메뉴 건너뛰기




Volumn 123, Issue 3, 1998, Pages 450-457

RecA protein has extremely high cooperativity for substrate in its ATPase activity

Author keywords

ATPase; Cooperativity; DNA binding; RecA protein; Recombination

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; RECA PROTEIN;

EID: 0031940556     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021958     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0023069449 scopus 로고
    • Enzymes of general recombination
    • Cox, M.M. and Lehman, I.R. (1987) Enzymes of general recombination. Annu. Rev. Biochem. 56, 229-262
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 229-262
    • Cox, M.M.1    Lehman, I.R.2
  • 2
    • 0027466424 scopus 로고
    • What do X-ray crystallographic and electron microscopic structural studies of the RecA protein tell us about recombination?
    • Egelman, E.H. (1993) What do X-ray crystallographic and electron microscopic structural studies of the RecA protein tell us about recombination? Curr. Opin. Struct. Biol. 3, 189-197
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 189-197
    • Egelman, E.H.1
  • 3
  • 4
    • 0002804041 scopus 로고
    • Organization of the recA gene of Escherichia coli
    • Horii, T., Ogawa, T., and Ogawa, H. (1980) Organization of the recA gene of Escherichia coli. Proc. Natl. Acad. Sci. USA 77, 313-317
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 313-317
    • Horii, T.1    Ogawa, T.2    Ogawa, H.3
  • 6
    • 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
  • 7
    • 0025634466 scopus 로고
    • Energetics of recA-mediated recombination reactions without ATP hydrolysis recA can mediate polar strand exchange but is unable to recycle
    • Rosselli, W. and Stasiak, A. (1990) Energetics of recA-mediated recombination reactions without ATP hydrolysis recA can mediate polar strand exchange but is unable to recycle. J. Mol. Biol. 216, 335-352
    • (1990) J. Mol. Biol. , vol.216 , pp. 335-352
    • Rosselli, W.1    Stasiak, A.2
  • 8
    • 0028967415 scopus 로고
    • DNA-strand exchange promoted by RecA protein in the absence of ATP: Implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions
    • Kowalczykowski, S.C. and Krupp, R.A. (1995) DNA-strand exchange promoted by RecA protein in the absence of ATP: Implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions. Proc. Natl. Acad. Sci. USA 92, 3478-3482
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3478-3482
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 9
    • 0026666652 scopus 로고
    • Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible
    • Yu, X. and Egelman, E.H. (1992) Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible. J. Mol. Biol. 227, 334-346
    • (1992) J. Mol. Biol. , vol.227 , pp. 334-346
    • Yu, X.1    Egelman, E.H.2
  • 10
    • 0027397313 scopus 로고
    • Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation
    • Rehrauer, W.M. and Kowalczykowski, S.C. (1993) Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation. J. Biol. Chem. 268, 1292-1297
    • (1993) J. Biol. Chem. , vol.268 , pp. 1292-1297
    • Rehrauer, W.M.1    Kowalczykowski, S.C.2
  • 11
    • 0026737631 scopus 로고
    • On the role of ATP hydrolysis in recA protein-mediated DNA strand exchange. 1. Bypassing a short heterologous insert in one DNA substrate
    • Kim, J.I., Cox, M.M., and Inman, R.B. (1992) On the role of ATP hydrolysis in recA protein-mediated DNA strand exchange. 1. Bypassing a short heterologous insert in one DNA substrate. J. Biol. Chem. 267, 16438-16443
    • (1992) J. Biol. Chem. , vol.267 , pp. 16438-16443
    • Kim, J.I.1    Cox, M.M.2    Inman, R.B.3
  • 12
    • 0026662981 scopus 로고
    • On the role of ATP hydrolysis in recA protein-mediated DNA strand exchange. 2. Four-strand exchanges
    • Kim, J.I., Cox, M.M., and Inman, R.B. (1992) On the role of ATP hydrolysis in recA protein-mediated DNA strand exchange. 2. Four-strand exchanges. J. Biol. Chem. 267, 16444-16449
    • (1992) J. Biol. Chem. , vol.267 , pp. 16444-16449
    • Kim, J.I.1    Cox, M.M.2    Inman, R.B.3
  • 13
