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Volumn 385, Issue 2, 2009, Pages 628-641

Unfolding Thermodynamics of the Δ-Domain in the Prohead I Subunit of Phage HK97: Determination by Factor Analysis of Raman Spectra

Author keywords

factor analysis; prohead I; Raman spectroscopy; thermostability; domain

Indexed keywords

PEPTIDE; PHENYLALANINE; PROHEAD 1 PROTEIN; PROTEIN PRECURSOR; PROTEIN SUBUNIT; TRYPTOPHAN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 58149092719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.046     Document Type: Article
Times cited : (9)

References (45)
  • 1
    • 0015329979 scopus 로고
    • Infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope: T4 head morphogenesis
    • Simon L.D. Infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope: T4 head morphogenesis. Proc. Natl Acad. Sci. USA 69 (1972) 907-911
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 907-911
    • Simon, L.D.1
  • 2
    • 0029908793 scopus 로고    scopus 로고
    • The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
    • Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., Homa F.L., Thomsen D.R., and Steven A.C. The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 263 (1996) 447-462
    • (1996) J. Mol. Biol. , vol.263 , pp. 447-462
    • Trus, B.L.1    Booy, F.P.2    Newcomb, W.W.3    Brown, J.C.4    Homa, F.L.5    Thomsen, D.R.6    Steven, A.C.7
  • 3
    • 0030872369 scopus 로고    scopus 로고
    • Intermediates in the assembly pathway of the double-stranded RNA virus φ6
    • Butcher S.J., Dokland T., Ojala P.M., Bamford D.H., and Fuller S.D. Intermediates in the assembly pathway of the double-stranded RNA virus φ6. EMBO J. 16 (1997) 4477-4487
    • (1997) EMBO J. , vol.16 , pp. 4477-4487
    • Butcher, S.J.1    Dokland, T.2    Ojala, P.M.3    Bamford, D.H.4    Fuller, S.D.5
  • 4
    • 0002608842 scopus 로고    scopus 로고
    • The procapsid to capsid transition in double-stranded DNA bacteriophages
    • Chiu W., Burnett R.M., and Garcea R. (Eds), Oxford University Press, New York
    • King J., and Chiu W. The procapsid to capsid transition in double-stranded DNA bacteriophages. In: Chiu W., Burnett R.M., and Garcea R. (Eds). Structural Biology of Viruses (1997), Oxford University Press, New York 288-311
    • (1997) Structural Biology of Viruses , pp. 288-311
    • King, J.1    Chiu, W.2
  • 6
    • 0034625320 scopus 로고    scopus 로고
    • Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω virus (NωV)
    • Canady M.A., Tihova M., Hanzlik T.N., Johnson J.E., and Yeager M. Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω virus (NωV). J. Mol. Biol. 299 (2000) 573-584
    • (2000) J. Mol. Biol. , vol.299 , pp. 573-584
    • Canady, M.A.1    Tihova, M.2    Hanzlik, T.N.3    Johnson, J.E.4    Yeager, M.5
  • 9
    • 33846262040 scopus 로고    scopus 로고
    • Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM
    • Gan L., Speir J.A., Conway J.F., Lander G., Cheng N., Firek B.A., et al. Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM. Structure 14 (2006) 1655-1665
    • (2006) Structure , vol.14 , pp. 1655-1665
    • Gan, L.1    Speir, J.A.2    Conway, J.F.3    Lander, G.4    Cheng, N.5    Firek, B.A.6
  • 10
    • 32544460955 scopus 로고    scopus 로고
    • Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallography
