메뉴 건너뛰기




Volumn 767, Issue , 2013, Pages 75-95

Structure and mechanism of hexameric helicases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; HELICASE; HEXAMERIC HELICASE; NUCLEOSIDE TRIPHOSPHATE; RECA PROTEIN; RNA HELICASE; SF1 HELICASE; SF2 HELICASE; SF3 HELICASE; SF4 HELICASE; SF5 HELICASE; SF6 HELICASE; SINGLE STRANDED DNA; T7 HELICASE; UNCLASSIFIED DRUG; ATPASE ASSOCIATED WITH VAROUS CELLULAR ACTIVITY PROTEIN; REGULATOR PROTEIN; DNA; DNA HELICASE; NUCLEOSIDE TRIPHOSPHATASE;

EID: 84873629798     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-5037-5_4     Document Type: Article
Times cited : (17)

References (92)
  • 1
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB. 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
  • 2
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark EJ, Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature. 2006;442:270-5.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 3
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: The structural basis for translocation polarity in hexameric helicases
    • Thomsen ND, Berger JM. Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell. 2009;139:523-34.
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 4
    • 0348133607 scopus 로고    scopus 로고
    • Hexameric ring structure of the full-length archaeal MCM protein complex
    • Pape T, Meka H, Chen S, Vicentini G, van Heel M, Onesti S. Hexameric ring structure of the full-length archaeal MCM protein complex. EMBO Rep. 2003;4:1079-83.
    • (2003) EMBO Rep , vol.4 , pp. 1079-1083
    • Pape, T.1    Meka, H.2    Chen, S.3    Vicentini, G.4    Van Heel, M.5    Onesti, S.6
  • 5
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey S, Eliason WK, Steitz TA. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science. 2007;318:459-63.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 6
    • 63349092249 scopus 로고    scopus 로고
    • The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA
    • Lo YH, Tsai KL, Sun YJ, Chen WT, Huang CY, Hsiao CD. The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA. Nucleic Acids Res. 2009;37:804-14.
    • (2009) Nucleic Acids Res , vol.37 , pp. 804-814
    • Lo, Y.H.1    Tsai, K.L.2    Sun, Y.J.3    Chen, W.T.4    Huang, C.Y.5    Hsiao, C.D.6
  • 7
    • 0038700763 scopus 로고    scopus 로고
    • Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen
    • Li D, Zhao R, Lilyestrom W, Gai D, Zhang R, DeCaprio JA, et al. Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen. Nature. 2003;423:512-8.
    • (2003) Nature , vol.423 , pp. 512-518
    • Li, D.1    Zhao, R.2    Lilyestrom, W.3    Gai, D.4    Zhang, R.5    Decaprio, J.A.6
  • 8
    • 22744445013 scopus 로고    scopus 로고
    • Pumps, paradoxes and ploughshares: Mechanism of the MCM2-7 DNA helicase
    • Takahashi TS, Wigley DB, Walter JC. Pumps, paradoxes and ploughshares: mechanism of the MCM2-7 DNA helicase. Trends Biochem Sci. 2005;30:437-44.
    • (2005) Trends Biochem Sci , vol.30 , pp. 437-444
    • Takahashi, T.S.1    Wigley, D.B.2    Walter, J.C.3
  • 10
    • 80052942659 scopus 로고    scopus 로고
    • Selective bypass of a lagging strand roadblock by the eukaryotic replicative DNA helicase
    • Fu YV, Yardimci H, Long DT, Ho TV, Guainazzi A, Bermudez VP, et al. Selective bypass of a lagging strand roadblock by the eukaryotic replicative DNA helicase. Cell. 2011;146:931-41.
    • (2011) Cell , vol.146 , pp. 931-941
    • Fu, Y.V.1    Yardimci, H.2    Long, D.T.3    Ho, T.V.4    Guainazzi, A.5    Bermudez, V.P.6
  • 11
    • 78751675312 scopus 로고    scopus 로고
    • RNA remodeling by hexameric RNA helicases
    • Rabhi M, Tuma R, Boudvillain M. RNA remodeling by hexameric RNA helicases. RNA Biol. 2010;7:655-66.