    • 0028131478 scopus 로고
    • On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. III. Unidirectional branch migration and extensive hybrid DNA formation
    • Jain, S.K., Cox, M.M., and Inman, R.B. (1994) On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. III. Unidirectional branch migration and extensive hybrid DNA formation. J. Biol. Chem. 269, 20653-20661
    • (1994) J. Biol. Chem. , vol.269 , pp. 20653-20661
    • Jain, S.K.1    Cox, M.M.2    Inman, R.B.3
  • 14
    • 0028308710 scopus 로고
    • Homologous pairing and DNA strand-exchange proteins
    • Kowalczykowski, S.C. and Eggleston, A.K. (1994) Homologous pairing and DNA strand-exchange proteins. Annu. Rev. Biochem. 63, 991-1043
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 991-1043
    • Kowalczykowski, S.C.1    Eggleston, A.K.2
  • 15
    • 0019818718 scopus 로고
    • Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Characterization of ATP hydrolysis
    • Weinstock, G.M., McEntee, K., and Lehman, I.R. (1981) Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Characterization of ATP hydrolysis. J. Biol. Chem. 256, 8829-8834
    • (1981) J. Biol. Chem. , vol.256 , pp. 8829-8834
    • Weinstock, G.M.1    McEntee, K.2    Lehman, I.R.3
  • 16
    • 0019839856 scopus 로고
    • Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Steady state kinetic analysis of ATP hydrolysis
    • Weinstock, G.M., McEntee, K., and Lehman, I.R. (1981) Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Steady state kinetic analysis of ATP hydrolysis. J. Biol. Chem. 256, 8845-8849
    • (1981) J. Biol. Chem. , vol.256 , pp. 8845-8849
    • Weinstock, G.M.1    McEntee, K.2    Lehman, I.R.3
  • 17
    • 0023901357 scopus 로고
    • High salt-activation of recA protein ATPase in the absence of DNA
    • Pugh, B.F. and Cox, M.M. (1988) High salt-activation of recA protein ATPase in the absence of DNA. J. Biol. Chem. 263, 76-83
    • (1988) J. Biol. Chem. , vol.263 , pp. 76-83
    • Pugh, B.F.1    Cox, M.M.2
  • 18
    • 0020489557 scopus 로고
    • Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative
    • Silver, M.S. and Fersht, A.R. (1982) Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative. Biochemistry 21, 6066-6072
    • (1982) Biochemistry , vol.21 , pp. 6066-6072
    • Silver, M.S.1    Fersht, A.R.2
  • 20
    • 0022429092 scopus 로고
    • Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors
    • Menetski, J.P. and Kowalczykowski, S.C. (1985) Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors. J. Mol. Biol. 181, 281-295
    • (1985) J. Mol. Biol. , vol.181 , pp. 281-295
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 21
    • 0027375810 scopus 로고
    • Analysis of two distinct single-stranded DNA binding sites on the recA nucleoprotein filament
    • Zlotnick, A., Mitchell, R.S., Steed, R.K., and Brenner, S.L. (1993) Analysis of two distinct single-stranded DNA binding sites on the recA nucleoprotein filament. J. Biol. Chem. 268, 22525-22530
    • (1993) J. Biol. Chem. , vol.268 , pp. 22525-22530
    • Zlotnick, A.1    Mitchell, R.S.2    Steed, R.K.3    Brenner, S.L.4
  • 22
    • 0023648297 scopus 로고
    • Homology-dependent changes in adenosine 5′-triphosphate hydrolysis during recA protein promoted DNA strand exchange: Evidence for long paranemic complexes
    • Schutte, B.C. and Cox, M.M. (1987) Homology-dependent changes in adenosine 5′-triphosphate hydrolysis during recA protein promoted DNA strand exchange: evidence for long paranemic complexes. Biochemistry 26, 5616-5625
    • (1987) Biochemistry , vol.26 , pp. 5616-5625
    • Schutte, B.C.1    Cox, M.M.2
  • 24
    • 0028105993 scopus 로고
    • Interactions between DNA molecules bound to RecA filament. Effects of base complementarity
    • Wittung, P., Nordén, B., Kim, S.K., and Takahashi, M. (1994) Interactions between DNA molecules bound to RecA filament. Effects of base complementarity. J. Biol. Chem. 269, 5799-5803
    • (1994) J. Biol. Chem. , vol.269 , pp. 5799-5803
    • Wittung, P.1    Nordén, B.2    Kim, S.K.3    Takahashi, M.4
  • 25
    • 0001327932 scopus 로고
