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Volumn 1774, Issue 6, 2007, Pages 737-748

On translocation mechanism of ring-shaped helicase along single-stranded DNA

Author keywords

DNA unwinding; Helicase; Hexamer; Molecular motor; Translocation mechanism

Indexed keywords

HELICASE; MOLECULAR MOTOR; PHOSPHATASE; RING SHAPED HELICASE; SINGLE STRANDED DNA; THYMIDINE TRIPHOSPHATASE; THYMIDINE TRIPHOSPHATE; UNCLASSIFIED DRUG;

EID: 34249782826     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.04.002     Document Type: Article
Times cited : (9)

References (68)
  • 2
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman T.M., and Bjornson K.P. Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65 (1996) 169-214
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 3
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel S.S., and Picha K.M. Structure and function of hexameric helicases. Annu. Rev. Biochem. 69 (2000) 651-697
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 4
    • 0034479416 scopus 로고    scopus 로고
    • Crawling and wiggling on DNA: structural insights to the mechanism of DNA unwinding by helicases
    • Marians K.J. Crawling and wiggling on DNA: structural insights to the mechanism of DNA unwinding by helicases. Structure 8 (2000) R227-R235
    • (2000) Structure , vol.8
    • Marians, K.J.1
  • 5
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer
    • Weigelt J., Brown S.E., Miles C.S., Dixon N.E., and Otting G. NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 7 (1999) 681-690
    • (1999) Structure , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4    Otting, G.5
  • 6
    • 0033152872 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the DnaB hexameric helicase
    • Fass D., Bogden C.E., and Berger J.M. Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7 (1999) 691-698
    • (1999) Structure , vol.7 , pp. 691-698
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 7
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • Kaplan D.L., and O'Donnell M. DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol. Cell 10 (2002) 647-657
    • (2002) Mol. Cell , vol.10 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 8
    • 0026091055 scopus 로고
    • Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA I. Cryoelectron microscopic studies
    • Gogol E.P., Seifried S.E., and von Hippel P.H. Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA I. Cryoelectron microscopic studies. J. Mol. Biol. 221 (1991) 1127-1138
    • (1991) J. Mol. Biol. , vol.221 , pp. 1127-1138
    • Gogol, E.P.1    Seifried, S.E.2    von Hippel, P.H.3
  • 9
    • 0034705329 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of transcription termination factor rho: orientation of the N-terminal domain and visualization of an RNA-binding site
    • Yu X., Horiguchi T., Shigesada K., and Egelman E.H. Three-dimensional reconstruction of transcription termination factor rho: orientation of the N-terminal domain and visualization of an RNA-binding site. J. Mol. Biol. 299 (2000) 1279-1287
    • (2000) J. Mol. Biol. , vol.299 , pp. 1279-1287
    • Yu, X.1    Horiguchi, T.2    Shigesada, K.3    Egelman, E.H.4
  • 10
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • Dong F., Gogol E.P., and von Hippel P.H. The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate. J. Biol. Chem. 270 (1995) 7462-7473
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    von Hippel, P.H.3
  • 12
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman E.H., Yu X., Wild R., Hingorani M.M., and Patel S.S. Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 3869-3873
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 13
    • 0030670510 scopus 로고    scopus 로고
    • A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding
    • Hacker K.J., and Johnson K.A. A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding. Biochemistry 36 (1997) 14080-14087
    • (1997) Biochemistry , vol.36 , pp. 14080-14087
    • Hacker, K.J.1    Johnson, K.A.2
  • 14
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar S.S., Soultanas P., Dillingham M.S., Subramanya H.S., and Wigley D.B. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97 (1999) 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
  • 16
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for active mechanism
    • Soultanas P., Dillingham M.S., Wiley P., Webb M.R., and Wigley D.B. Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for active mechanism. EMBO J. 19 (2000) 3799-3810
    • (2000) EMBO J. , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 18
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong I., and Lohman T.M. Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256 (1992) 350-355
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 19
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • Chen W., Hsieh J., Brendza K.M., and Lohman T.M. E. coli Rep oligomers are required to initiate DNA unwinding in vitro. J. Mol. Biol. 310 (2001) 327-350