    • (2010) RNA Biol , vol.7 , pp. 655-666
    • Rabhi, M.1    Tuma, R.2    Boudvillain, M.3
  • 12
    • 78650854687 scopus 로고    scopus 로고
    • RNA helicases at work: Binding and rearranging
    • Jankowsky E. RNA helicases at work: binding and rearranging. Trends Biochem Sci. 2011;36:19-29.
    • (2011) Trends Biochem Sci , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 13
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe DD, Koonin EV, Aravind L. Evolution and classification of P-loop kinases and related proteins. J Mol Biol. 2003;333:781-815.
    • (2003) J Mol Biol , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 14
    • 5144223072 scopus 로고    scopus 로고
    • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: Implications for the origins of chromosome segregation, cell division and viral capsid packaging
    • Iyer LM, Makarova KS, Koonin EV, Aravind L. Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Res. 2004;32:5260-79.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 15
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger JP, Berger JM. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu Rev Biophys Biomol Struct. 2006;35:93-114.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 16
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AG, Lutter R, Walker JE. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 1994;370:621-8.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 17
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer PD. The ATP synthase-a splendid molecular machine. Annu Rev Biochem. 1997;66:717-49.
    • (1997) Annu Rev Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 19
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T, Wilkinson AJ. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells. 2001;6:575-97.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 20
    • 55549132236 scopus 로고    scopus 로고
    • The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins
    • Zhang X, Wigley DB. The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins. Nat Struct Mol Biol. 2008;15:1223-7.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1223-1227
    • Zhang, X.1    Wigley, D.B.2
  • 21
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol. 2004;146:11-31.
    • (2004) J Struct Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 23
    • 26944435616 scopus 로고    scopus 로고
    • Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism
    • McGeoch AT, Trakselis MA, Laskey RA, Bell SD. Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism. Nat Struct Mol Biol. 2005;12:756-62.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 756-762
    • McGeoch, A.T.1    Trakselis, M.A.2    Laskey, R.A.3    Bell, S.D.4
  • 24
    • 33646754407 scopus 로고    scopus 로고
    • Minichromosome maintenance helicase activity is controlled by Nand C-terminal motifs and requires the ATPase domain helix-2 insert
    • Jenkinson ER, Chong JP. Minichromosome maintenance helicase activity is controlled by Nand C-terminal motifs and requires the ATPase domain helix-2 insert. Proc Natl Acad Sci USA. 2006;103:7613-8.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7613-7618
    • Jenkinson, E.R.1    Chong, J.P.2
  • 25
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationship
    • Gorbalenya AE, Koonin EV. Helicases: amino acid sequence comparisons and structure-function relationship. Curr Opin Struct Biol. 1993;3:419-29.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 26
    • 0027267908 scopus 로고
    • A common set of conserved motifs in a vast variety of putative nucleic aciddependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
    • Koonin EV. A common set of conserved motifs in a vast variety of putative nucleic aciddependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucleic Acids Res. 1993;21:2541-7.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2541-2547
    • Koonin, E.V.1
  • 27
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai D, Zhao R, Li D, Finkielstein CV, Chen XS. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell. 2004;119:47-60.
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 29
    • 0034938363 scopus 로고    scopus 로고
    • A helicase is born
    • Moraes CT. A helicase is born. Nat Genet. 2001;28:200-1.
    • (2001) Nat Genet , vol.28 , pp. 200-201
    • Moraes, C.T.1
  • 30
    • 0345276497 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional primase-helicase of bacteriophage T7
    • Toth EA, Li Y, Sawaya MR, Cheng Y, Ellenberger T. The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Mol Cell. 2003;12:1113-23.