    • Wikoff W.R., Conway J.F., Tang J., Lee K.K., Gan L., Cheng N., et al. Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallography. J. Struct. Biol. 153 (2006) 300-306
    • (2006) J. Struct. Biol. , vol.153 , pp. 300-306
    • Wikoff, W.R.1    Conway, J.F.2    Tang, J.3    Lee, K.K.4    Gan, L.5    Cheng, N.6
  • 11
    • 0015897898 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22: II. Morphogenetic pathway
    • King J., Lenk E.V., and Botstein D. Mechanism of head assembly and DNA encapsulation in Salmonella phage P22: II. Morphogenetic pathway. J. Mol. Biol. 80 (1973) 697-731
    • (1973) J. Mol. Biol. , vol.80 , pp. 697-731
    • King, J.1    Lenk, E.V.2    Botstein, D.3
  • 12
    • 0017892996 scopus 로고
    • Adenovirus type 2 assembly analyzed by reversible cross-linking of labile intermediates
    • D'Halluin J.C., Martin G.R., Torpier G., and Boulanger P.A. Adenovirus type 2 assembly analyzed by reversible cross-linking of labile intermediates. J. Virol. 26 (1978) 357-363
    • (1978) J. Virol. , vol.26 , pp. 357-363
    • D'Halluin, J.C.1    Martin, G.R.2    Torpier, G.3    Boulanger, P.A.4
  • 13
    • 0023986450 scopus 로고
    • Characterization of intranuclear capsids made by ts morphogenic mutants of HSV-1
    • Sherman G., and Bachenheimer S.L. Characterization of intranuclear capsids made by ts morphogenic mutants of HSV-1. Virology 163 (1988) 471-480
    • (1988) Virology , vol.163 , pp. 471-480
    • Sherman, G.1    Bachenheimer, S.L.2
  • 14
    • 0033039372 scopus 로고    scopus 로고
    • Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids
    • Thuman-Commike P.A., Greene B., Malinski J.A., Burbea M., McGough A., Chiu W., and Prevelige Jr. P.E. Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids. Biophys. J. 76 (1999) 3267-3277
    • (1999) Biophys. J. , vol.76 , pp. 3267-3277
    • Thuman-Commike, P.A.1    Greene, B.2    Malinski, J.A.3    Burbea, M.4    McGough, A.5    Chiu, W.6    Prevelige Jr., P.E.7
  • 15
    • 33846847658 scopus 로고    scopus 로고
    • Molecular dissection of φ29 scaffolding protein function in an in vitro assembly system
    • Fu C.Y., Morais M.C., Battisti A.J., Rossmann M.G., and Prevelige Jr. P.E. Molecular dissection of φ29 scaffolding protein function in an in vitro assembly system. J. Mol. Biol. 366 (2007) 1161-1173
    • (2007) J. Mol. Biol. , vol.366 , pp. 1161-1173
    • Fu, C.Y.1    Morais, M.C.2    Battisti, A.J.3    Rossmann, M.G.4    Prevelige Jr., P.E.5
  • 16
    • 0042326090 scopus 로고    scopus 로고
    • Mechanism of scaffolding-assisted viral assembly
    • Fane B.A., and Prevelige Jr. P.E. Mechanism of scaffolding-assisted viral assembly. Adv. Protein Chem. 64 (2003) 259-299
    • (2003) Adv. Protein Chem. , vol.64 , pp. 259-299
    • Fane, B.A.1    Prevelige Jr., P.E.2
  • 18
    • 2442544585 scopus 로고    scopus 로고
    • Domain structures and roles in bacteriophage HK97 capsid assembly and maturation
    • Benevides J.M., Bondre P., Duda R.L., Hendrix R.W., and Thomas Jr. G.J. Domain structures and roles in bacteriophage HK97 capsid assembly and maturation. Biochemistry 43 (2004) 5428-5436
    • (2004) Biochemistry , vol.43 , pp. 5428-5436
    • Benevides, J.M.1    Bondre, P.2    Duda, R.L.3    Hendrix, R.W.4    Thomas Jr., G.J.5
  • 19
    • 33750844822 scopus 로고    scopus 로고
    • A free energy cascade with locks drives assembly and maturation of bacteriophage HK97 capsid
