메뉴 건너뛰기




Volumn 109, Issue 25, 2012, Pages 9804-9809

RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; NUCLEOPROTEIN; NUCLEOTIDE; RECQ HELICASE; SINGLE STRANDED DNA;

EID: 84862544678     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1114468109     Document Type: Article
Times cited : (24)

References (51)
  • 2
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • Harmon FG, Kowalczykowski SC (1998) RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination. Genes Dev 12:1134-1144.
    • (1998) Genes Dev , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 3
    • 43049162175 scopus 로고    scopus 로고
    • RecQ helicases: Guardian angels of the DNA replication fork
    • Bachrati CZ, Hickson ID (2008) RecQ helicases: Guardian angels of the DNA replication fork. Chromosoma 117:219-233.
    • (2008) Chromosoma , vol.117 , pp. 219-233
    • Bachrati, C.Z.1    Hickson, I.D.2
  • 4
    • 33751426143 scopus 로고    scopus 로고
    • DNA helicases required for homologous recombination and repair of damaged replication forks
    • Wu L, Hickson ID (2006) DNA helicases required for homologous recombination and repair of damaged replication forks. Annu Rev Genet 40:279-306.
    • (2006) Annu Rev Genet , vol.40 , pp. 279-306
    • Wu, L.1    Hickson, I.D.2
  • 5
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 76:23-50.
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 6
    • 34447536139 scopus 로고    scopus 로고
    • BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules
    • Oh SD, et al. (2007) BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules. Cell 130:259-272.
    • (2007) Cell , vol.130 , pp. 259-272
    • Oh, S.D.1
  • 7
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: The role of human RecQ helicases in genome maintenance
    • Bohr VA (2008) Rising from the RecQ-age: The role of human RecQ helicases in genome maintenance. Trends Biochem Sci 33:609-620.
    • (2008) Trends Biochem Sci , vol.33 , pp. 609-620
    • Bohr, V.A.1
  • 8
    • 0942289875 scopus 로고    scopus 로고
    • Human diseases deficient in RecQ helicases
    • Harrigan JA, Bohr VA (2003) Human diseases deficient in RecQ helicases. Biochimie 85: 1185-1193.
    • (2003) Biochimie , vol.85 , pp. 1185-1193
    • Harrigan, J.A.1    Bohr, V.A.2
  • 9
    • 0030888233 scopus 로고    scopus 로고
    • RecQ DNA helicase is a suppressor of illegitimate recombination in Escherichia coli
    • Hanada K, et al. (1997) RecQ DNA helicase is a suppressor of illegitimate recombination in Escherichia coli. Proc Natl Acad Sci USA 94:3860-3865.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3860-3865
    • Hanada, K.1
  • 10
    • 66149130735 scopus 로고    scopus 로고
    • Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli
    • Handa N, Morimatsu K, Lovett ST, Kowalczykowski SC (2009) Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli. Genes Dev 23:1234-1245.
    • (2009) Genes Dev , vol.23 , pp. 1234-1245
    • Handa, N.1    Morimatsu, K.2    Lovett, S.T.3    Kowalczykowski, S.C.4
  • 11
    • 0032740855 scopus 로고    scopus 로고
    • RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli
    • Courcelle J, Hanawalt PC (1999) RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli. Mol Gen Genet 262: 543-551.
    • (1999) Mol Gen Genet , vol.262 , pp. 543-551
    • Courcelle, J.1    Hanawalt, P.C.2
  • 12
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97:75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 13
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • Dillingham MS, Wigley DB, Webb MR (2000) Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed. Biochemistry 39:205-212.
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 14
    • 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. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 15
    • 77955247067 scopus 로고    scopus 로고
    • Processive translocation mechanism of the human Bloom's syndrome helicase along single-stranded DNA
    • Gyimesi M, Sarlós K, Kovács M (2010) Processive translocation mechanism of the human Bloom's syndrome helicase along single-stranded DNA. Nucleic Acids Res 38: 4404-4414.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4404-4414
    • Gyimesi, M.1    Sarlós, K.2    Kovács, M.3
  • 16
    • 34247602963 scopus 로고    scopus 로고
    • A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko EJ, Fischer CJ, Niedziela-Majka A, Lohman TM (2007) A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol Cell 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
  • 17
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
    • Dumont S, et al. (2006) RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP. Nature 439:105-108.