    • (2003) Mol Cell , vol.12 , pp. 1113-1123
    • Toth, E.A.1    Li, Y.2    Sawaya, M.R.3    Cheng, Y.4    Ellenberger, T.5
  • 31
    • 33749119130 scopus 로고    scopus 로고
    • Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions
    • Corn JE, Berger JM. Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions. Nucleic Acids Res. 2006;34:4082-8.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4082-4088
    • Corn, J.E.1    Berger, J.M.2
  • 32
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya MR, Guo S, Tabor S, Richardson CC, Ellenberger T. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell. 1999;99:167-77.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 33
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton MR, Sawaya MR, Ellenberger T, Wigley DB. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell. 2000;101:589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 34
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman EH, Yu X, Wild R, Hingorani MM, Patel SS. Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc Natl Acad Sci USA 1995;92:3869-73.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 35
    • 33749121811 scopus 로고    scopus 로고
    • Mechanisms of a ring shaped helicase
    • Donmez I, Patel SS. Mechanisms of a ring shaped helicase. Nucleic Acids Res. 2006;34:4216-24.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4216-4224
    • Donmez, I.1    Patel, S.S.2
  • 36
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz JH, McMacken R. The Escherichia coli dnaB replication protein is a DNA helicase. J Biol Chem. 1986;261:4738-48.
    • (1986) J Biol Chem , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    McMacken, R.2
  • 37
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • Kaplan DL, O'Donnell M. DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol Cell. 2002;10:647-57.
    • (2002) Mol Cell , vol.10 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 39
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin MC, Stamford NP, Dammerova N, Dixon NE, Carazo JM. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J Struct Biol. 1995;114:167-76.
    • (1995) J Struct Biol , vol.114 , pp. 167-176
    • San Martin, M.C.1    Stamford, N.P.2    Dammerova, N.3    Dixon, N.E.4    Carazo, J.M.5
  • 41
  • 42
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • Leipe DD, Aravind L, Grishin NV, Koonin EV. The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res. 2000;10:5-16.
    • (2000) Genome Res , vol.10 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 43
    • 0034705329 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of transcription termination factor rho: Orientation of the N-terminal domain and visualization of an RNAbinding site
    • Yu X, Horiguchi T, Shigesada K, Egelman EH. Three-dimensional reconstruction of transcription termination factor rho: orientation of the N-terminal domain and visualization of an RNAbinding site. J Mol Biol. 2000;299:1279-87.
    • (2000) J Mol Biol , vol.299 , pp. 1279-1287
    • Yu, X.1    Horiguchi, T.2    Shigesada, K.3    Egelman, E.H.4
  • 44
    • 0041696782 scopus 로고    scopus 로고
    • Loading Rho to terminate transcription
    • Richardson JP. Loading Rho to terminate transcription. Cell. 2003;114:157-9.
    • (2003) Cell , vol.114 , pp. 157-159
    • Richardson, J.P.1
  • 45
    • 0037559627 scopus 로고    scopus 로고
    • Structure of the Rho transcription terminator: Mechanism of mRNA recognition and helicase loading
    • Skordalakes E, Berger JM. Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading. Cell. 2003;114:135-46.
    • (2003) Cell , vol.114 , pp. 135-146
    • Skordalakes, E.1    Berger, J.M.2
  • 46
    • 33750477997 scopus 로고    scopus 로고
    • Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor
    • Skordalakes E, Berger JM. Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell. 2006;127:553-64.
    • (2006) Cell , vol.127 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 47
    • 77953012026 scopus 로고    scopus 로고
    • Simple enzymatic assays for the in vitro motor activity of transcription termination factor Rho from Escherichia coli
    • Boudvillain M, Walmacq C, Schwartz A, Jacquinot F. Simple enzymatic assays for the in vitro motor activity of transcription termination factor Rho from Escherichia coli. Methods Mol Biol. 2010;587:137-54.
    • (2010) Methods Mol Biol , vol.587 , pp. 137-154
    • Boudvillain, M.1    Walmacq, C.2    Schwartz, A.3    Jacquinot, F.4
  • 48
  • 49
    • 84861992434 scopus 로고    scopus 로고
    • Activation of the replicative DNA helicase: Breaking up is hard to do
    • Boos D, Frigola J, Dif fl ey JF. Activation of the replicative DNA helicase: breaking up is hard to do. Curr Opin Cell Biol. 2012;24:423-30.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 423-430
    • Boos, D.1    Frigola, J.2    Diffley, J.F.3
  • 50
    • 64149093563 scopus 로고    scopus 로고
    • Unwinding the structure and function of the archaeal MCM helicase
    • Sakakibara N, Kelman LM, Kelman Z. Unwinding the structure and function of the archaeal MCM helicase. Mol Microbiol. 2009;72:286-96.
