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Volumn 101, Issue 4, 2011, Pages 976-984

Single-molecule nanopositioning: Structural transitions of a helicase-DNA complex during ATP hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CARBOCYANINE; CYANINE DYE 3; DNA; DRUG DERIVATIVE; ESCHERICHIA COLI PROTEIN; HELICASE; NANOPARTICLE; REP PROTEIN, E COLI; UVRD PROTEIN, E COLI;

EID: 80052449840     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.07.010     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicasecatalyzed DNA unwinding
    • Lohman, T. M., and K. P. Bjornson. 1996. Mechanisms of helicasecatalyzed DNA unwinding. Annu. Rev. Biochem. 65:169214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 2
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel, S. S., and K. M. Picha. 2000. Structure and function of hexameric helicases. Annu. Rev. Biochem. 69:651697
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651697
    • Patel, S.S.1    Picha, K.M.2
  • 3
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M. R., M. S. Dillingham, and D. B. Wigley. 2007. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76:2350.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 2350
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 4
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • Lohman, T. M., E. J. Tomko, and C. G. Wu. 2008. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat. Rev. Mol. Cell Biol. 9:391401.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 391401
    • Lohman, T.M.1    Tomko, E.J.2    Wu., C.G.3
  • 5
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin, O., J. Banroques, ., P. Linder. 2006. The DEAD-box protein family of RNA helicases. Gene. 367:1737.
    • (2006) Gene , vol.367 , pp. 1737
    • Cordin, O.1    Banroques, J.2    Linder, P.3
  • 6
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: Integration of helicases into cellular processes
    • Delagoutte, E., and P. H. von Hippel. 2003. Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: Integration of helicases into cellular processes. Q. Rev. Biophys. 36: 169.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 169
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 7
    • 0027950513 scopus 로고
    • DNA helicases: Enzymes with essential roles in all aspects of DNA metabolism
    • Korolev, S., J. Hsieh, ., G. Waksman. 1997. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 90:635647.
    • (1994) Bioessays , vol.16 , pp. 1322
    • Matson, S.W.1    Bean, D.W.2    George, J.W.3
  • 8
    • 33745790132 scopus 로고    scopus 로고
    • Chromatin remodelling: The industrial revolution of DNA around histones
    • Saha, A., J. Wittmeyer, and B. R. Cairns. 2006. Chromatin remodelling: the industrial revolution of DNA around histones. Nat. Rev. Mol. Cell Biol. 7:437447.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 437447
    • Saha, A.1    Wittmeyer, J.2    Cairns, B.R.3
  • 9
    • 13244252309 scopus 로고    scopus 로고
    • UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli
    • Veaute, X., S. Delmas,., M. A. Petit. 2005. UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli. EMBO J. 24:180189.
    • (2005) EMBO J. , vol.24 , pp. 180189
    • Veaute, X.1    Delmas, S.2    Petit, M.A.3
  • 10
    • 0030861685 scopus 로고    scopus 로고
    • DNA helicases in inherited human disorders
    • Ellis, N. A. 1997. DNA helicases in inherited human disorders. Curr. Opin. Genet. Dev. 7:354363.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 354363
    • Ellis, N.A.1
  • 11
    • 85101729276 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., J. Hsieh, ., G. Waksman. 1997. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 90:635647.
    • (1997) Cell , vol.90 , pp. 635647
    • Korolev, S.1    Hsieh, J.2    Waksman, G.3
  • 12
    • 0029856618 scopus 로고    scopus 로고
    • Crystal structure of a DExx box DNA helicase
    • Subramanya, H. S., L. E. Bird,., D. B.Wigley. 1996. Crystal structure of a DExx box DNA helicase. Nature. 384:379383.
    • (1996) Nature , vol.384 , pp. 379383
    • Subramanya, H.S.1    Bird, L.E.2    Wigley, D.B.3
  • 13
    • 85101730280 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S. S., P. Soultanas,., D. B.Wigley. 1999. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell. 97:7584.