    • (2001) J. Mol. Biol. , vol.310 , pp. 327-350
    • Chen, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 20
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and reinitiation of DNA unwinding by the Escherichia coli Rep helicase
    • Ha T., Rasnik I., Chen W., Babcock H.P., Gauss G.H., Lohman T.M., and Chu S. Initiation and reinitiation of DNA unwinding by the Escherichia coli Rep helicase. Nature 419 (2002) 638-641
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1    Rasnik, I.2    Chen, W.3    Babcock, H.P.4    Gauss, G.H.5    Lohman, T.M.6    Chu, S.7
  • 22
    • 0034732885 scopus 로고    scopus 로고
    • DNA binding in the central channel of bacteriophage T7 helicase-primase is a multistep process. Nucleotide hydrolysis is not required
    • Picha K.M., Ahnert P., and Patel S.S. DNA binding in the central channel of bacteriophage T7 helicase-primase is a multistep process. Nucleotide hydrolysis is not required. Biochemistry 39 (2000) 6401-6409
    • (2000) Biochemistry , vol.39 , pp. 6401-6409
    • Picha, K.M.1    Ahnert, P.2    Patel, S.S.3
  • 23
    • 2142675722 scopus 로고
    • Template recognition sequence for RNA primer synthesis by gene 4 protein of bacteriophage T7
    • Tabor S., and Richardson C.C. Template recognition sequence for RNA primer synthesis by gene 4 protein of bacteriophage T7. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 205-209
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 205-209
    • Tabor, S.1    Richardson, C.C.2
  • 24
    • 0036382873 scopus 로고    scopus 로고
    • T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA
    • Kim D.-E., Narayan M., and Patel S.S. T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA. J. Mol. Biol. 321 (2002) 807-819
    • (2002) J. Mol. Biol. , vol.321 , pp. 807-819
    • Kim, D.-E.1    Narayan, M.2    Patel, S.S.3
  • 25
    • 0032478641 scopus 로고    scopus 로고
    • Increased DNA unwinding efficiency of bacteriophage T7 DNA helicase mutant protein 4A′/E348K
    • Washington M.T., and Patel S.S. Increased DNA unwinding efficiency of bacteriophage T7 DNA helicase mutant protein 4A′/E348K. J. Biol. Chem. 273 (1998) 7880-7887
    • (1998) J. Biol. Chem. , vol.273 , pp. 7880-7887
    • Washington, M.T.1    Patel, S.S.2
  • 26
    • 2442513338 scopus 로고    scopus 로고
    • The DNA-unwinding mechanism of the ring helicase of bacteriophage T7
    • Jeong Y.-J., Levin M.K., and Patel S.S. The DNA-unwinding mechanism of the ring helicase of bacteriophage T7. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 7264-7269
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7264-7269
    • Jeong, Y.-J.1    Levin, M.K.2    Patel, S.S.3
  • 27
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: a τ-DnaB interaction mediates rapid replication fork movement
    • Kim S., Dallmann H.G., McHenry C.S., and Marians K.J. Coupling of a replicative polymerase and helicase: a τ-DnaB interaction mediates rapid replication fork movement. Cell 84 (1996) 643-650
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 28
    • 0035836479 scopus 로고    scopus 로고
    • Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork
    • Delagoutte E., and von Hippel P.H. Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork. Biochemistry 40 (2001) 4459-4477
    • (2001) Biochemistry , vol.40 , pp. 4459-4477
    • Delagoutte, E.1    von Hippel, P.H.2
  • 29
    • 19644399070 scopus 로고    scopus 로고
    • DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase
    • Stano N.M., Jeong Y.-J., Donmez I., Tummalapalli P., Levin M.K., and Patel S.S. DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase. Nature 435 (2005) 370-373
    • (2005) Nature , vol.435 , pp. 370-373
    • Stano, N.M.1    Jeong, Y.-J.2    Donmez, I.3    Tummalapalli, P.4    Levin, M.K.5    Patel, S.S.6
  • 30
    • 33748335314 scopus 로고    scopus 로고
    • Structure-based model of the stepping motor of PcrA helicase
    • Yu J., Ha T., and Schulten K. Structure-based model of the stepping motor of PcrA helicase. Biophys. J. 91 (2006) 2097-2114
    • (2006) Biophys. J. , vol.91 , pp. 2097-2114
    • Yu, J.1    Ha, T.2    Schulten, K.3
  • 31
    • 0038607629 scopus 로고    scopus 로고
    • ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase
    • Levin M.K., Gurjar M.M., and Patel S.S. ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase. J. Biol. Chem. 278 (2003) 23311-23316
    • (2003) J. Biol. Chem. , vol.278 , pp. 23311-23316
    • Levin, M.K.1    Gurjar, M.M.2    Patel, S.S.3
  • 32
    • 20444440763 scopus 로고    scopus 로고
    • A Brownian motor mechanism of translocation and strand separation by hepatits C virus helicase
    • Levin M.K., Gurjar M.M., and Patel S.S. A Brownian motor mechanism of translocation and strand separation by hepatits C virus helicase. Nat. Struct. Mol. Biol. 12 (2005) 429-435
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 429-435
    • Levin, M.K.1    Gurjar, M.M.2    Patel, S.S.3
  • 33