    • (2009) Mol Microbiol , vol.72 , pp. 286-296
    • Sakakibara, N.1    Kelman, L.M.2    Kelman, Z.3
  • 51
    • 74749095240 scopus 로고    scopus 로고
    • Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins
    • Ilves I, Petojevic T, Pesavento JJ, Botchan MR. Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins. Mol Cell. 2010;37:247-58.
    • (2010) Mol Cell , vol.37 , pp. 247-258
    • Ilves, I.1    Petojevic, T.2    Pesavento, J.J.3    Botchan, M.R.4
  • 52
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • West SC. Processing of recombination intermediates by the RuvABC proteins. Annu Rev Genet. 1997;31:213-44.
    • (1997) Annu Rev Genet , vol.31 , pp. 213-244
    • West, S.C.1
  • 53
    • 50249180325 scopus 로고    scopus 로고
    • SnapShot: Nucleic acid helicases and translocases
    • Berger JM. SnapShot: nucleic acid helicases and translocases. Cell . 2008;134: 888-888.e1
    • (2008) Cell , vol.134
    • Berger, J.M.1
  • 54
    • 66449130744 scopus 로고    scopus 로고
    • RVB1/RVB2: Running rings around molecular biology
    • Jha S, Dutta A. RVB1/RVB2: running rings around molecular biology. Mol Cell. 2009;34:521-33.
    • (2009) Mol Cell , vol.34 , pp. 521-533
    • Jha, S.1    Dutta, A.2
  • 55
    • 78651373440 scopus 로고    scopus 로고
    • The multifaceted proteins Reptin and Pontin as major players in cancer
    • Grigoletto A, Lestienne P, Rosenbaum J. The multifaceted proteins Reptin and Pontin as major players in cancer. Biochim Biophys Acta. 2011;1815:147-57.
    • (2011) Biochim Biophys Acta , vol.1815 , pp. 147-157
    • Grigoletto, A.1    Lestienne, P.2    Rosenbaum, J.3
  • 56
    • 18644379392 scopus 로고    scopus 로고
    • Crystal structure of the RuvA-RuvB complex: A structural basis for the Holliday junction migrating motor machinery
    • Yamada K, Miyata T, Tsuchiya D, Oyama T, Fujiwara Y, Ohnishi T, et al. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol Cell. 2002;10:671-81.
    • (2002) Mol Cell , vol.10 , pp. 671-681
    • Yamada, K.1    Miyata, T.2    Tsuchiya, D.3    Oyama, T.4    Fujiwara, Y.5    Ohnishi, T.6
  • 57
    • 0035852703 scopus 로고    scopus 로고
    • Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8
    • Yamada K, Kunishima N, Mayanagi K, Ohnishi T, Nishino T, Iwasaki H, et al. Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8. Proc Natl Acad Sci USA 2001;98:1442-7.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1442-1447
    • Yamada, K.1    Kunishima, N.2    Mayanagi, K.3    Ohnishi, T.4    Nishino, T.5    Iwasaki, H.6
  • 59
    • 0033792010 scopus 로고    scopus 로고
    • Two different oligomeric states of the RuvB branch migration motor protein as revealed by electron microscopy
    • Miyata T, Yamada K, Iwasaki H, Shinagawa H, Morikawa K, Mayanagi K. Two different oligomeric states of the RuvB branch migration motor protein as revealed by electron microscopy. J Struct Biol. 2000;13:83-9.
    • (2000) J Struct Biol , vol.13 , pp. 83-89
    • Miyata, T.1    Yamada, K.2    Iwasaki, H.3    Shinagawa, H.4    Morikawa, K.5    Mayanagi, K.6
  • 60
    • 0036308842 scopus 로고    scopus 로고
    • The hexameric ring structure of the Escherichia coli RuvB branch migration protein
    • Chen YJ, Yu X, Egelman EH. The hexameric ring structure of the Escherichia coli RuvB branch migration protein. J Mol Biol. 2002;319:587-91.
