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Volumn 42, Issue 10, 2003, Pages 3096-3104

HU binding to bent DNA: A fluorescence resonance energy transfer and anisotropy study

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; ENERGY TRANSFER; FLUORESCENCE; PROTEINS;

EID: 0037452946     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0264014     Document Type: Article
Times cited : (45)

References (58)
  • 1
    • 0023413620 scopus 로고
    • Histonelike proteins of bacteria
    • Drlica, K., and Rouviere-Yaniv, J. (1987) Histonelike Proteins of Bacteria, Microbial. Rev. 51, 301-319.
    • (1987) Microbial. Rev. , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 2
    • 0343794843 scopus 로고
    • Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli
    • Rouviere-Yaniv, J., and Gros, F. (1975) Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 72, 3428-3432.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 3428-3432
    • Rouviere-Yaniv, J.1    Gros, F.2
  • 4
    • 0027729660 scopus 로고
    • Site-specific HU binding in the Mu transpososome: Conversion of a sequence-independent DNA-binding protein into a chemical nuclease
    • Lavoie, B. D., and Chaconas, G. (1993) Site-specific HU binding in the Mu transpososome: conversion of a sequence-independent DNA-binding protein into a chemical nuclease, Genes Dev. 7, 2510-2519.
    • (1993) Genes Dev. , vol.7 , pp. 2510-2519
    • Lavoie, B.D.1    Chaconas, G.2
  • 5
    • 0029973105 scopus 로고    scopus 로고
    • Anatomy of a flexer-DNA complex inside a higher-order transposition intermediate
    • Lavoie, B. D., Shaw, G. S., Millner, A., and Chaconas, G. (1996) Anatomy of a Flexer-DNA Complex inside a Higher-Order Transposition Intermediate, Cell 85, 761-771.
    • (1996) Cell , vol.85 , pp. 761-771
    • Lavoie, B.D.1    Shaw, G.S.2    Millner, A.3    Chaconas, G.4
  • 6
    • 0030928287 scopus 로고    scopus 로고
    • Repressor induced site-specific binding of HU for transcriptional regulation
    • Aki, T., and Adhya, S. (1997) Repressor induced site-specific binding of HU for transcriptional regulation, EMBO J. 16, 3666-3674.
    • (1997) EMBO J. , vol.16 , pp. 3666-3674
    • Aki, T.1    Adhya, S.2
  • 7
    • 0028043678 scopus 로고
    • Prokaryotic HU and eukaryotic HMG1: A kinked relationship
    • Bianchi, M. E. (1994) Prokaryotic HU and eukaryotic HMG1: a kinked relationship, Mol. Microbiol. 14, 1-5.
    • (1994) Mol. Microbiol. , vol.14 , pp. 1-5
    • Bianchi, M.E.1
  • 8
    • 0031052180 scopus 로고    scopus 로고
    • Making DNA do a U-turn: IHF and related proteins
    • Rice, P. A. (1997) Making DNA do a U-turn: IHF and related proteins, Curr. Opin. Struct. Biol. 7, 86-93.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 86-93
    • Rice, P.A.1
  • 10
    • 0028901705 scopus 로고
    • HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps
    • Castaing, B., Zelwer, C., Laval, J., and Boiteux, S. (1995) HU Protein of Escherichia coli Binds Specifically to DNA That Contains Single-strand Breaks or Gaps, J. Biol. Chem. 270, 10291-10296.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10291-10296
    • Castaing, B.1    Zelwer, C.2    Laval, J.3    Boiteux, S.4
  • 11
    • 0033214062 scopus 로고    scopus 로고
    • The binding motif recognized by HU on both nicked and cruciform DNA
    • Kamashev, D., Balandina, A., and Rouvière-Yaniv, J. (1999) The binding motif recognized by HU on both nicked and cruciform DNA, EMBO J. 18, 5434-5444.
    • (1999) EMBO J. , vol.18 , pp. 5434-5444
    • Kamashev, D.1    Balandina, A.2    Rouvière-Yaniv, J.3
  • 12
    • 0033515646 scopus 로고    scopus 로고
    • Differential binding of the Escherichia Coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA
    • Pinson, V., Takahashi, M., and Rouviere-Yaniv, J. (1999) Differential Binding of the Escherichia Coli HU, Homodimeric Forms and Heterodimeric Form to Linear, Gapped and Cruciform DNA, J. Mol. Biol. 287, 485-497.