    • Ross P.D., Conway J.F., Cheng N., Dierkes L., Firek B.A., Hendrix R.W., et al. A free energy cascade with locks drives assembly and maturation of bacteriophage HK97 capsid. J. Mol. Biol. 364 (2006) 512-525
    • (2006) J. Mol. Biol. , vol.364 , pp. 512-525
    • Ross, P.D.1    Conway, J.F.2    Cheng, N.3    Dierkes, L.4    Firek, B.A.5    Hendrix, R.W.6
  • 20
    • 17044437232 scopus 로고    scopus 로고
    • Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization
    • Ross P.D., Cheng N., Conway J.F., Firek B.A., Hendrix R.W., Duda R.L., and Steven A.C. Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization. EMBO J. 24 (2005) 1352-1363
    • (2005) EMBO J. , vol.24 , pp. 1352-1363
    • Ross, P.D.1    Cheng, N.2    Conway, J.F.3    Firek, B.A.4    Hendrix, R.W.5    Duda, R.L.6    Steven, A.C.7
  • 21
    • 34248384340 scopus 로고    scopus 로고
    • A thermally induced phase transition in a viral capsid transforms the hexamers, leaving the pentamers unchanged
    • Conway J.F., Cheng N., Ross P.D., Hendrix R.W., Duda R.L., and Steven A.C. A thermally induced phase transition in a viral capsid transforms the hexamers, leaving the pentamers unchanged. J. Struct. Biol. 158 (2007) 224-232
    • (2007) J. Struct. Biol. , vol.158 , pp. 224-232
    • Conway, J.F.1    Cheng, N.2    Ross, P.D.3    Hendrix, R.W.4    Duda, R.L.5    Steven, A.C.6
  • 22
    • 0029864052 scopus 로고    scopus 로고
    • Structural transitions in the scaffolding and coat proteins of P22 virus during assembly and disassembly
    • Tuma R., Prevelige Jr. P.E., and Thomas Jr. G.J. Structural transitions in the scaffolding and coat proteins of P22 virus during assembly and disassembly. Biochemistry 35 (1996) 4619-4627
    • (1996) Biochemistry , vol.35 , pp. 4619-4627
    • Tuma, R.1    Prevelige Jr., P.E.2    Thomas Jr., G.J.3
  • 23
    • 0032493694 scopus 로고    scopus 로고
    • A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein
    • Tuma R., Parker M.H., Weigele P., Sampson L., Sun Y., Krishna N.R., et al. A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein. J. Mol. Biol. 281 (1998) 81-94
    • (1998) J. Mol. Biol. , vol.281 , pp. 81-94
    • Tuma, R.1    Parker, M.H.2    Weigele, P.3    Sampson, L.4    Sun, Y.5    Krishna, N.R.6
  • 25
    • 0017294711 scopus 로고
    • Accessible area, packing volumes and interaction surfaces of globular proteins
    • Teller D.C. Accessible area, packing volumes and interaction surfaces of globular proteins. Nature 260 (1976) 729-731
    • (1976) Nature , vol.260 , pp. 729-731
    • Teller, D.C.1
  • 27
    • 12344271844 scopus 로고    scopus 로고
    • Raman spectroscopy of proteins
    • Coligan J.E., Dunn B.M., Ploegh H.L., Speicher D.W., and Wingfield P.T. (Eds), John Wiley and Sons, New York
    • Benevides J.M., Overman S.A., and Thomas Jr. G.J. Raman spectroscopy of proteins. In: Coligan J.E., Dunn B.M., Ploegh H.L., Speicher D.W., and Wingfield P.T. (Eds). Current Protocols in Protein Science (2005), John Wiley and Sons, New York 17.8.1-17.8.35
    • (2005) Current Protocols in Protein Science
    • Benevides, J.M.1    Overman, S.A.2    Thomas Jr., G.J.3
  • 28
    • 84986759513 scopus 로고
    • Determination of the secondary structure of proteins from the Raman amide I band: the reference intensity profiles method