    • (2002) J Mol Biol , vol.319 , pp. 587-591
    • Chen, Y.J.1    Yu, X.2    Egelman, E.H.3
  • 61
    • 59649110896 scopus 로고    scopus 로고
    • Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog
    • Bae B, Chen YH, Costa A, Onesti S, Brunzelle JS, Lin Y, et al. Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog. Structure. 2009;17:211-22.
    • (2009) Structure , vol.17 , pp. 211-222
    • Bae, B.1    Chen, Y.H.2    Costa, A.3    Onesti, S.4    Brunzelle, J.S.5    Lin, Y.6
  • 62
    • 58149505656 scopus 로고    scopus 로고
    • Crystal structure of a near-full-length archaeal MCM: Functional insights for an AAA+ hexameric helicase
    • Brewster AS, Wang G, Yu X, Greenleaf WB, Carazo JM, Tjajadi M, et al. Crystal structure of a near-full-length archaeal MCM: functional insights for an AAA+ hexameric helicase. Proc Natl Acad Sci USA 2008;105:20191-6.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20191-20196
    • Brewster, A.S.1    Wang, G.2    Yu, X.3    Greenleaf, W.B.4    Carazo, J.M.5    Tjajadi, M.6
  • 63
    • 0036668640 scopus 로고    scopus 로고
    • The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings
    • Yu X, VanLoock MS, Poplawski A, Kelman Z, Xiang T, Tye BK, et al. The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings. EMBO Rep. 2002;3:792-7.
    • (2002) EMBO Rep , vol.3 , pp. 792-797
    • Yu, X.1    Vanloock, M.S.2    Poplawski, A.3    Kelman, Z.4    Xiang, T.5    Tye, B.K.6
  • 64
    • 28844449554 scopus 로고    scopus 로고
    • Polymorphism and double hexamer structure in the archaeal minichromosome maintenance (MCM) helicase from Methanobacterium thermoautotrophicum
    • Gómez-Llorente Y, Fletcher RJ, Chen XS, Carazo JM, San Martín C. Polymorphism and double hexamer structure in the archaeal minichromosome maintenance (MCM) helicase from Methanobacterium thermoautotrophicum. J Biol Chem. 2005;280:40909-15.
    • (2005) J Biol Chem , vol.280 , pp. 40909-40915
    • Gómez-Llorente, Y.1    Fletcher, R.J.2    Chen, X.S.3    Carazo, J.M.4    San Martín, C.5
  • 65
  • 66
    • 33845648483 scopus 로고    scopus 로고
    • Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity
    • Costa A, Pape T, van Heel M, Brick P, Patwardhan A, Onesti S. Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity. Nucleic Acids Res. 2006;34:5829-38.
    • (2006) Nucleic Acids Res , vol.34 , pp. 5829-5838
    • Costa, A.1    Pape, T.2    Van Heel, M.3    Brick, P.4    Patwardhan, A.5    Onesti, S.6
  • 67
    • 49949096157 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals a novel DNA-binding site on the MCM helicase
    • Costa A, van Duinen G, Medagli B, Chong J, Sakakibara N, Kelman Z, et al. Cryo-electron microscopy reveals a novel DNA-binding site on the MCM helicase. EMBO J. 2008;27:2250-8.
    • (2008) EMBO J , vol.27 , pp. 2250-2258
    • Costa, A.1    Van Duinen, G.2    Medagli, B.3    Chong, J.4    Sakakibara, N.5    Kelman, Z.6
  • 68
    • 7444249512 scopus 로고    scopus 로고
    • Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily
    • Wang J. Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily. J Struct Biol. 2004;148:259-67.
    • (2004) J Struct Biol , vol.148 , pp. 259-267
    • Wang, J.1
  • 69
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary states
    • Yu X, Jezewska MJ, Bujalowski W, Egelman EH. The hexameric E. coli DnaB helicase can exist in different quaternary states. J Mol Biol. 1996;259:7-14.