    • (1999) J. Mol. Biol. , vol.287 , pp. 485-497
    • Pinson, V.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 13
    • 0034416406 scopus 로고    scopus 로고
    • The histone-like protein HU binds specifically to DNA recombination and repair intermediates
    • Kamashev, D., and Rouviere-Yaniv, J. (2000) The histone-like protein HU binds specifically to DNA recombination and repair intermediates, EMBO J. 19, 6527-6535.
    • (2000) EMBO J. , vol.19 , pp. 6527-6535
    • Kamashev, D.1    Rouviere-Yaniv, J.2
  • 14
    • 0033057518 scopus 로고    scopus 로고
    • Supercoiling-dependent site-specific binding of HU to naked Mu DNA
    • Kobryn, K., Lavoie, B. D., and Chaconas, G. (1999) Supercoiling-dependent Site-specific Binding of HU to Naked Mu DNA, J. Mol. Biol. 289, 777-784.
    • (1999) J. Mol. Biol. , vol.289 , pp. 777-784
    • Kobryn, K.1    Lavoie, B.D.2    Chaconas, G.3
  • 15
    • 0028136642 scopus 로고
    • DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA
    • Bonnefoy, E., Takahashi, M., and Rouviere-Yaniv, J. (1994) DNA-binding Parameters of the HU protein of Escherichia coli to Cruciform DNA, J. Mol. Biol. 242, 116-129.
    • (1994) J. Mol. Biol. , vol.242 , pp. 116-129
    • Bonnefoy, E.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 16
    • 0026019440 scopus 로고
    • HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments
    • Bonnefoy, E., and Rouviere-Yaniv, J. (1991) HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments, EMBO J. 10, 687-696.
    • (1991) EMBO J. , vol.10 , pp. 687-696
    • Bonnefoy, E.1    Rouviere-Yaniv, J.2
  • 17
    • 0027172958 scopus 로고
    • Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli
    • Tanaka, H., Goshima, N., Kohno, K., Kano, Y., and Imamoto, F. (1993) Properties of DNA-Binding of HU Heterotypic and Homotypic Dimers from Escherichia coli, J. Biochem. 113, 568-572.
    • (1993) J. Biochem. , vol.113 , pp. 568-572
    • Tanaka, H.1    Goshima, N.2    Kohno, K.3    Kano, Y.4    Imamoto, F.5
  • 18
    • 0029610588 scopus 로고
    • Characterization of the binding of HU and IHF, homologous histone-like proteins of Escherichia coli, to curved and uncurved DNA
    • Shimizu, M., Miyake, M., Kanke, F., Matsumoto, U., and Shindo, H. (1995) Characterization of the binding of HU and IHF, homologous histone-like proteins of Escherichia coli, to curved and uncurved DNA, Biochim. Biophys. Acta 1264, 330-336.
    • (1995) Biochim. Biophys. Acta , vol.1264 , pp. 330-336
    • Shimizu, M.1    Miyake, M.2    Kanke, F.3    Matsumoto, U.4    Shindo, H.5
  • 19
    • 0026687952 scopus 로고
    • Fluorescence resonance energy transfer and nucleic acids
    • Clegg, R. M. (1992) Fluorescence Resonance Energy Transfer and Nucleic Acids, Methods Enzymol. 211, 353-388.
    • (1992) Methods Enzymol. , vol.211 , pp. 353-388
    • Clegg, R.M.1
  • 20
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin, P. R. (1995) Fluorescence Resonance Energy Transfer, Methods Enzymol. 246, 300-334.
    • (1995) Methods Enzymol. , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 21
    • 0035312659 scopus 로고    scopus 로고
    • Recent advances in FRET: Distance determination in protein-DNA complexes
    • Hillisch, A., Lorenz, M., and Diekmann, S. (2001) Recent advances in FRET: distance determination in protein-DNA complexes, Curr. Opin. Struct. Biol. 11, 201-207.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 201-207
    • Hillisch, A.1    Lorenz, M.2    Diekmann, S.3
  • 22
    • 14244270749 scopus 로고    scopus 로고
    • Time-resolved fluorescence resonance transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes
    • Parkhurst, L. J., Parkhurst, K. M., Powell, R., Wu, J., and Williams, S. (2002) Time-resolved Fluorescence Resonance Transfer Studies of DNA Bending in Double-Stranded Oligonucleotides and in DNA-Protein Complexes, Biopolymers (Nucleic Acid Sciences) 61, 180-200.
