메뉴 건너뛰기




Volumn 277, Issue 1, 1998, Pages 1-11

Homologous DNA pairing domain peptides of RecA protein: Intrinsic propensity to form β-structures and filaments

Author keywords

Coil to transition; DNA binding peptides; DNA protein interaction; Peptide CD; RecA protein

Indexed keywords

AMINO ACID; AROMATIC AMINO ACID; DODECYL SULFATE SODIUM; DOUBLE STRANDED DNA; RECA PROTEIN; SINGLE STRANDED DNA;

EID: 0032549672     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1591     Document Type: Article
Times cited : (23)

References (31)
  • 3
    • 0027243084 scopus 로고
    • Parallel DNA triplexes, homologous recombination, and other homology-dependent DNA interactions
    • Camerini-Otero R.D., Hsieh P. Parallel DNA triplexes, homologous recombination, and other homology-dependent DNA interactions. Cell. 73:1993;217-223
    • (1993) Cell , vol.73 , pp. 217-223
    • Camerini-Otero, R.D.1    Hsieh, P.2
  • 4
    • 0029174547 scopus 로고
    • Homologous recombination proteins in prokaryotes and eukaryotes
    • Camerini-Otero R.D., Hsieh P. Homologous recombination proteins in prokaryotes and eukaryotes. Annu. Rev. Genet. 29:1995;509-552
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 509-552
    • Camerini-Otero, R.D.1    Hsieh, P.2
  • 5
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Advan. Enzymol. 47:1978;45-148
    • (1978) Advan. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 6
    • 0020475459 scopus 로고
    • Characterization of complexes between RecA protein and duplex DNA by electron microscopy
    • DiCapua E., Engel A., Stasiak A., Koller T. Characterization of complexes between RecA protein and duplex DNA by electron microscopy. J. Mol. Biol. 157:1982;87-103
    • (1982) J. Mol. Biol. , vol.157 , pp. 87-103
    • Dicapua, E.1    Engel, A.2    Stasiak, A.3    Koller, T.4
  • 7
    • 0023008741 scopus 로고
    • Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-γ-S or ATP
    • Egelman E.H., Stasiak A. Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-γ-S or ATP. J. Mol. Biol. 191:1986;677-697
    • (1986) J. Mol. Biol. , vol.191 , pp. 677-697
    • Egelman, E.H.1    Stasiak, A.2
  • 8
    • 0028867292 scopus 로고
    • The identification of the single-stranded binding domain of the Escherichia coli RecA protein
    • Gardner R.V., Voloshin O.N., Camerini-Otero R.D. The identification of the single-stranded binding domain of the Escherichia coli RecA protein. Eur. J. Biochem. 233:1995;419-425
    • (1995) Eur. J. Biochem. , vol.233 , pp. 419-425
    • Gardner, R.V.1    Voloshin, O.N.2    Camerini-Otero, R.D.3
  • 9
    • 0028716614 scopus 로고
    • Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators
    • Grishina I.B., Woody R.W. Contributions of tryptophan side chains to the circular dichroism of globular proteins Exciton couplets and coupled oscillators. Faraday Discuss. 99:1994;245-262
    • (1994) Faraday Discuss. , vol.99 , pp. 245-262
    • Grishina, I.B.1    Woody, R.W.2
  • 10
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
    • Hilbich C., Kisters-Woike B., Reed J., Masters C.L., Beyreuther K. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J. Mol. Biol. 218:1991;149-163
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 11
    • 0026740399 scopus 로고
    • The synapsis event in the homologous pairing of DNAs: RecA recognizes and pairs less than one helical repeat of DNA
    • Hsieh P., Camerini-Otero C.S., Camerini-Otero R.D. The synapsis event in the homologous pairing of DNAs RecA recognizes and pairs less than one helical repeat of DNA. Proc. Natl Acad. Sci. USA. 89:1992;6492-6496
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6492-6496
    • Hsieh, P.1    Camerini-Otero, C.S.2    Camerini-Otero, R.D.3
  • 12
    • 0027411181 scopus 로고
    • Thermodynamic β-sheet propensities measured using a zinc-finger host peptide
    • Kim C.A., Berg J.M. Thermodynamic β-sheet propensities measured using a zinc-finger host peptide. Nature. 362:1993;267-270
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 13
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation
    • Kirschner D., Abraham C., Selkoe D. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl Acad. Sci. USA. 83:1986;6953-6957
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6953-6957
    • Kirschner, D.1    Abraham, C.2    Selkoe, D.3
  • 15
    • 0028934071 scopus 로고
    • Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity
    • Maenaka K., Matsushuima M., Song H., Sunada F., Watanabe K., Kumagai I. Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity. J. Mol. Biol. 247:1995;281-293
    • (1995) J. Mol. Biol. , vol.247 , pp. 281-293
    • Maenaka, K.1    Matsushuima, M.2    Song, H.3    Sunada, F.4    Watanabe, K.5    Kumagai, I.6
  • 16
    • 0029620927 scopus 로고
    • Photocross-links between single-stranded DNA and Escherichia coli RecA protein map to loops L1 (amino acid residues 157-164) and L2 (amino acid residues 195-209)