    • (1996) J Mol Biol , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4
  • 72
    • 64149103213 scopus 로고    scopus 로고
    • Mutations in subdomain B of the minichromosome maintenance (MCM) helicase affect DNA binding and modulate conformational transitions
    • Jenkinson ER, Costa A, Leech AP, Patwardhan A, Onesti S, Chong JP. Mutations in subdomain B of the minichromosome maintenance (MCM) helicase affect DNA binding and modulate conformational transitions. J Biol Chem. 2009;284:5654-61.
    • (2009) J Biol Chem , vol.284 , pp. 5654-5661
    • Jenkinson, E.R.1    Costa, A.2    Leech, A.P.3    Patwardhan, A.4    Onesti, S.5    Chong, J.P.6
  • 73
    • 39449123549 scopus 로고    scopus 로고
    • The MCM complex: (Just) a replicative helicase?
    • Costa A, Onesti S. The MCM complex: (just) a replicative helicase? Biochem Soc Trans. 2008;36:136-40.
    • (2008) Biochem Soc Trans , vol.36 , pp. 136-140
    • Costa, A.1    Onesti, S.2
  • 76
    • 70350751416 scopus 로고    scopus 로고
    • Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing
    • Remus D, Beuron F, Tolun G, Grif fi th JD, Morris EP, Dif fl ey JF. Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing. Cell. 2009;139:719-30.
    • (2009) Cell , vol.139 , pp. 719-730
    • Remus, D.1    Beuron, F.2    Tolun, G.3    Griffith, J.D.4    Morris, E.P.5    Diffley, J.F.6
  • 77
    • 0030840509 scopus 로고    scopus 로고
    • Dimerization of simian virus 40 T-antigen hexamers activates T-antigen DNA helicase activity
    • Smelkova NV, Borowiec JA. Dimerization of simian virus 40 T-antigen hexamers activates T-antigen DNA helicase activity. J Virol. 1997;71:8766-73.
    • (1997) J Virol , vol.71 , pp. 8766-8773
    • Smelkova, N.V.1    Borowiec, J.A.2
  • 78
    • 29644436609 scopus 로고    scopus 로고
    • Double hexamer disruption and biochemical activities of Methanobacterium thermoautotrophicum MCM
    • Fletcher RJ, Shen J, Gómez-Llorente Y, Martín CS, Carazo JM, Chen XS. Double hexamer disruption and biochemical activities of Methanobacterium thermoautotrophicum MCM. J Biol Chem. 2005;280:42405-10.
    • (2005) J Biol Chem , vol.280 , pp. 42405-42410
    • Fletcher, R.J.1    Shen, J.2    Gómez-Llorente, Y.3    Martín, C.S.4    Carazo, J.M.5    Chen, X.S.6
  • 79
    • 58649105140 scopus 로고    scopus 로고
    • The Methanothermobacter thermautotrophicus MCM helicase is active as a hexameric ring
    • Shin JH, Heo GY, Kelman Z. The Methanothermobacter thermautotrophicus MCM helicase is active as a hexameric ring. J Biol Chem. 2009;284:540-6.
    • (2009) J Biol Chem , vol.284 , pp. 540-546
    • Shin, J.H.1    Heo, G.Y.2    Kelman, Z.3
  • 80
    • 0031231083 scopus 로고    scopus 로고
    • Con fi rmation of the arginine- fi nger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian MR, Stege P, Scheffzek K, Wittinghofer A. Con fi rmation of the arginine- fi nger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nat Struct Biol. 1997;4:686-9.
    • (1997) Nat Struct Biol , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 81
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATPfuelled machines
    • Martin A, Baker TA, Sauer RT. Rebuilt AAA+ motors reveal operating principles for ATPfuelled machines. Nature. 2005;437:1115-20.
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 82
    • 80053897431 scopus 로고    scopus 로고
    • ATP-induced helicase slippage reveals highly coordinated subunits
    • Sun B, Johnson DS, Patel G, Smith BY, Pandey M, Patel SS, et al. ATP-induced helicase slippage reveals highly coordinated subunits. Nature. 2011;478:132-5.
