a grip on human DNA repair
    • Wolski S.C., Kuper J., Kisker C. The XPD helicase: XPanDing archaeal XPD structures to get a grip on human DNA repair. Biol. Chem. 2010, 391:761-765.
    • (2010) Biol. Chem. , vol.391 , pp. 761-765
    • Wolski, S.C.1    Kuper, J.2    Kisker, C.3
  • 102
    • 79953292607 scopus 로고    scopus 로고
    • Ultrahigh-resolution optical trap with single-fluorophore sensitivity
    • Comstock M.J., Ha T., Chemla Y.R. Ultrahigh-resolution optical trap with single-fluorophore sensitivity. Nat. Meth. 2011, 8:335-340.
    • (2011) Nat. Meth. , vol.8 , pp. 335-340
    • Comstock, M.J.1    Ha, T.2    Chemla, Y.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.