    • (2002) Biopolymers (Nucleic Acid Sciences) , vol.61 , pp. 180-200
    • Parkhurst, L.J.1    Parkhurst, K.M.2    Powell, R.3    Wu, J.4    Williams, S.5
  • 23
    • 2442519939 scopus 로고    scopus 로고
    • Time-resolved fluorescence resonance energy transfer: A versatile tool for the analysis of nucleic acids
    • Klostermeier, D., and Millar, D. P. (2002) Time-Resolved Fluorescence Resonance Energy Transfer: A Versatile Tool for the Analysis of Nucleic Acids, Biopolymers 61, 159-179.
    • (2002) Biopolymers , vol.61 , pp. 159-179
    • Klostermeier, D.1    Millar, D.P.2
  • 24
    • 0041829746 scopus 로고    scopus 로고
    • DNA curvature in solution measured by fluorescence resonance energy transfer
    • Toth, K., Sauermann, V., and Langowski, J. (1998) DNA Curvature in Solution Measured by Fluorescence Resonance Energy Transfer, Biochemistry 37, 8173-8179.
    • (1998) Biochemistry , vol.37 , pp. 8173-8179
    • Toth, K.1    Sauermann, V.2    Langowski, J.3
  • 25
    • 0033485813 scopus 로고    scopus 로고
    • Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer
    • Lorenz, M., Hillisch, A., Goodman, S. D., and Diekmann, S. (1999) Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer, Nucl. Acids Res. 27, 4619-4625.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 4619-4625
    • Lorenz, M.1    Hillisch, A.2    Goodman, S.D.3    Diekmann, S.4
  • 26
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex: A protein-induced DNA U-turn
    • Rice, P. A., Yang, S.-W., Mizuuchi, K., and Nash, H. A. (1996) Crystal Structure of an IHF-DNA Complex: A Protein-Induced DNA U-Turn, Cell 87, 1295-1306.
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.-W.2    Mizuuchi, K.3    Nash, H.A.4
  • 27
    • 0035957055 scopus 로고    scopus 로고
    • HU binding to DNA: Evidence for multiple complexes and DNA bending
    • Wojtuszewski, K., Hawkins, M. E., Cole, J. L., and Mukerji, I. (2001) HU Binding to DNA: Evidence for Multiple Complexes and DNA Bending, Biochemistry 40, 2588-2598.
    • (2001) Biochemistry , vol.40 , pp. 2588-2598
    • Wojtuszewski, K.1    Hawkins, M.E.2    Cole, J.L.3    Mukerji, I.4
  • 29
    • 0027216519 scopus 로고
    • The nonspecific DNA-binding and bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structure
    • Paull, T., Haykinson, M., and Johnson, R. (1993) The nonspecific DNA-binding and bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structure, Genes Dev. 7, 1521-1534.
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.1    Haykinson, M.2    Johnson, R.3
  • 30
    • 0022527052 scopus 로고
    • Sequence-directed curvature of DNA
    • Hagerman, P. J. (1986) Sequence-directed curvature of DNA, Nature 321, 449.
    • (1986) Nature , vol.321 , pp. 449
    • Hagerman, P.J.1
  • 31
    • 0026081533 scopus 로고
    • A spectroscopic and calorimetric study of the melting behaviors of a 'bent' and 'normal' DNA duplex: [d(GA4T4C)]2 versus [d(GT4A4C)]2
    • Park, Y.-W., and Breslauer, K. J. (1991) A Spectroscopic and Calorimetric Study of the Melting Behaviors of a 'bent' and 'normal' DNA Duplex: [d(GA4T4C)]2 versus [d(GT4A4C)]2, Proc. Natl. Acad. Sci. U.S.A. 88, 1551-1555.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1551-1555
    • Park, Y.-W.1    Breslauer, K.J.2
  • 33
    • 77956988666 scopus 로고
    • DNA-cellulose chromatography
    • Alberts, B., and Herrick, G. (1971) DNA-Cellulose Chromatography, Methods Enzymol. 21, 198-217.
    • (1971) Methods Enzymol. , vol.21 , pp. 198-217
    • Alberts, B.1    Herrick, G.2
  • 38
    • 33847682952 scopus 로고
    • Correction of fluorescence spectra and measurement of fluorescence quantum efficiency
    • Parker, C. A., and Rees, W. T. (1960) Correction of Fluorescence Spectra and Measurement of Fluorescence Quantum Efficiency, Analyst 85, 587-600.