    • (2006) Nature , vol.439 , pp. 105-108
    • Dumont, S.1
  • 18
    • 2542475076 scopus 로고    scopus 로고
    • Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius AL, Lohman TM (2004) Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding. J Mol Biol 339:751-771.
    • (2004) J Mol Biol , vol.339 , pp. 751-771
    • Lucius, A.L.1    Lohman, T.M.2
  • 19
    • 20444440763 scopus 로고    scopus 로고
    • A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase
    • Levin MK, Gurjar M, Patel SS (2005) A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase. Nat Struct Mol Biol 12:429-435.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 429-435
    • Levin, M.K.1    Gurjar, M.2    Patel, S.S.3
  • 20
    • 0027158626 scopus 로고
    • RecQ DNA helicase of Escherichia coli. Characterization of the helix-unwinding activity with emphasis on the effect of single-stranded DNA-binding protein
    • Umezu K, Nakayama H (1993) RecQ DNA helicase of Escherichia coli. Characterization of the helix-unwinding activity with emphasis on the effect of single-stranded DNA-binding protein. J Mol Biol 230:1145-1150.
    • (1993) J Mol Biol , vol.230 , pp. 1145-1150
    • Umezu, K.1    Nakayama, H.2
  • 21
    • 1342346600 scopus 로고    scopus 로고
    • The DNA binding properties of the Escherichia coli RecQ helicase
    • Dou SX, Wang PY, Xu HQ, Xi XG (2004) The DNA binding properties of the Escherichia coli RecQ helicase. J Biol Chem 279:6354-6363.
    • (2004) J Biol Chem , vol.279 , pp. 6354-6363
    • Dou, S.X.1    Wang, P.Y.2    Xu, H.Q.3    Xi, X.G.4
  • 23
    • 0035808456 scopus 로고    scopus 로고
    • Biochemical characterization of the DNA helicase activity of the escherichia coli RecQ helicase
    • Harmon FG, Kowalczykowski SC (2001) Biochemical characterization of the DNA helicase activity of the escherichia coli RecQ helicase. J Biol Chem 276:232-243.
    • (2001) J Biol Chem , vol.276 , pp. 232-243
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 24
    • 0042818314 scopus 로고    scopus 로고
    • The Escherichia coli RecQ helicase functions as a monomer
    • Xu HQ, et al. (2003) The Escherichia coli RecQ helicase functions as a monomer. J Biol Chem 278:34925-34933.
    • (2003) J Biol Chem , vol.278 , pp. 34925-34933
    • Xu, H.Q.1
  • 25
    • 33744951869 scopus 로고    scopus 로고
    • Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    • Zhang XD, et al. (2006) Escherichia coli RecQ is a rapid, efficient, and monomeric helicase. J Biol Chem 281:12655-12663.
    • (2006) J Biol Chem , vol.281 , pp. 12655-12663
    • Zhang, X.D.1
  • 26
    • 77951247935 scopus 로고    scopus 로고
    • Multiple Escherichia coli RecQ helicase monomers cooperate to unwind long DNA substrates: A fluorescence cross-correlation spectroscopy study
    • Li N, et al. (2010) Multiple Escherichia coli RecQ helicase monomers cooperate to unwind long DNA substrates: A fluorescence cross-correlation spectroscopy study. J Biol Chem 285:6922-6936.
    • (2010) J Biol Chem , vol.285 , pp. 6922-6936
    • Li, N.1
  • 27
    • 77952392122 scopus 로고    scopus 로고
    • Mutual inhibition of RecQ molecules in DNA unwinding
    • Pan BY, et al. (2010) Mutual inhibition of RecQ molecules in DNA unwinding. J Biol Chem 285:15884-15893.
    • (2010) J Biol Chem , vol.285 , pp. 15884-15893
    • Pan, B.Y.1
  • 28
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E. coli RecQ helicase catalytic core
    • Bernstein DA, Zittel MC, Keck JL (2003) High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J 22:4910-4921.