    • Berjot M., Marx J., and Alix A.J.P. Determination of the secondary structure of proteins from the Raman amide I band: the reference intensity profiles method. J. Raman Spectrosc. 18 (1987) 289-300
    • (1987) J. Raman Spectrosc. , vol.18 , pp. 289-300
    • Berjot, M.1    Marx, J.2    Alix, A.J.P.3
  • 29
    • 0031406242 scopus 로고    scopus 로고
    • Mechanisms of virus assembly probed by Raman spectroscopy: the icosahedral bacteriophage P22
    • Tuma R., and Thomas Jr. G.J. Mechanisms of virus assembly probed by Raman spectroscopy: the icosahedral bacteriophage P22. Biophys. Chem. 68 (1997) 17-31
    • (1997) Biophys. Chem. , vol.68 , pp. 17-31
    • Tuma, R.1    Thomas Jr., G.J.2
  • 30
    • 0033616633 scopus 로고    scopus 로고
    • Raman markers of nonaromatic side chains in an α-helix assembly: Ala, Asp, Glu, Gly, Ile, Leu, Lys, Ser, and Val residues of phage fd subunits
    • Overman S.A., and Thomas Jr. G.J. Raman markers of nonaromatic side chains in an α-helix assembly: Ala, Asp, Glu, Gly, Ile, Leu, Lys, Ser, and Val residues of phage fd subunits. Biochemistry 38 (1999) 4018-4027
    • (1999) Biochemistry , vol.38 , pp. 4018-4027
    • Overman, S.A.1    Thomas Jr., G.J.2
  • 31
    • 0028999261 scopus 로고
    • Raman spectroscopy of the filamentous virus Ff (fd, fl, M13): structural interpretation for coat protein aromatics
    • Overman S.A., and Thomas Jr. G.J. Raman spectroscopy of the filamentous virus Ff (fd, fl, M13): structural interpretation for coat protein aromatics. Biochemistry 34 (1995) 5440-5451
    • (1995) Biochemistry , vol.34 , pp. 5440-5451
    • Overman, S.A.1    Thomas Jr., G.J.2
  • 32
    • 0021095333 scopus 로고
    • Structure similarity, difference and variability in the filamentous viruses fd, If1, IKe, Pf1 and Xf. Investigation by laser Raman spectroscopy
    • Thomas Jr. G.J., Prescott B., and Day L.A. Structure similarity, difference and variability in the filamentous viruses fd, If1, IKe, Pf1 and Xf. Investigation by laser Raman spectroscopy. J. Mol. Biol. 165 (1983) 321-356
    • (1983) J. Mol. Biol. , vol.165 , pp. 321-356
    • Thomas Jr., G.J.1    Prescott, B.2    Day, L.A.3
  • 33
    • 0023671571 scopus 로고
    • Ultraviolet resonance Raman spectroscopy as a probe of protein structure in the fd virus
    • Grygon C.A., Perno J.R., Fodor S.P., and Spiro T.G. Ultraviolet resonance Raman spectroscopy as a probe of protein structure in the fd virus. Biotechniques 6 (1988) 50-55
    • (1988) Biotechniques , vol.6 , pp. 50-55
    • Grygon, C.A.1    Perno, J.R.2    Fodor, S.P.3    Spiro, T.G.4
  • 34
    • 14344262928 scopus 로고    scopus 로고
    • Structural characterization of the filamentous bacteriophage PH75 from Thermus thermophilus by Raman and UV-resonance Raman spectroscopy
    • Overman S.A., Bondre P., Maiti N.C., and Thomas Jr. G.J. Structural characterization of the filamentous bacteriophage PH75 from Thermus thermophilus by Raman and UV-resonance Raman spectroscopy. Biochemistry 44 (2005) 3091-3100
    • (2005) Biochemistry , vol.44 , pp. 3091-3100
    • Overman, S.A.1    Bondre, P.2    Maiti, N.C.3    Thomas Jr., G.J.4
  • 35
    • 18744429919 scopus 로고    scopus 로고
    • Bacteriophage P22 scaffolding protein forms oligomers in solution
    • Parker M.H., Stafford III W.F., and Prevelige Jr. P.E. Bacteriophage P22 scaffolding protein forms oligomers in solution. J. Mol. Biol. 268 (1997) 655-665
