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Volumn 48, Issue 19, 2009, Pages 4019-4030

Mutational analysis of mycobacterium UvrD1 identifies functional groups required for ATP hydrolysis, DNA unwinding, and chemomechanical coupling

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; BINDING RESIDUES; C-TERMINAL DOMAINS; CHEMO-MECHANICAL COUPLINGS; DIVALENT CATION; DNA HELICASE; DNA UNWINDING; GAIN-OF FUNCTION; HELICASE; HELICASES; MOTOR ACTIVITY; MOTOR DOMAIN; MUTATIONAL ANALYSIS; MYCOBACTERIAL; SUBSTRATE SPECIFICITY; TRANSITION STATE; TRANSITION STATE STABILIZATION;

EID: 66049148193     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900103d     Document Type: Article
Times cited : (29)

References (32)
  • 1
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M. R., Dillingham, M. S., and Wigley, D. B. (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
  • 2
    • 0030740262 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
    • DOI 10.1016/S0092-8674(00)80525-5
    • Korolev, S., Hsieh, J., Gauss, G. H., Lohman, T. M., and Waksman, G. (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, 635-647. (Pubitemid 27357956)
    • (1997) Cell , vol.90 , Issue.4 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 3
    • 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. (1999) Crystal structure of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 87, 75-84. (Pubitemid 29165891)
    • (1999) Cell , vol.97 , Issue.1 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 4
    • 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 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
  • 5
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • DOI 10.1021/bi992105o
    • Dillingham, M. S., Wigley, D. B., and Webb, M. R. (2000) Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry 39, 205-212. (Pubitemid 30033335)
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 6
    • 34247602963 scopus 로고    scopus 로고
    • Coli UvrD monomer translocation along single-stranded DNA
    • Tomko, E. J., Fischer, C. J., Niedziela-Majka, A., and Lohman, T. M. (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
  • 7
    • 34447515950 scopus 로고    scopus 로고
    • Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair
    • Sinha, K. M., Stephanou, N. C., Gao, F., Glickman, M. S., and Shuman, S. (2007) Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair. J. Biol. Chem. 282, 15114-15125.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15114-15125
    • Sinha, K.M.1    Stephanou, N.C.2    Gao, F.3    Glickman, M.S.4    Shuman, S.5
  • 8
    • 51549091830 scopus 로고    scopus 로고
    • Domain requirements for DNA unwinding by mycobacterial UvrD2, an essential DNA helicase
    • Sinha, K. M., Stephanou, N. C., Unciuleac, M. C., Glickman, M. S., and Shuman, S. (2008) Domain requirements for DNA unwinding by mycobacterial UvrD2, an essential DNA helicase. Biochemistry 47, 9355-9364.
    • (2008) Biochemistry , vol.47 , pp. 9355-9364
    • Sinha, K.M.1    Stephanou, N.C.2    Unciuleac, M.C.3    Glickman, M.S.4    Shuman, S.5
  • 9
    • 33947393189 scopus 로고    scopus 로고
    • Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD
    • DOI 10.1128/JB.01421-06
    • Curti, E., Smerdon, S. J., and Davis, E. O. (2007) Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD. J. Bacteriol. 189, 1542-1555. (Pubitemid 46446115)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1542-1555
    • Curti, E.1    Smerdon, S.J.2    Davis, E.O.3
  • 10
    • 39449129496 scopus 로고    scopus 로고
    • The pathways and outcomes of mycobacterial NHEJ depend on the structure of the broken DNA ends
    • Aniukwu, J., Glickman, M. S., and Shuman, S. (2008) The pathways and outcomes of mycobacterial NHEJ depend on the structure of the broken DNA ends. Genes Dev. 22, 512-527.
    • (2008) Genes Dev. , vol.22 , pp. 512-527
    • Aniukwu, J.1    Glickman, M.S.2    Shuman, S.3
  • 11
    • 0033516596 scopus 로고    scopus 로고
    • DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase
    • DOI 10.1006/jmbi.1999.2873
    • Soultanas, P., Dillingham, M. S., Velankar, S. S., and Wigley, D. B. (1999) DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase. J. Mol. Biol. 290, 137-148. (Pubitemid 29308580)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.1 , pp. 137-148