    • A comparative study of polydeoxyribonucleotides and polyribonucleotides by optical rotatory dispersion
    • Ts'o, P.O.P., Rapaport, S.A., and Bollum, F.J. (1966) A comparative study of polydeoxyribonucleotides and polyribonucleotides by optical rotatory dispersion. Biochemistry 5, 4153-4170
    • (1966) Biochemistry , vol.5 , pp. 4153-4170
    • Ts'o, P.O.P.1    Rapaport, S.A.2    Bollum, F.J.3
  • 26
    • 0022454127 scopus 로고
    • Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA
    • Morrical, S.W., Lee, J., and Cox, M.M. (1986) Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA. Biochemistry 25, 1482-1494
    • (1986) Biochemistry , vol.25 , pp. 1482-1494
    • Morrical, S.W.1    Lee, J.2    Cox, M.M.3
  • 27
    • 0024999088 scopus 로고
    • Inhibition of recA protein promoted ATP hydrolysis. 1. ATPγS and ADP are antagonistic inhibitors
    • Lee, J.W. and Cox, M.M. (1990) Inhibition of recA protein promoted ATP hydrolysis. 1. ATPγS and ADP are antagonistic inhibitors. Biochemistry 29, 7666-7676
    • (1990) Biochemistry , vol.29 , pp. 7666-7676
    • Lee, J.W.1    Cox, M.M.2
  • 28
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R.M. and Steitz, T.A. (1992) Structure of the recA protein-ADP complex. Nature 355, 374-376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 29
    • 0023928883 scopus 로고
    • Construction of a recombinase-deficient mutant recA protein that retains single-stranded DNA-dependent ATPase activity
    • Bryant, F.R. (1988) Construction of a recombinase-deficient mutant recA protein that retains single-stranded DNA-dependent ATPase activity. J. Biol. Chem. 263, 8716-8723
    • (1988) J. Biol. Chem. , vol.263 , pp. 8716-8723
    • Bryant, F.R.1
  • 30
    • 0025150398 scopus 로고
    • Inhibition of recA protein promoted ATP hydrolysis. 2. Longitudinal assembly and disassembly of recA protein filaments mediated by ATP and ADP
    • Lee, J.W. and Cox, M.M. (1990) Inhibition of recA protein promoted ATP hydrolysis. 2. Longitudinal assembly and disassembly of recA protein filaments mediated by ATP and ADP. Biochemistry 29, 7677-7683
    • (1990) Biochemistry , vol.29 , pp. 7677-7683
    • Lee, J.W.1    Cox, M.M.2
  • 31
    • 0021486663 scopus 로고
    • Inhibition of ATPase of the recA protein by ATP ribose-modified analogs
    • Karasaki, Y. and Higashi, K. (1984) Inhibition of ATPase of the recA protein by ATP ribose-modified analogs. Arch. Biochem. Biophys. 233, 796-799
    • (1984) Arch. Biochem. Biophys. , vol.233 , pp. 796-799
    • Karasaki, Y.1    Higashi, K.2
  • 32
    • 0007388049 scopus 로고
    • Cation transport in Escherichia coli 1. Intracellular Na and K concentrations and net cation movement
    • Schultz, S.G. and Solomon, A.K. (1961) Cation transport in Escherichia coli 1. Intracellular Na and K concentrations and net cation movement. J. Gen. Physiol. 45, 355-368
    • (1961) J. Gen. Physiol. , vol.45 , pp. 355-368
    • Schultz, S.G.1    Solomon, A.K.2
  • 33
    • 0011939443 scopus 로고
    • Cation transport in Escherichia coli 2. Intracellular chloride concentration
    • Schultz, S.G., Wilson, N.L., and Epstein, W. (1962) Cation transport in Escherichia coli 2. Intracellular chloride concentration. J. Gen. Physiol. 46, 159-166
    • (1962) J. Gen. Physiol. , vol.46 , pp. 159-166
    • Schultz, S.G.1    Wilson, N.L.2    Epstein, W.3
  • 34
    • 0028346429 scopus 로고
    • Introduction of a tryptophan reporter group into loop 1 of the recA protein. Examination of the conformational states of the recA-ssDNA complex by fluorescence spectroscopy
    • Stole, E. and Bryant, F.R. (1994) Introduction of a tryptophan reporter group into loop 1 of the recA protein. Examination of the conformational states of the recA-ssDNA complex by fluorescence spectroscopy. J. Biol. Chem. 269, 7919-7925
    • (1994) J. Biol. Chem. , vol.269 , pp. 7919-7925
    • Stole, E.1    Bryant, F.R.2
  • 35
  • 36
    • 0028980994 scopus 로고
    • N-terminal 33 amino acid residues of Escherichia coli RecA protein contribute to its self-assembly