    • Malkov V.A., Camerini-Otero R.D. Photocross-links between single-stranded DNA and Escherichia coli RecA protein map to loops L1 (amino acid residues 157-164) and L2 (amino acid residues 195-209). J. Biol. Chem. 270:1995;20230-20233
    • (1995) J. Biol. Chem. , vol.270 , pp. 20230-20233
    • Malkov, V.A.1    Camerini-Otero, R.D.2
  • 17
    • 0029569115 scopus 로고
    • The central aromatic residue in loop L2 of RecA interacts with DNA: Quenching of the fluorescence of a tryptophan reporter inserted in L2 upon binding to DNA
    • Maraboeuf F., Voloshin O.N., Camerini-Otero R.D., Takahashi M. The central aromatic residue in loop L2 of RecA interacts with DNA quenching of the fluorescence of a tryptophan reporter inserted in L2 upon binding to DNA. J. Biol. Chem. 270:1995;30927-30932
    • (1995) J. Biol. Chem. , vol.270 , pp. 30927-30932
    • Maraboeuf, F.1    Voloshin, O.N.2    Camerini-Otero, R.D.3    Takahashi, M.4
  • 18
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor D.L. Jr, Kim P.S. Measurement of the β-sheet-forming propensities of amino acids. Nature. 367:1994;660-663
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor Jr., D.L.1    Kim, P.S.2
  • 19
    • 0024473893 scopus 로고
    • Persistence of α-helix stop signal in the S-peptide in trifluoroethanol solution
    • Nelson J.W., Kallenbach N.R. Persistence of α-helix stop signal in the S-peptide in trifluoroethanol solution. Biochemistry. 28:1989;5226-5261
    • (1989) Biochemistry , vol.28 , pp. 5226-5261
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 20
    • 2042487484 scopus 로고
    • Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. The pure CD spectra of type I and type II β-turns
    • Perczel A., Hollosi M., Foxman B.M., Fasman G.D. Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. The pure CD spectra of type I and type II β-turns. J. Am. Chem. Soc. 113:1991;9772-9784
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9772-9784
    • Perczel, A.1    Hollosi, M.2    Foxman, B.M.3    Fasman, G.D.4
  • 22
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith C.K., Withka J.M., Regan L. A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry. 33:1994;5510-5517
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 23
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid β-peptide
    • Soto C., Branes M.C., Alvarez J., Inestrosa N.C. Structural determinants of the Alzheimer's amyloid β-peptide. J. Neurochem. 63:1994;1191-1198
    • (1994) J. Neurochem. , vol.63 , pp. 1191-1198
    • Soto, C.1    Branes, M.C.2    Alvarez, J.3    Inestrosa, N.C.4
  • 24
    • 0026500416 scopus 로고
    • The structure of the E. coli RecA protein monomer and polymer
    • Story R.M., Weber I.T., Steitz T.A. The structure of the E. coli RecA protein monomer and polymer. Nature. 355:1992;318-325
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 25
    • 0021813201 scopus 로고
    • Networks of DNA and RecA protein are intermediates in homologous pairing
    • Tsang S.S., Chow S.A., Radding C.M. Networks of DNA and RecA protein are intermediates in homologous pairing. Biochemistry. 24:1985;3226-3232
    • (1985) Biochemistry , vol.24 , pp. 3226-3232
    • Tsang, S.S.1    Chow, S.A.2    Radding, C.M.3
  • 26
    • 0029974806 scopus 로고    scopus 로고
    • Homologous DNA pairing promoted by a 20 amino acid peptide from RecA
    • Voloshin O.N., Wang L., Camerini-Otero R.D. Homologous DNA pairing promoted by a 20 amino acid peptide from RecA. Science. 272:1996;868-872
    • (1996) Science , vol.272 , pp. 868-872
    • Voloshin, O.N.1    Wang, L.2    Camerini-Otero, R.D.3
  • 27
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous D.V., Johnson J.W.C. Importance of environment in determining secondary structure in proteins. Biochemistry. 33:1994;2121-2128
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson, J.W.C.2
  • 28
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interaction
    • Wong, Lohman. A double-filter method for nitrocellulose-filter binding application to protein-nucleic acid interaction. Proc. Natl Acad. Sci. USA. 90:1993;5428-5432
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong1    Lohman2
  • 29
    • 0002439879 scopus 로고
    • Circular dichroism of peptides
    • Woody R.W. Circular dichroism of peptides. The Peptides. 7:1985;15-103
    • (1985) The Peptides , vol.7 , pp. 15-103
    • Woody, R.W.1
  • 30
    • 0029379540 scopus 로고
    • The search for DNA homology does not limit stable homologous pairing promoted by RecA protein
    • Yancey-Wrona J.E., Camerini-Otero R.D. The search for DNA homology does not limit stable homologous pairing promoted by RecA protein. Curr. Biol. 5:1995;1149-1158
    • (1995) Curr. Biol. , vol.5 , pp. 1149-1158
    • Yancey-Wrona, J.E.1    Camerini-Otero, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.