    • Soultanas, P.1    Dillingham, M.S.2    Velankar, S.S.3    Wigley, D.B.4
  • 12
    • 0033566657 scopus 로고    scopus 로고
    • Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation
    • DOI 10.1093/nar/27.16.3310
    • Dillingham, M. S., Soultanas, P., and Wigley, D. B. (1999) Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation. Nucleic Acids Res. 27, 3310-3317. (Pubitemid 29381324)
    • (1999) Nucleic Acids Research , vol.27 , Issue.16 , pp. 3310-3317
    • Dillingham, M.S.1    Soultanas, P.2    Wigley, D.B.3
  • 14
    • 0029079703 scopus 로고
    • Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase-II, a DExH box RNA helicase
    • Gross, C. H., and Shuman, S. (1995) Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase-II, a DExH box RNA helicase. J. Virol. 69, 4727-4736.
    • (1995) J. Virol. , vol.69 , pp. 4727-4736
    • Gross, C.H.1    Shuman, S.2
  • 15
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: A newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • Tanner, N. K., Cordin, O., Banroques, J., Doere, M., and Linder, P. (2003) The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol. Cell 11, 127-138.
    • (2003) Mol. Cell , vol.11 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 16
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • DOI 10.1038/sj.emboj.7600272
    • Cordin, O., Tanner, N. K., Moere, M., Linder, P., and Banroques, J. (2004) The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBOJ. 23, 2478-2487. (Pubitemid 38988220)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroques, J.5
  • 17
    • 0033573066 scopus 로고    scopus 로고
    • Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
    • Theis, K., Chen, P. J., Skorvaga, M., Van Houten, B., and Kisker, C. (1999) Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair. EMBO J. 18, 6899-6907.
    • (1999) EMBO J. , vol.18 , pp. 6899-6907
    • Theis, K.1    Chen, P.J.2    Skorvaga, M.3    Van Houten, B.4    Kisker, C.5
  • 18
    • 0010456859 scopus 로고    scopus 로고
    • Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae - The prototype of the DEAD box protein family
    • DOI 10.1016/S0969-2126(99)80088-4
    • Benz, J., Trachsel, H., and Baumann, U. (1999) Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae - the prototype of the DEAD box protein family. Structure 7, 671-679. (Pubitemid 29277420)
    • (1999) Structure , vol.7 , Issue.6 , pp. 671-679
    • Benz, J.1    Trachsel, H.2    Baumann, U.3
  • 19
    • 23644449094 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of DEAD-box protein Dhh1p
    • DOI 10.1261/rna.2920905
    • Cheng, Z., Coller, J., Parker, R., and Song, H. (2005) Crystal structure and functional analysis of the DEAD-box protein Dhh1p. RNA 11, 1258-1270. (Pubitemid 41132397)
    • (2005) RNA , vol.11 , Issue.8 , pp. 1258-1270
    • Cheng, Z.1    Coller, J.2    Parker, R.3    Song, H.4
  • 20
    • 33746853440 scopus 로고    scopus 로고
    • Crystal Structure and Nucleotide Binding of the Thermus thermophilus RNA Helicase Hera N-terminal Domain
    • DOI 10.1016/j.jmb.2006.06.065, PII S0022283606008096
    • Rudolph, M. G., Heissmann, R., Wittmann, J. G., and Klostermeier, D. (2006) Crystal structure and nucleotide binding of the Thermus thermophilus RNA helicase Hera. J. Mol. Biol. 361, 731-743. (Pubitemid 44177741)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.4 , pp. 731-743
    • Rudolph, M.G.1    Heissmann, R.2    Wittmann, J.G.3    Klostermeier, D.4
  • 21
    • 0029620994 scopus 로고
    • Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction
    • Brosh, R. M., and Matson, S. W. (1995) Mutations in motif II of Escherichia coli helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with different effects on the unwinding reaction. J. Bacteriol. 177, 5612-5621. (Pubitemid 26028872)
    • (1995) Journal of Bacteriology , vol.177 , Issue.19 , pp. 5612-5621
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 22
    • 15444357274 scopus 로고    scopus 로고
    • A point mutation in Escherichia coli helicase II renders the enzyme nonfunctional in two DNA repair pathways
    • Brosh, R. M., and Matson, S. W. (1997) A point mutation in Escherichia coli helicase II renders the enzyme nonfunctional in two DNA repair pathways. J. Biol. Chem. 272, 572-579.
    • (1997) J. Biol. Chem. , vol.272 , pp. 572-579
    • Brosh, R.M.1    Matson, S.W.2
  • 23