    • (1999) Cell , vol.97 , pp. 7584
    • Velankar, S.S.1    Soultanas, P.2    Wigley, D.B.3
  • 14
    • 22544482026 scopus 로고    scopus 로고
    • Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain
    • Brendza, K. M., W. Cheng,., T. M. Lohman. 2005. Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain. Proc. Natl. Acad. Sci. USA. 102:1007610081.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1007610081
    • Brendza, K.M.1    Cheng, W.2    Lohman, T.M.3
  • 15
    • 0037080166 scopus 로고    scopus 로고
    • Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine
    • Dillingham, M. S., D. B. Wigley, and M. R. Webb. 2002. Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine. Biochemistry. 41:643651.
    • (2002) Biochemistry , vol.41 , pp. 643651
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 16
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA
    • Fischer, C. J., N. K. Maluf, and T. M. Lohman. 2004. Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA. J. Mol. Biol. 344:12871309.
    • (2004) J. Mol. Biol. , vol.344 , pp. 12871309
    • Fischer, C.J.1    Maluf, N.K.2    Lohman, T.M.3
  • 17
    • 27644514163 scopus 로고    scopus 로고
    • Repetitive shuttling of a motor protein on DNA
    • Myong, S., I. Rasnik, ., T. Ha. 2005. Repetitive shuttling of a motor protein on DNA. Nature. 437:13211325.
    • (2005) Nature , vol.437 , pp. 13211325
    • Myong, S.1    Rasnik, I.2    Ha, T.3
  • 18
    • 34848840105 scopus 로고    scopus 로고
    • Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro
    • Niedziela-Majka, A., M. A. Chesnik,., T. M. Lohman. 2007. Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. J. Biol. Chem. 282: 2707627085.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2707627085
    • Niedziela-Majka, A.1    Chesnik, M.A.2    Lohman, T.M.3
  • 19
    • 34247602963 scopus 로고    scopus 로고
    • A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko, E. J., C. J. Fischer, ., T. M. Lohman. 2007. A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol. Cell. 26:335347.
    • (2007) Mol. Cell , vol.26 , pp. 335347
    • Tomko, E.J.1    Fischer, C.J.2    Lohman, T.M.3
  • 20
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • Cheng,W., J. Hsieh,., T. M. Lohman. 2001. E. coli Rep oligomers are required to initiate DNA unwinding in vitro. J. Mol. Biol. 310:327350.
    • (2001) J. Mol. Biol. , vol.310 , pp. 327350
    • Cheng, W.1    Hsieh, J.2    Lohman, T.M.3
  • 21
    • 0037474547 scopus 로고    scopus 로고
    • A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro
    • Maluf, N. K., C. J. Fischer, and T. M. Lohman. 2003. A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J. Mol. Biol. 325:913935.
    • (2003) J. Mol. Biol. , vol.325 , pp. 913935
    • Maluf, N.K.1    Fischer, C.J.2    Lohman, T.M.3
  • 22
    • 79960907291 scopus 로고    scopus 로고
    • Rotations of the 2B Subdomain of E. coli UvrD Helicase/Translocase Coupled to Nucleotide and DNA Binding
    • 10.1016/j.jmb.2011.06.019.
    • Jia, H., S. Korolev, ., T. M. Lohman. 2011. Rotations of the 2B Subdomain of E. coli UvrD Helicase/Translocase Coupled to Nucleotide and DNA Binding. J. Mol. Biol. 10.1016/j.jmb.2011.06.019.
    • (2011) J. Mol. Biol.
    • Jia, H.1    Korolev, S.2    Lohman, T.M.3
  • 23
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee, J. Y., and W. Yang. 2006. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell. 127:13491360.
    • (2006) Cell , vol.127 , pp. 13491360
    • Lee, J.Y.1    Yang, W.2
  • 24
    • 0037058917 scopus 로고    scopus 로고
    • The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity
    • Cheng,W., K. M. Brendza,., T. M. Lohman. 2002. The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity. Proc. Natl. Acad. Sci. USA. 99:1600616011.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1600616011
    • Cheng, W.1    Brendza, K.M.2    Lohman, T.M.3
  • 25
    • 85080841934 scopus 로고    scopus 로고
    • DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: Single-molecule studies of fluorescently labeled enzymes
    • Rasnik, I., S. Myong, ., T. Ha. 2004. DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: single-molecule studies of fluorescently labeled enzymes. J. Mol. Biol. 336:395408.