    • (2003) EMBO J , vol.22 , pp. 4910-4921
    • Bernstein, D.A.1    Zittel, M.C.2    Keck, J.L.3
  • 29
    • 31144475762 scopus 로고    scopus 로고
    • Coupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: Role of a highly conserved aromatic-rich sequence
    • Zittel MC, Keck JL (2005) Coupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: Role of a highly conserved aromatic-rich sequence. Nucleic Acids Res 33: 6982-6991.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6982-6991
    • Zittel, M.C.1    Keck, J.L.2
  • 30
    • 77954133346 scopus 로고    scopus 로고
    • Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities
    • Gyimesi M, Sarlós K, Derényi I, Kovács M (2010) Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities. Nucleic Acids Res 38:e102.
    • (2010) Nucleic Acids Res , vol.38
    • Gyimesi, M.1    Sarlós, K.2    Derényi, I.3    Kovács, M.4
  • 31
    • 9244237061 scopus 로고    scopus 로고
    • ATP-dependent translocation of proteins along single-stranded DNA: Models and methods of analysis of pre-steady state kinetics
    • Fischer CJ, Lohman TM (2004) ATP-dependent translocation of proteins along single-stranded DNA: Models and methods of analysis of pre-steady state kinetics. J Mol Biol 344:1265-1286.
    • (2004) J Mol Biol , vol.344 , pp. 1265-1286
    • Fischer, C.J.1    Lohman, T.M.2
  • 32
    • 0028275036 scopus 로고
    • Kinetic theory of ATP-driven translocases on one-dimensional polymer lattices
    • Young MC, Kuhl SB, von Hippel PH (1994) Kinetic theory of ATP-driven translocases on one-dimensional polymer lattices. J Mol Biol 235:1436-1446.
    • (1994) J Mol Biol , vol.235 , pp. 1436-1446
    • Young, M.C.1    Kuhl, S.B.2    Von Hippel, P.H.3
  • 33
    • 65249083349 scopus 로고    scopus 로고
    • Kinetic mechanism for single-stranded DNA binding and translocation by Saccharomyces cerevisiae Isw2
    • Fischer CJ, Yamada K, Fitzgerald DJ (2009) Kinetic mechanism for single-stranded DNA binding and translocation by Saccharomyces cerevisiae Isw2. Biochemistry 48: 2960-2968.
    • (2009) Biochemistry , vol.48 , pp. 2960-2968
    • Fischer, C.J.1    Yamada, K.2    Fitzgerald, D.J.3
  • 34
    • 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
  • 35
    • 77952909625 scopus 로고    scopus 로고
    • The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase
    • Rajagopal V, Gurjar M, Levin MK, Patel SS (2010) The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase. J Biol Chem 285:17821-17832.
    • (2010) J Biol Chem , vol.285 , pp. 17821-17832
    • Rajagopal, V.1    Gurjar, M.2    Levin, M.K.3    Patel, S.S.4
  • 36
    • 0035905687 scopus 로고    scopus 로고
    • Processive translocation and DNA unwinding by individual RecBCD enzyme molecules
    • Bianco PR, et al. (2001) Processive translocation and DNA unwinding by individual RecBCD enzyme molecules. Nature 409:374-378.
    • (2001) Nature , vol.409 , pp. 374-378
    • Bianco, P.R.1
  • 37
    • 77949447376 scopus 로고    scopus 로고
    • Investigation of translocation, DNA unwinding, and protein displacement by NS3h, the helicase domain from the hepatitis C virus helicase
    • Matlock DL, et al. (2010) Investigation of translocation, DNA unwinding, and protein displacement by NS3h, the helicase domain from the hepatitis C virus helicase. Biochemistry 49:2097-2109.
    • (2010) Biochemistry , vol.49 , pp. 2097-2109
    • Matlock, D.L.1
  • 38
    • 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, Chesnik MA, Tomko EJ, Lohman TM (2007) Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. J Biol Chem 282:27076-27085.
    • (2007) J Biol Chem , vol.282 , pp. 27076-27085
    • Niedziela-Majka, A.1    Chesnik, M.A.2    Tomko, E.J.3    Lohman, T.M.4
  • 40
    • 0033527761 scopus 로고    scopus 로고
    • An oligomeric form of E. coli UvrD is required for optimal helicase activity
    • Ali JA, Maluf NK, Lohman TM (1999) An oligomeric form of E. coli UvrD is required for optimal helicase activity. J Mol Biol 293:815-834.