    • 0030877168 scopus 로고    scopus 로고
    • Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect
    • DOI 10.1074/jbc.272.30.18614
    • Hall, M. C., and Matson, S. W. (1997) Mutations of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect. J. Biol. Chem. 272, 18614-18620. (Pubitemid 27318202)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18614-18620
    • Hall, M.C.1    Matson, S.W.2
  • 24
    • 0032571396 scopus 로고    scopus 로고
    • Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: Evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes
    • Hall, M. C., Özsoy, A. Z., and Matson, S. W. (1998) Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes. J. Mol. Biol. 277, 257-271.
    • (1998) J. Mol. Biol. , vol.277 , pp. 257-271
    • Hall, M.C.1    Özsoy, A.Z.2    Matson, S.W.3
  • 25
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • Soultanas, P., Dillingham, M. S., Wiley, P., Webb, M. R., and Wigley, D. B. (2000) Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J. 19, 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
  • 26
    • 0031901334 scopus 로고    scopus 로고
    • The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication
    • Gross, C. H., and Shuman, S. (1998) The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication. J. Virol. 72, 4729-4736. (Pubitemid 28215648)
    • (1998) Journal of Virology , vol.72 , Issue.6 , pp. 4729-4736
    • Gross, C.H.1    Shuman, S.2
  • 27
    • 0032907367 scopus 로고    scopus 로고
    • A region near the C-terminal end of Escherichia coli DNA helicase II is required for single-stranded DNA binding
    • Mechanic, L. E., Latta, M. E., and Matson, S. W. (1999) A region near the C-terminal end of Escherichia coli helicase II is required for single-stranded DNA binding. J. Bacteriol. 181 2519-2526. (Pubitemid 29181578)
    • (1999) Journal of Bacteriology , vol.181 , Issue.8 , pp. 2519-2526
    • Mechanic, L.E.1    Latta, M.E.2    Matson, S.W.3
  • 28
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to dna and its implications for double-strand break repair
    • DOI 10.1038/35088000
    • Walker, J. R., Corpina, R. A., and Goldberg, J. (2001) Structure of the Kuheterodimer bound to DNA and its implications for double-strand break repair. Nature (London) 412, 607-614. (Pubitemid 32772267)
    • (2001) Nature , vol.412 , Issue.6847 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 29
    • 32044462969 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis
    • DOI 10.1128/MCB.26.4.1183-1194.2006
    • Granneman, S., Bernstein, K. A., Bleichert, F., and Baserga, S. J. (2006) Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis. Mol. Cell. Biol. 26, 1183-1194. (Pubitemid 43202548)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.4 , pp. 1183-1194
    • Granneman, S.1    Bernstein, K.A.2    Bleichert, F.3    Baserga, S.J.4
  • 30
    • 32044449843 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis
    • DOI 10.1128/MCB.26.4.1195-1208.2006
    • Bernstein, K. A., Granneman, S., Lee, A. V., Manickam, S., and Baserga, S. J. (2006) Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis. Mol. Cell. Biol. 26, 1195-1208. (Pubitemid 43202549)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.4 , pp. 1195-1208
    • Bernstein, K.A.1    Granneman, S.2    Lee, A.V.3    Manickam, S.4    Baserga, S.J.5
  • 31
    • 0023654061 scopus 로고
    • DNA helicase II of Escherichia coli: Characterization of the single-stranded DNA-dependent NTPase and helicase activities
    • Matson, S. W., and George, J. W. (1987) DNA helicase II of Escherichia coli: characterization of the single-stranded DNA-dependent NTPase and helicase activities. J. Biol. Chem. 262, 2066-2076.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2066-2076
    • Matson, S.W.1    George, J.W.2
  • 32
    • 0032102956 scopus 로고    scopus 로고
    • Characterisation of Bacillus stearothermophilus PcrA helicase: Evidence against an active rolling mechanism
    • Bird, L. E., Brannigan, J. A., Subramanya, H. S., and Wigley, D. B. (1998) Characterisation of Bacillus stearothermophilus PcrA helicase: evidence against an active rolling mechanism. Nucleic Acids Res. 26, 2686-2693.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2686-2693
    • Bird, L.E.1    Brannigan, J.A.2    Subramanya, H.S.3    Wigley, D.B.4


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