메뉴 건너뛰기




Volumn 22, Issue 18, 2003, Pages 4579-4583

Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes

Author keywords

ATP hydrolysis; Binding energy; Catalysis; Nucleic acid modifying enzymes

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA; ENZYME; NUCLEIC ACID;

EID: 0141514042     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg441     Document Type: Review
Times cited : (14)

References (31)
  • 1
    • 0038193630 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase IIIβ sliding clamp: Bona fide primer/templates preferentially trigger the γ complex to hydrolyze ATP and load the clamp
    • Ason, B., Handayani, R., Williams, C.R., Bertram, J.G., Hingorani, M.M., O'Donnell, M., Goodman, M.F. and Bloom, L.B. (2003) Mechanism of loading the Escherichia coli DNA polymerase IIIβ sliding clamp: bona fide primer/templates preferentially trigger the γ complex to hydrolyze ATP and load the clamp. J. Biol. Chem., 278, 10033-10040.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10033-10040
    • Ason, B.1    Handayani, R.2    Williams, C.R.3    Bertram, J.G.4    Hingorani, M.M.5    O'Donnell, M.6    Goodman, M.F.7    Bloom, L.B.8
  • 2
    • 0037119967 scopus 로고    scopus 로고
    • Nucleosome sliding: Facts and fiction
    • Becker, P.B. (2002) Nucleosome sliding: facts and fiction. EMBO J., 21, 4749-4753.
    • (2002) EMBO J. , vol.21 , pp. 4749-4753
    • Becker, P.B.1
  • 3
  • 4
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • 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.
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 5
    • 77956919579 scopus 로고
    • DNA ligases
    • Boyer, P.D. (ed.). Academic Press, New York, NY
    • Engler, M.J., and Richardson, C.C. (1982) DNA ligases. In Boyer, P.D. (ed.), The Enzymes, Vol. 15. Academic Press, New York, NY, pp. 3-29.
    • (1982) The Enzymes , vol.15 , pp. 3-29
    • Engler, M.J.1    Richardson, C.C.2
  • 6
    • 0001341401 scopus 로고
    • Binding energy and catalysis: A lesson from protein engineering of the tyrosyl-tRNA synthetase
    • Fersht, A.R., Leatherbarrow, R.J. and Wells, T.N.C. (1986) Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthetase. Trends Biochem. Sci., 11, 321-325.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 321-325
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.C.3
  • 7
    • 0034595208 scopus 로고    scopus 로고
    • Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement
    • Firman, K. and Szczelkun, M.D. (2000) Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement. EMBO J., 19, 2094-2102.
    • (2000) EMBO J. , vol.19 , pp. 2094-2102
    • Firman, K.1    Szczelkun, M.D.2
  • 8
    • 0004214524 scopus 로고
    • Longman Green, London, UK
    • Haldane, J.B.S. (1930) Enzymes. Longman Green, London, UK, p. 182.
    • (1930) Enzymes , pp. 182
    • Haldane, J.B.S.1
  • 9
    • 0033555922 scopus 로고    scopus 로고
    • The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity
    • Hall, M.C. and Matson, S.W. (1999) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity. J. Biol. Chem., 274, 1306-1312.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1306-1312
    • Hall, M.C.1    Matson, S.W.2
  • 10
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in Dna double-strand break repair and in the ABC-ATPase superfamily
    • Hopfner, K.P., Karcher, A., Shin, D.S., Craig, L., Arthur, L.M., Carney, J.P. and Tainer J.A. (2000) Structural biology of Rad50 ATPase: ATP-driven conformational control in Dna double-strand break repair and in the ABC-ATPase superfamily. Cell, 101, 789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 11
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DexH/D RNA helicase
    • Jankowsky, E., Gross, C.H., Shuman, S. and Pyle, A.M. (2001) Active disruption of an RNA-protein interaction by a DexH/D RNA helicase. Science, 291, 121-125.
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 13
    • 0345270445 scopus 로고    scopus 로고
    • Powering DNA repair through substrate electrostatic interactions
    • Jiang, Y.L., Ichikawa, Y., Song, F. and Stivers, J.T. (2003) Powering DNA repair through substrate electrostatic interactions. Biochemistry, 42, 1922-1929.
    • (2003) Biochemistry , vol.42 , pp. 1922-1929
    • Jiang, Y.L.1    Ichikawa, Y.2    Song, F.3    Stivers, J.T.4
  • 14
    • 0035102126 scopus 로고    scopus 로고
    • Composite active site of an ATPase: MutS uses ATP to verify mismatch recognition and authorise DNA repair
    • Junop, M.S., Obmolova, Rausch, K., Hseih, P. and Yang, W. (2001) Composite active site of an ATPase: MutS uses ATP to verify mismatch recognition and authorise DNA repair. Mol. Cell, 7, 1-12.
    • (2001) Mol. Cell , vol.7 , pp. 1-12
    • Junop, M.S.1    Obmolova2    Rausch, K.3    Hseih, P.4    Yang, W.5
  • 15
    • 0035902562 scopus 로고    scopus 로고
    • ATP bound to the origin recognition complex is important for preRC formation
    • Klemm, R.D. and Bell, S.P. (2001) ATP bound to the origin recognition complex is important for preRC formation. Proc. Natl Acad. Sci. USA, 98, 8361-8367.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8361-8367