    • (1999) J Mol Biol , vol.293 , pp. 815-834
    • Ali, J.A.1    Maluf, N.K.2    Lohman, T.M.3
  • 41
    • 0037474547 scopus 로고    scopus 로고
    • A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro
    • Maluf NK, Fischer CJ, Lohman TM (2003) A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J Mol Biol 325:913-935.
    • (2003) J Mol Biol , vol.325 , pp. 913-935
    • Maluf, N.K.1    Fischer, C.J.2    Lohman, T.M.3
  • 42
    • 0041355282 scopus 로고    scopus 로고
    • Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex
    • Maluf NK, Ali JA, Lohman TM (2003) Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex. J Biol Chem 278:31930-31940.
    • (2003) J Biol Chem , vol.278 , pp. 31930-31940
    • Maluf, N.K.1    Ali, J.A.2    Lohman, T.M.3
  • 43
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • Cheng W, Hsieh J, Brendza KM, Lohman TM (2001) E. coli Rep oligomers are required to initiate DNA unwinding in vitro. J Mol Biol 310:327-350.
    • (2001) J Mol Biol , vol.310 , pp. 327-350
    • Cheng, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 44
    • 22544482026 scopus 로고    scopus 로고
    • Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain
    • Brendza KM, et al. (2005) Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain. Proc Natl Acad Sci USA 102:10076-10081.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10076-10081
    • Brendza, K.M.1
  • 45
    • 54049147388 scopus 로고    scopus 로고
    • The Werner syndrome protein binds replication fork and holliday junction DNAs as an oligomer
    • Compton SA, Tolun G, Kamath-Loeb AS, Loeb LA, Griffith JD (2008) The Werner syndrome protein binds replication fork and holliday junction DNAs as an oligomer. J Biol Chem 283:24478-24483.
    • (2008) J Biol Chem , vol.283 , pp. 24478-24483
    • Compton, S.A.1    Tolun, G.2    Kamath-Loeb, A.S.3    Loeb, L.A.4    Griffith, J.D.5
  • 46
    • 33846941210 scopus 로고    scopus 로고
    • Different quaternary structures of human RECQ1 are associated with its dual enzymatic activity
    • Muzzolini L, et al. (2007) Different quaternary structures of human RECQ1 are associated with its dual enzymatic activity. PLoS Biol 5:e20.
    • (2007) PLoS Biol , vol.5
    • Muzzolini, L.1
  • 47
    • 75849155802 scopus 로고    scopus 로고
    • RecQ helicases: Multiple structures for multiple functions?
    • Vindigni A, Hickson ID (2009) RecQ helicases: Multiple structures for multiple functions? HFSP J 3:153-164.
    • (2009) HFSP J , vol.3 , pp. 153-164
    • Vindigni, A.1    Hickson, I.D.2
  • 48
    • 84857137035 scopus 로고    scopus 로고
    • Efficient coupling of ATP hydrolysis to translocation by RecQ helicase
    • Rad B, Kowalczykowski SC (2012) Efficient coupling of ATP hydrolysis to translocation by RecQ helicase. Proc Natl Acad Sci USA 109:1443-1448.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 1443-1448
    • Rad, B.1    Kowalczykowski, S.C.2
  • 49
    • 84859397679 scopus 로고    scopus 로고
    • Translocation of E. coli RecQ helicase on single-stranded DNA
    • Rad B, Kowalczykowski SC (2012) Translocation of E. coli RecQ helicase on single-stranded DNA. Biochemistry 51:2921-2929.
    • (2012) Biochemistry , vol.51 , pp. 2921-2929
    • Rad, B.1    Kowalczykowski, S.C.2
  • 50
    • 80052870830 scopus 로고    scopus 로고
    • Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes
    • Hickson ID, Mankouri HW (2011) Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes. Cell Cycle 10: 3078-3085.
    • (2011) Cell Cycle , vol.10 , pp. 3078-3085
    • Hickson, I.D.1    Mankouri, H.W.2
  • 51
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • Brune M, Hunter JL, Corrie JE, Webb MR (1994) Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry 33:8262-8271.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.