    • (1960) Analyst , vol.85 , pp. 587-600
    • Parker, C.A.1    Rees, W.T.2
  • 39
    • 0027976675 scopus 로고
    • The solution structure of the four-way DNA junction at low-salt conditions: A fluorescence resonance energy transfer analysis
    • Clegg, R. M., Murchie, A. I., and Lilley, D. M. (1994) The solution structure of the four-way DNA junction at low-salt conditions: a fluorescence resonance energy transfer analysis, Biophys J. 66, 99-109.
    • (1994) Biophys J. , vol.66 , pp. 99-109
    • Clegg, R.M.1    Murchie, A.I.2    Lilley, D.M.3
  • 40
    • 0028934572 scopus 로고
    • Fluorescence anisotropy applied to biomolecular interactions
    • Jameson, D. M., and Sawyer, W. H. (1995) Fluorescence Anisotropy Applied to Biomolecular Interactions, Methods Enzymol. 246, 283-300.
    • (1995) Methods Enzymol. , vol.246 , pp. 283-300
    • Jameson, D.M.1    Sawyer, W.H.2
  • 41
    • 0025261344 scopus 로고
    • Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction
    • Heyduk, T., and Lee, J. C. (1990) Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction, Proc. Natl. Acad. Sci. U.S.A. 87, 1744-1748.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 1744-1748
    • Heyduk, T.1    Lee, J.C.2
  • 42
    • 0030337874 scopus 로고    scopus 로고
    • Fluorescence anisotropy: Rapid, quanititative assay for protein-DNA and protein-protein interaction
    • Heyduk, T., Ma, Y., Tang, H., and Ebright, R. H. (1996) Fluorescence Anisotropy: Rapid, Quanititative Assay for Protein- DNA and Protein-Protein Interaction, Methods Enzymol. 274, 492-503.
    • (1996) Methods Enzymol. , vol.274 , pp. 492-503
    • Heyduk, T.1    Ma, Y.2    Tang, H.3    Ebright, R.H.4
  • 43
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence Methods for studying equilibrium macromolecule-ligand interactions
    • Eftink, M. R. (1997) Fluorescence Methods for Studying Equilibrium Macromolecule-Ligand Interactions, Methods Enzymol. 278, 221-258.
    • (1997) Methods Enzymol. , vol.278 , pp. 221-258
    • Eftink, M.R.1
  • 44
    • 0029118594 scopus 로고
    • Incorporation of a fluorescent guanosine analogue into oligonucleotides and its application to a real time assay for the HIV-1 integrase 3′-processing reaction
    • Hawkins, M. E., Pfleiderer, W., Mazumder, A., Pommier, Y. G., and Balis, F. M. (1995) Incorporation of a fluorescent guanosine analogue into oligonucleotides and its application to a real time assay for the HIV-1 integrase 3′-processing reaction, Nucl. Acids Res. 23, 2872-2880.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2872-2880
    • Hawkins, M.E.1    Pfleiderer, W.2    Mazumder, A.3    Pommier, Y.G.4    Balis, F.M.5
  • 45
    • 0031023096 scopus 로고    scopus 로고
    • Fluorescence properties of pteridine nucleoside analogues as monomers and incorporated into oligonucleotides
    • Hawkins, M. E., Pfleiderer, W., Balis, F. M., Porter, D., and Knutson, J. R. (1997) Fluorescence Properties of Pteridine Nucleoside Analogues as Monomers and Incorporated into Oligonucleotides, Anal. Biochem. 244, 86-95.
    • (1997) Anal. Biochem. , vol.244 , pp. 86-95
    • Hawkins, M.E.1    Pfleiderer, W.2    Balis, F.M.3    Porter, D.4    Knutson, J.R.5
  • 46
    • 0036567249 scopus 로고    scopus 로고
    • Effect of primary and secondary structure of oligodeoxyribonucleotides on the fluorescent properties of conjugated dyes
    • Nazarenko, I., Pires, R., Lowe, B., Obaidy, M., and Rashtchian, A. (2002) Effect of primary and secondary structure of oligodeoxyribonucleotides on the fluorescent properties of conjugated dyes, Nucl. Acids Res. 30, 2089-2195.