    • (2011) Nature , vol.478 , pp. 132-135
    • Sun, B.1    Johnson, D.S.2    Patel, G.3    Smith, B.Y.4    Pandey, M.5    Patel, S.S.6
  • 83
    • 1842533240 scopus 로고    scopus 로고
    • The arginine fi nger of bacteriophage T7 gene 4 helicase: Role in energy coupling
    • Crampton DJ, Guo S, Johnson DE, Richardson CC. The arginine fi nger of bacteriophage T7 gene 4 helicase: role in energy coupling. Proc Natl Acad Sci USA 2004;101:4373-8.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4373-4378
    • Crampton, D.J.1    Guo, S.2    Johnson, D.E.3    Richardson, C.C.4
  • 85
  • 86
    • 0029762774 scopus 로고    scopus 로고
    • DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase
    • Yu X, Hingorani MM, Patel SS, Egelman EH. DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase. Nat Struct Biol. 1996;3:740-3.
    • (1996) Nat Struct Biol , vol.3 , pp. 740-743
    • Yu, X.1    Hingorani, M.M.2    Patel, S.S.3    Egelman, E.H.4
  • 87
    • 33846936301 scopus 로고    scopus 로고
    • Mechanisms of nucleic acid translocases: Lessons from structural biology and single-molecule biophysics
    • Hopfner KP, Michaelis J. Mechanisms of nucleic acid translocases: lessons from structural biology and single-molecule biophysics. Curr Opin Struct Biol. 2007;17:87-95.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 87-95
    • Hopfner, K.P.1    Michaelis, J.2
  • 88
    • 71449109999 scopus 로고    scopus 로고
    • A stepwise 2 ¢ -hydroxyl activation mechanism for the bacterial transcription termination factor Rho helicase
    • Schwartz A, Rabhi M, Jacquinot F, Margeat E, Rahmouni AR, Boudvillain M. A stepwise 2 ¢ -hydroxyl activation mechanism for the bacterial transcription termination factor Rho helicase. Nat Struct Mol Biol. 2009;16:1309-16.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1309-1316
    • Schwartz, A.1    Rabhi, M.2    Jacquinot, F.3    Margeat, E.4    Rahmouni, A.R.5    Boudvillain, M.6
  • 89
    • 84859980381 scopus 로고    scopus 로고
    • Properties of the human Cdc45/Mcm2-7/ GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis
    • Kang YH, Galal WC, Farina A, Tappin I, Hurwitz J. Properties of the human Cdc45/Mcm2-7/ GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis. Proc Natl Acad Sci USA 2012;109:6042-7.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 6042-6047
    • Kang, Y.H.1    Galal, W.C.2    Farina, A.3    Tappin, I.4    Hurwitz, J.5
  • 90
    • 84864571394 scopus 로고    scopus 로고
    • Structural basis for the interaction of a hexameric replicative helicase with the regulatory subunit of human DNA polymerase alpha-primase
    • Zhou B, Arnett DR, Yu X, Brewster A, Sowd GA, Xie CL, et al. Structural basis for the interaction of a hexameric replicative helicase with the regulatory subunit of human DNA polymerase alpha-primase. J Biol Chem. 2012;387(32):26854-66.
    • (2012) J Biol Chem , vol.387 , Issue.32 , pp. 26854-26866
    • Zhou, B.1    Arnett, D.R.2    Yu, X.3    Brewster, A.4    Sowd, G.A.5    Xie, C.L.6
  • 91
    • 80053575452 scopus 로고    scopus 로고
    • Dynamic coupling between the motors of DNA replication: Hexameric helicase DNA polymerase and primase
    • Patel SS, Pandey M, Nandakumar D. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase. Curr Opin Chem Biol. 2011;15:595-605.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 595-605
    • Patel, S.S.1    Pandey, M.2    Nandakumar, D.3
  • 92
    • 84864447544 scopus 로고    scopus 로고
    • Collaborative coupling between polymerase and helicase for leading-strand synthesis
    • Manosas M, Spiering MM, Ding F, Croquette V, Benkovic SJ. Collaborative coupling between polymerase and helicase for leading-strand synthesis. Nucleic Acids Res. 2012;40(13):6187-98.
    • (2012) Nucleic Acids Res , vol.40 , Issue.13 , pp. 6187-6198
    • Manosas, M.1    Spiering, M.M.2    Ding, F.3    Croquette, V.4    Benkovic, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.