    • 17644443277 scopus 로고    scopus 로고
    • A motor that makes its own track: helicase unwinding of DNA
    • Betterton M.D., and Julicher F. A motor that makes its own track: helicase unwinding of DNA. Phys. Rev. Lett. 91 (2003) 258103
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 258103
    • Betterton, M.D.1    Julicher, F.2
  • 35
    • 33846001316 scopus 로고    scopus 로고
    • Model for helicase translocating along single-stranded DNA and unwinding double-stranded DNA
    • Xie P. Model for helicase translocating along single-stranded DNA and unwinding double-stranded DNA. Biochim. Biophys. Acta 1764 (2006) 1719-1729
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1719-1729
    • Xie, P.1
  • 36
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their 'coupling' within macromolecular machines
    • von Hippel P.H., and Delagoutte E. A general model for nucleic acid helicases and their 'coupling' within macromolecular machines. Cell 104 (2001) 177-190
    • (2001) Cell , vol.104 , pp. 177-190
    • von Hippel, P.H.1    Delagoutte, E.2
  • 37
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M., Sawaya M., Ellenberger T., and Wigley D. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101 (2000) 589-600
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.1    Sawaya, M.2    Ellenberger, T.3    Wigley, D.4
  • 39
    • 30744451401 scopus 로고    scopus 로고
    • DNA-induced switch from independent to sequential dTTP hydrolysis in the Bacteriophage T7 DNA helicase
    • Crampton D.J., Mukherjee S., and Richardson C.C. DNA-induced switch from independent to sequential dTTP hydrolysis in the Bacteriophage T7 DNA helicase. Mol. Cell 21 (2006) 165-174
    • (2006) Mol. Cell , vol.21 , pp. 165-174
    • Crampton, D.J.1    Mukherjee, S.2    Richardson, C.C.3
  • 40
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark E.J., and Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442 (2006) 270-275
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 41
    • 0030987298 scopus 로고    scopus 로고
    • The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase
    • Hingorani M.M., Washington M.T., Moore K.C., and Patel S.S. The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 5012-5017
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5012-5017
    • Hingorani, M.M.1    Washington, M.T.2    Moore, K.C.3    Patel, S.S.4
  • 42
    • 0037113894 scopus 로고    scopus 로고
    • Kinetic pathway of dTTP hydrolysis by hexameric T7 helicase-primase in the absence of DNA
    • Jeong Y.J., Kim D.E., and Patel S.S. Kinetic pathway of dTTP hydrolysis by hexameric T7 helicase-primase in the absence of DNA. J. Biol. Chem. 277 (2002) 43778-43784
    • (2002) J. Biol. Chem. , vol.277 , pp. 43778-43784
    • Jeong, Y.J.1    Kim, D.E.2    Patel, S.S.3
  • 43
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - some probabilities and possibilities
    • Boyer P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215-250
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 46
    • 0030045742 scopus 로고    scopus 로고
    • Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases
    • Hingorani M.M., and Patel S.S. Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases. Biochemistry 35 (1996) 2218-2228
    • (1996) Biochemistry , vol.35 , pp. 2218-2228
    • Hingorani, M.M.1    Patel, S.S.2
  • 47
    • 0027373139 scopus 로고
    • Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs
    • Hingorani M.M., and Patel S.S. Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs. Biochemistry 32 (1993) 12478-12487
    • (1993) Biochemistry , vol.32 , pp. 12478-12487
    • Hingorani, M.M.1    Patel, S.S.2
  • 48
    • 0029072199 scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer
    • Bujalowski W., and Jezewska M.J. Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer. Biochemistry 34 (1995) 8513-8519
    • (1995) Biochemistry , vol.34 , pp. 8513-8519
    • Bujalowski, W.1    Jezewska, M.J.2
  • 49
    • 0030052444 scopus 로고    scopus 로고
    • Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer
    • Jezewska M.J., Kim U.-S., and Bujalowski W. Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer. Biochemistry 35 (1996) 2129-2145
    • (1996) Biochemistry , vol.35 , pp. 2129-2145
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 50
    • 0023745709 scopus 로고
    • A 7-kDa region of the bacteriophage T7 gene 4 protein is required for primase but not for helicase activity
    • Bernstein J.A., and Richardson C.C. A 7-kDa region of the bacteriophage T7 gene 4 protein is required for primase but not for helicase activity. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 396-400
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 396-400
    • Bernstein, J.A.1    Richardson, C.C.2
  • 51
    • 0026651756 scopus 로고
    • Large scale purification and biochemical characterization of T7 primase/helicase proteins. Evidence for homodimer and heterodimer formation