    • Klemm, R.D.1    Bell, S.P.2
  • 16
    • 0037415693 scopus 로고    scopus 로고
    • The alternating ATPase domains of MutS control DNA mismatch repair
    • Lamers, M.H., Winterwerp, H.H.K. and Sixma, T. (2003) The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J., 22, 746-756.
    • (2003) EMBO J. , vol.22 , pp. 746-756
    • Lamers, M.H.1    Winterwerp, H.H.K.2    Sixma, T.3
  • 17
    • 0025166577 scopus 로고
    • Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis
    • Menetski, J.P., Bear, D.G. and Kowalczykowski, S.C. (1990) Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis. Proc. Natl Acad. Sci. USA, 87, 21-25.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 21-25
    • Menetski, J.P.1    Bear, D.G.2    Kowalczykowski, S.C.3
  • 18
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination and cancer biology
    • Modrich, P. and Lahue, R. (1996) Mismatch repair in replication fidelity, genetic recombination and cancer biology. Annu. Rev. Biochem., 65, 101-133.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 19
    • 0033586732 scopus 로고    scopus 로고
    • DNA helicases displace streptavidin from biotin-labeled oligonucleotides
    • Morris, P.D. and Raney, K.D. (1999) DNA helicases displace streptavidin from biotin-labeled oligonucleotides. Biochemistry, 38, 5164-5171.
    • (1999) Biochemistry , vol.38 , pp. 5164-5171
    • Morris, P.D.1    Raney, K.D.2
  • 20
    • 0037178719 scopus 로고    scopus 로고
    • Segregating sister genomes: The molecular biology of chromosome separation
    • Nasmyth, K. (2002) Segregating sister genomes: the molecular biology of chromosome separation. Science, 297, 559-565.
    • (2002) Science , vol.297 , pp. 559-565
    • Nasmyth, K.1
  • 21
    • 0030758268 scopus 로고    scopus 로고
    • Simplification of DNA topology below equilibrium values by type II topoisomerases
    • Rybenkov, V.V., Ullsperger, C., Vologodskii, A.V. and Cozzarelli, N.R. (1997) Simplification of DNA topology below equilibrium values by type II topoisomerases. Science, 277, 690-693.
    • (1997) Science , vol.277 , pp. 690-693
    • Rybenkov, V.V.1    Ullsperger, C.2    Vologodskii, A.V.3    Cozzarelli, N.R.4
  • 22
    • 0028817877 scopus 로고
    • From molecular diversity to catalysis: Lessons from the immune system
    • Schultz, P.G. and Lerner, R.A. (1995) From molecular diversity to catalysis: lessons from the immune system. Science, 269, 1835-1842.
    • (1995) Science , vol.269 , pp. 1835-1842
    • Schultz, P.G.1    Lerner, R.A.2
  • 23
    • 0000262312 scopus 로고
    • Mechanism of mRNA capping by vaccinia virus guanylyltransferase: Characterization of an enzyme-guanylate intermediate
    • Shuman S., and Hurwitz, J. (1981) Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate. Proc. Natl Acad. Sci. USA, 78, 187-191.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 187-191
    • Shuman, S.1    Hurwitz, J.2
  • 24
    • 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
  • 25
    • 0033167929 scopus 로고    scopus 로고
    • Structural maintenance of chromosomes (SMC) proteins: Conserved molecular properties for multiple biological functions
    • Strunnikov, A.V. and Jessberger, R. (1999) Structural maintenance of chromosomes (SMC) proteins: conserved molecular properties for multiple biological functions. Eur. J. Biochem., 263, 6-13.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 6-13
    • Strunnikov, A.V.1    Jessberger, R.2
  • 26
    • 0032913521 scopus 로고    scopus 로고
    • A surfeit of Rad51-like genes?
    • Thacker, J. (1999) A surfeit of Rad51-like genes? Trends Genet., 15, 166-168.
    • (1999) Trends Genet. , vol.15 , pp. 166-168
    • Thacker, J.1
  • 27
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA 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 structures of complexes of PcrA 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
  • 28
    • 0027317028 scopus 로고
    • Structure-function correlation for the EcoRV restriction enzyme: From non-specific binding to specific DNA cleavage
    • Vipond, I.B. and Halford S.E. (1993) Structure-function correlation for the EcoRV restriction enzyme: from non-specific binding to specific DNA cleavage. Mol. Microbiol., 9, 225-231.
    • (1993) Mol. Microbiol. , vol.9 , pp. 225-231
    • Vipond, I.B.1    Halford, S.E.2
  • 29
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang, J.C. (1996) DNA topoisomerases. Ann. Rev. Biochem., 65, 635-692.
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 30
    • 0029911566 scopus 로고    scopus 로고
    • The RuvABC proteins and Holliday junction processing in E.coli
    • West, S.C. (1996) The RuvABC proteins and Holliday junction processing in E.coli. J. Bacteriol., 178, 1237-1241.
    • (1996) J. Bacteriol. , vol.178 , pp. 1237-1241
    • West, S.C.1
  • 31
    • 0034659247 scopus 로고    scopus 로고
    • DNA helicases: One small step for PcrA, one giant leap for RecBC?
    • Wigley, D.B. (2000) DNA helicases: one small step for PcrA, one giant leap for RecBC? Curr. Biol., 10, R444-R445.
    • (2000) Curr. Biol. , vol.10
    • Wigley, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.