    • Mikawa, T., Masui, R., Ogawa, T., Ogawa, H., and Kuramitu, S. (1995) N-terminal 33 amino acid residues of Escherichia coli RecA protein contribute to its self-assembly. J. Mol. Biol. 250, 471-483
    • (1995) J. Mol. Biol. , vol.250 , pp. 471-483
    • Mikawa, T.1    Masui, R.2    Ogawa, T.3    Ogawa, H.4    Kuramitu, S.5
  • 37
    • 0025848721 scopus 로고
    • Biochemical and biological function of Escherichia coli recA protein: Behavior of mutant recA proteins
    • Kowalczykowski, S.C. (1991) Biochemical and biological function of Escherichia coli recA protein: behavior of mutant recA proteins. Biochimie 73, 289-304
    • (1991) Biochimie , vol.73 , pp. 289-304
    • Kowalczykowski, S.C.1
  • 38
    • 0023008741 scopus 로고
    • Structure of helical recA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP
    • Egelman, E.H. and Stasiak, A. (1986) Structure of helical recA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP. J. Mol. Biol. 191, 677-697
    • (1986) J. Mol. Biol. , vol.191 , pp. 677-697
    • Egelman, E.H.1    Stasiak, A.2
  • 40
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R.M., Weber, I., and Steitz, T.A. (1992) The structure of the E. coli recA protein monomer and polymer. Nature 355, 318-325
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.2    Steitz, T.A.3
  • 41
    • 0024297457 scopus 로고
    • Affinity chromatography of recA protein and recA nucleoprotein complexes on recA protein-agarose column
    • Freitag, N. and McEntee, K. (1988) Affinity chromatography of recA protein and recA nucleoprotein complexes on recA protein-agarose column. J. Biol. Chem. 263, 19525-19534
    • (1988) J. Biol. Chem. , vol.263 , pp. 19525-19534
    • Freitag, N.1    McEntee, K.2
  • 42
    • 0023193491 scopus 로고
    • Properties of the duplex DNA-dependent ATPase activity of Escherichia coli recA protein and its role in branch migration
    • Kowalczykowski, S.C., Clow, J., and Krupp, R.A. (1987) Properties of the duplex DNA-dependent ATPase activity of Escherichia coli recA protein and its role in branch migration. Proc. Natl. Acad. Sci. USA 84, 3127-3131
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3127-3131
    • Kowalczykowski, S.C.1    Clow, J.2    Krupp, R.A.3
  • 43
    • 0019085413 scopus 로고
    • Conformational characteristics of the trinucleoside diphosphate dApdApdA and its constituents from nuclear magnetic resonance and circular dichroism studies. Extrapolation to the stacked conformers
    • Olsthoorn, C.S.M., Bostelaar, L.J., van Boom, J.H., and Altona, C. (1980) Conformational characteristics of the trinucleoside diphosphate dApdApdA and its constituents from nuclear magnetic resonance and circular dichroism studies. Extrapolation to the stacked conformers. Eur. J. Biochem. 112, 95-110
    • (1980) Eur. J. Biochem. , vol.112 , pp. 95-110
    • Olsthoorn, C.S.M.1    Bostelaar, L.J.2    Van Boom, J.H.3    Altona, C.4
  • 44
    • 0016837953 scopus 로고
    • Ligation of EcoRI endonuclease-generated DNA fragments into linear and circular structures
    • Dugaiczyk, A., Boyer, H.W., and Goodman, H.M. (1975) Ligation of EcoRI endonuclease-generated DNA fragments into linear and circular structures. J. Mol. Biol. 96, 171-184
    • (1975) J. Mol. Biol. , vol.96 , pp. 171-184
    • Dugaiczyk, A.1    Boyer, H.W.2    Goodman, H.M.3
  • 45
    • 0018861067 scopus 로고
    • Cooperativity in enzyme function: Equilibrium and kinetic aspects
    • Neet, K.E. (1980) Cooperativity in enzyme function: equilibrium and kinetic aspects. Methods Enzymol. 64, 139-192
    • (1980) Methods Enzymol. , vol.64 , pp. 139-192
    • Neet, K.E.1
  • 46
    • 0027742805 scopus 로고
    • Zinc as modulater of oxygenation function and stabilizer of quaternary structure in earthworm hemoglobin
    • Ochiai, T., Hoshina, S., and Usuki, I. (1993) Zinc as modulater of oxygenation function and stabilizer of quaternary structure in earthworm hemoglobin. Biochim. Biophys. Acta 1203, 310-314
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 310-314
    • Ochiai, T.1    Hoshina, S.2    Usuki, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.