    • (1997) J. Mol. Biol. , vol.268 , pp. 655-665
    • Parker, M.H.1    Stafford III, W.F.2    Prevelige Jr., P.E.3
  • 36
    • 17444370140 scopus 로고    scopus 로고
    • Molecular genetics of bacteriophage P22 scaffolding protein's functional domains
    • Weigele P.R., Sampson L., Winn-Stapley D., and Casjens S.R. Molecular genetics of bacteriophage P22 scaffolding protein's functional domains. J. Mol. Biol. 348 (2005) 831-844
    • (2005) J. Mol. Biol. , vol.348 , pp. 831-844
    • Weigele, P.R.1    Sampson, L.2    Winn-Stapley, D.3    Casjens, S.R.4
  • 37
    • 0028927348 scopus 로고
    • Genetic basis of bacteriophage HK97 prohead assembly
    • Duda R.L., Martincic K., and Hendrix R.W. Genetic basis of bacteriophage HK97 prohead assembly. J. Mol. Biol. 247 (1995) 636-647
    • (1995) J. Mol. Biol. , vol.247 , pp. 636-647
    • Duda, R.L.1    Martincic, K.2    Hendrix, R.W.3
  • 39
    • 0037920996 scopus 로고    scopus 로고
    • Thermodynamics of protein folding and stability
    • Allen G. (Ed), JAI Press, Inc.
    • Cooper A. Thermodynamics of protein folding and stability. In: Allen G. (Ed). Protein: A Comprehensive Treatise (1999), JAI Press, Inc. 217-270
    • (1999) Protein: A Comprehensive Treatise , pp. 217-270
    • Cooper, A.1
  • 40
    • 0001144723 scopus 로고    scopus 로고
    • Temperature dependence of the Raman spectrum of DNA: I. Raman signatures of premelting and melting transitions of poly(dA-dT)·poly(dA-dT)
    • Movileanu L., Benevides J.M., and Thomas G.J. Temperature dependence of the Raman spectrum of DNA: I. Raman signatures of premelting and melting transitions of poly(dA-dT)·poly(dA-dT). J. Raman Spectrosc. 30 (1999) 637-649
    • (1999) J. Raman Spectrosc. , vol.30 , pp. 637-649
    • Movileanu, L.1    Benevides, J.M.2    Thomas, G.J.3
  • 42
    • 0003287523 scopus 로고    scopus 로고
    • Raman spectroscopic study of triplex-like complexes of polyuridylic acid with the isopolar, non-isosteric phosphonate analogues of diadenosine monophosphate
    • Hanus J., Chmelova K., Stepanek J., Turpin P.-Y., Bok J., Rosenberg I., and Tocik Z. Raman spectroscopic study of triplex-like complexes of polyuridylic acid with the isopolar, non-isosteric phosphonate analogues of diadenosine monophosphate. J. Raman Spectrosc. 30 (1999) 667-676
    • (1999) J. Raman Spectrosc. , vol.30 , pp. 667-676
    • Hanus, J.1    Chmelova, K.2    Stepanek, J.3    Turpin, P.-Y.4    Bok, J.5    Rosenberg, I.6    Tocik, Z.7
  • 43
    • 2442650251 scopus 로고    scopus 로고
    • Structural compatibility of novel nucleotide modifications with shortened linkages designed for antigene/antisense therapy
    • Hanus J., Nemecek D., Stepanek J., and Turpin P.-Y. Structural compatibility of novel nucleotide modifications with shortened linkages designed for antigene/antisense therapy. J. Raman Spectrosc. 35 (2004) 418-425
    • (2004) J. Raman Spectrosc. , vol.35 , pp. 418-425
    • Hanus, J.1    Nemecek, D.2    Stepanek, J.3    Turpin, P.-Y.4
  • 44
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 45
    • 1842481270 scopus 로고    scopus 로고
    • Analysis of heterogeneous interactions
    • Cole J.L. Analysis of heterogeneous interactions. Methods Enzymol. 384 (2004) 212-232
    • (2004) Methods Enzymol. , vol.384 , pp. 212-232
    • Cole, J.L.1


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