    • (2004) J. Mol. Biol. , vol.336 , pp. 395408
    • Rasnik, I.1    Myong, S.2    Ha, T.3
  • 26
    • 85101896417 scopus 로고    scopus 로고
    • PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps
    • Park, J., S. Myong, ., T. Ha. 2010. PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps. Cell. 142:544555.
    • (2010) Cell , vol.142 , pp. 544555
    • Park, J.1    Myong, S.2    Ha, T.3
  • 27
    • 78449275796 scopus 로고    scopus 로고
    • 50-Single-stranded/ duplex DNA junctions are loading sites for E. coli UvrD translocase
    • Tomko, E. J., H. Jia, ., T. M. Lohman. 2010. 50-Single-stranded/ duplex DNA junctions are loading sites for E. coli UvrD translocase. EMBO J. 29:38263839.
    • (2010) EMBO J. , vol.29 , pp. 38263839
    • Tomko, E.J.1    Jia, H.2    Lohman, T.M.3
  • 28
    • 38349173560 scopus 로고    scopus 로고
    • Single-molecule tracking of mRNA exiting from RNA polymerase II
    • Andrecka, J., R. Lewis, ., J. Michaelis. 2008. Single-molecule tracking of mRNA exiting from RNA polymerase II. Proc. Natl. Acad. Sci. USA. 105:135140.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 135140
    • Andrecka, J.1    Lewis, R.2    Michaelis, J.3
  • 29
    • 56149121056 scopus 로고    scopus 로고
    • A nano-positioning system for macromolecular structural analysis
    • Muschielok, A., J. Andrecka, ., J. Michaelis. 2008. A nano-positioning system for macromolecular structural analysis. Nat. Methods. 5:965971.
    • (2008) Nat. Methods , vol.5 , pp. 965971
    • Muschielok, A.1    Andrecka, J.2    Michaelis, J.3
  • 30
    • 33751010184 scopus 로고    scopus 로고
    • Architecture of the 99 bp DNA-six-protein regulatory complex of the lambda att site
    • Sun, X., D. F. Mierke,., M. Radman-Livaja. 2006. Architecture of the 99 bp DNA-six-protein regulatory complex of the lambda att site. Mol. Cell. 24:569580.
    • (2006) Mol. Cell , vol.24 , pp. 569580
    • Sun, X.1    Mierke, D.F.2    Radman-Livaja, M.3
  • 31
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha, T., T. Enderle,., S. Weiss. 1996. Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl. Acad. Sci. USA. 93:62646268.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 62646268
    • Ha, T.1    Enderle, T.2    Weiss, S.3
  • 32
    • 0015936920 scopus 로고
    • Possible transition-state analogs for ribonuclease. The complexes of uridine with oxovanadium(IV) ion and vanadium(V) ion
    • Lindquist, R. N., J. L. Lynn, Jr. , and G. E. Lienhard. 1973. Possible transition-state analogs for ribonuclease. The complexes of uridine with oxovanadium(IV) ion and vanadium(V) ion. J. Am. Chem. Soc. 95:87628768.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 87628768
    • Lindquist, R.N.1    Lynn Jr., J.L.2    Lienhard, G.E.3
  • 33
    • 0023099216 scopus 로고
    • Why nature chose phosphates
    • Westheimer, F. H. 1987. Why nature chose phosphates. Science. 235: 11731178.
    • (1987) Science , vol.235 , pp. 11731178
    • Westheimer, F.H.1
  • 34
    • 77949264921 scopus 로고    scopus 로고
    • Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex
    • Choi, U. B., P. Strop, ., K. R. Weninger. 2010. Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex. Nat. Struct. Mol. Biol. 17:318324.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 318324
    • Choi, U.B.1    Strop, P.2    Weninger, K.R.3
  • 35
    • 0028598302 scopus 로고
    • Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 2. Application of a kinetic competition approach
    • Moore, K. J., and T. M. Lohman. 1994. Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 2. Application of a kinetic competition approach. Biochemistry. 33:1456514578.
    • (1994) Biochemistry , vol.33 , pp. 1456514578
    • Moore, K.J.1    Lohman, T.M.2
  • 36
    • 0028566711 scopus 로고
    • Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogues
    • Moore, K. J., and T. M. Lohman. 1994. Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogues. Biochemistry. 33:1455014564.
    • (1994) Biochemistry , vol.33 , pp. 1455014564
    • Moore, K.J.1    Lohman, T.M.2


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