    • (2002) Nucl. Acids Res. , vol.30 , pp. 2089-2195
    • Nazarenko, I.1    Pires, R.2    Lowe, B.3    Obaidy, M.4    Rashtchian, A.5
  • 47
    • 0034732989 scopus 로고    scopus 로고
    • Location of cyanine-3 on double-stranded DNA: Importance for fluorescence resonance energy transfer studies
    • Norman, D. G., Grainger, R. J., Uhrin, D., and Lilley, D. M. J. (2000) Location of Cyanine-3 on Double-Stranded DNA: Importance for Fluorescence Resonance Energy Transfer Studies, Biochemistry 39, 6317-6324.
    • (2000) Biochemistry , vol.39 , pp. 6317-6324
    • Norman, D.G.1    Grainger, R.J.2    Uhrin, D.3    Lilley, D.M.J.4
  • 48
    • 0034612993 scopus 로고    scopus 로고
    • Fluorescence energy transfer analysis of DNA structures containing several bulges and their interaction with CAP
    • Stuhmeier, F., Hillisch, A., Clegg, R. M., and Diekmann, S. (2000) Fluorescence Energy Transfer Analysis of DNA Structures Containing Several Bulges and their Interaction with CAP, J. Mol. Biol. 302, 1081-1100.
    • (2000) J. Mol. Biol. , vol.302 , pp. 1081-1100
    • Stuhmeier, F.1    Hillisch, A.2    Clegg, R.M.3    Diekmann, S.4
  • 49
    • 0037129935 scopus 로고    scopus 로고
    • DNA bending by bZIP charge variants: A unified study using electrophoretic phasing and fluorescence resonance energy transfer
    • Hardwidge, P. R., Wu, J., Williams, S. L., Parkhurst, K. M., Parkhurst, L. J., and Maher, L. J. (2002) DNA Bending by bZIP Charge Variants: A Unified Study Using Electrophoretic Phasing and Fluorescence Resonance Energy Transfer, Biochemistry 41, 7732-7742.
    • (2002) Biochemistry , vol.41 , pp. 7732-7742
    • Hardwidge, P.R.1    Wu, J.2    Williams, S.L.3    Parkhurst, K.M.4    Parkhurst, L.J.5    Maher, L.J.6
  • 50
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to λ sitespecific recombination complexes
    • Thompson, J. F., and Landy, A. (1988) Empirical estimation of protein-induced DNA bending angles: applications to λ sitespecific recombination complexes, Nucl. Acids Res. 16, 9687-9705.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 51
    • 0035805572 scopus 로고    scopus 로고
    • DNA sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes
    • Wu, J., Parkhurst, K. M., Powell, R. M., and Parkhurst, L. J. (2001) DNA Sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes, J. Biol. Chem. 276, 14623-14627.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14623-14627
    • Wu, J.1    Parkhurst, K.M.2    Powell, R.M.3    Parkhurst, L.J.4
  • 52
    • 0023846051 scopus 로고
    • Structural details of an adenine tract that does not cause DNA to bend
    • Burkhoff, A. M., and Tullius, T. D. (1988) Structural Details of an Adenine Tract That Does Not Cause DNA to Bend, Nature 331, 455-457.
    • (1988) Nature , vol.331 , pp. 455-457
    • Burkhoff, A.M.1    Tullius, T.D.2
  • 53
    • 0022914418 scopus 로고
    • Principles of sequence-dependent flexure of DNA
    • Calladine, C. R., and Drew, H. R. (1986) Principles of sequence-dependent flexure of DNA, J. Mol. Biol. 192, 907-918.
    • (1986) J. Mol. Biol. , vol.192 , pp. 907-918
    • Calladine, C.R.1    Drew, H.R.2
  • 55
    • 0022456498 scopus 로고
    • Bending and flexibility of kinetoplast DNA
    • Levene, S. D., Wu, H. M., and Crothers, D. M. (1986) Bending and flexibility of kinetoplast DNA, Biochemistry 25, 3988-3995.
    • (1986) Biochemistry , vol.25 , pp. 3988-3995
    • Levene, S.D.1    Wu, H.M.2    Crothers, D.M.3
  • 56
    • 0023513912 scopus 로고
    • The structure of an oligo (dA).oligo (dT) tract and its biological implications
    • Nelson, H. C. M., Finch, J. T., Luisi, B. F., and Klug, A. (1987) The Structure of an oligo (dA).oligo (dT) Tract and its Biological Implications, Nature 330, 221-226.
    • (1987) Nature , vol.330 , pp. 221-226
    • Nelson, H.C.M.1    Finch, J.T.2    Luisi, B.F.3    Klug, A.4


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