    • Patel S.S., Rosenberg A.H., Studier F.W., and Johnson K.A. Large scale purification and biochemical characterization of T7 primase/helicase proteins. Evidence for homodimer and heterodimer formation. J. Biol. Chem. 267 (1992) 15013-15021
    • (1992) J. Biol. Chem. , vol.267 , pp. 15013-15021
    • Patel, S.S.1    Rosenberg, A.H.2    Studier, F.W.3    Johnson, K.A.4
  • 52
    • 0032538625 scopus 로고    scopus 로고
    • 2+. The presence of dTTP is sufficient for hexamer formation and DNA binding
    • 2+. The presence of dTTP is sufficient for hexamer formation and DNA binding. J. Biol. Chem. 273 (1998) 27315-27319
    • (1998) J. Biol. Chem. , vol.273 , pp. 27315-27319
    • Picha, K.M.1    Patel, S.S.2
  • 53
    • 0034600838 scopus 로고    scopus 로고
    • A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein
    • Ahnert P., Picha K.M., and Patel S.S. A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein. EMBO J. 19 (2000) 3418-3427
    • (2000) EMBO J. , vol.19 , pp. 3418-3427
    • Ahnert, P.1    Picha, K.M.2    Patel, S.S.3
  • 54
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya M.R., Guo S., Tabor S., Richardson C.C., and Ellenberger T. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell 99 (1999) 167-177
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 56
    • 4544386863 scopus 로고    scopus 로고
    • Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation
    • Mancini E.J., Kainov D.E., Grimes J.M., Tuma R., Bamford D.H., and Stuart D.I. Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation. Cell 118 (2004) 743-755
    • (2004) Cell , vol.118 , pp. 743-755
    • Mancini, E.J.1    Kainov, D.E.2    Grimes, J.M.3    Tuma, R.4    Bamford, D.H.5    Stuart, D.I.6
  • 57
    • 12144258604 scopus 로고    scopus 로고
    • Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda helicase
    • Eoff R.L., Spurling T.L., and Raney K.D. Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda helicase. Biochemistry 44 (2005) 666-674
    • (2005) Biochemistry , vol.44 , pp. 666-674
    • Eoff, R.L.1    Spurling, T.L.2    Raney, K.D.3
  • 58
    • 33749121811 scopus 로고    scopus 로고
    • Mechanisms of a ring shaped helicase
    • Donmez I., and Patel S.S. Mechanisms of a ring shaped helicase. Nucleic Acids Res. 34 (2006) 4216-4224
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4216-4224
    • Donmez, I.1    Patel, S.S.2
  • 60
    • 4644261530 scopus 로고    scopus 로고
    • Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: Quantitative analysis of the rate of the dsDNA unwinding, processivity and kinetic step-size of the Escherichia coli DnaB helicase using rapid quench-flow method
    • Galletto R., Jezewska M.J., and Bujalowski W. Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: Quantitative analysis of the rate of the dsDNA unwinding, processivity and kinetic step-size of the Escherichia coli DnaB helicase using rapid quench-flow method. J. Mol. Biol. 343 (2004) 83-99
    • (2004) J. Mol. Biol. , vol.343 , pp. 83-99
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 62
    • 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 M., Patel S.S., and Egelman E.H. DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase. Nat. Struct. Biol. 3 (1996) 740-743
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 740-743
    • Yu, X.1    Hingorani, M.2    Patel, S.S.3    Egelman, E.H.4
  • 63
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith S.B., Yujia C., and Bustamante C. Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science 271 (1996) 795-799
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Yujia, C.2    Bustamante, C.3
  • 64
    • 0031238076 scopus 로고    scopus 로고
    • Persistence length of single-stranded DNA
    • Tinland B., Pluen A., Sturm J., and Weill G. Persistence length of single-stranded DNA. Macromolecules 30 (1997) 5763-5765
    • (1997) Macromolecules , vol.30 , pp. 5763-5765
    • Tinland, B.1    Pluen, A.2    Sturm, J.3    Weill, G.4
  • 65
    • 33750441848 scopus 로고    scopus 로고
    • Model for unidirectional movement of axonemal and cytoplasmic dynein molecules
    • Xie P., Dou S.-X., and Wang P.-Y. Model for unidirectional movement of axonemal and cytoplasmic dynein molecules. Acta Biochim. Biophys. Sin. 38 (2006) 711-724
    • (2006) Acta Biochim. Biophys. Sin. , vol.38 , pp. 711-724
    • Xie, P.1    Dou, S.-X.2    Wang, P.-Y.3
  • 66
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed
    • Dilingham M., Wigley D.B., and Webb M.R. Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry 39 (2000) 205-212
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dilingham, M.1    Wigley, D.B.2    Webb, M.R.3
  • 67
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ{symbol} 29
    • Guo P.X., Peterson C., and Anderson D.L. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ{symbol} 29. J. Mol. Biol. 197 (1987) 229-236
    • (1987) J. Mol. Biol. , vol.197 , pp. 229-236
    • Guo, P.X.1    Peterson, C.2    Anderson, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.