메뉴 건너뛰기




Volumn 1, Issue 2, 2002, Pages 87-93

The Sso7d protein of Sulfolobus solfataricus: In vitro relationship among different activities

Author keywords

ATP hydrolysis; DNA binding protein; Hydrophobic protein interaction; Protein aggregation

Indexed keywords

BACTERIA (MICROORGANISMS); GARCIA; SULFOLOBUS; SULFOLOBUS SOLFATARICUS;

EID: 0037692270     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2002/313147     Document Type: Article
Times cited : (14)

References (21)
  • 1
    • 0031851758 scopus 로고    scopus 로고
    • Architecture of nonspecific protein-DNA interactions in the Sso7d-DNA complex
    • Agback, P.H., S. Baumann, R. Knapp, R. Ladenstein and T. Hard. 1998. Architecture of nonspecific protein-DNA interactions in the Sso7d-DNA complex. Nat. Struct. Biol. 5:579-584.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 579-584
    • Agback, P.H.1    Baumann, S.2    Knapp, R.3    Ladenstein, R.4    Hard, T.5
  • 2
    • 0030922584 scopus 로고    scopus 로고
    • Structure of the chromatin binding (chromo) domain from mouse modifier protein 1
    • Ball, L.J., N. V. Murzina, R.W. Broadhurst et al. 1997. Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. EMBO J. 16:2473-2481.
    • (1997) EMBO J. , vol.16 , pp. 2473-2481
    • Ball, L.J.1    Murzina, N.V.2    Broadhurst, R.W.3
  • 3
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Baumann, H., S. Knapp, T. Lundback, R. Ladenstein and T. Hard. 1994. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nat. Struct. Biol. 1:808-819.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundback, T.3    Ladenstein, R.4    Hard, T.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing dye binding of proteins
    • Bradford, M.M. 1976. A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing dye binding of proteins. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone, M. and N.K. Puri. 1992. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem. J. 282:589-593.
    • (1992) Biochem. J. , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 7
    • 0034986024 scopus 로고    scopus 로고
    • DNA binding proteins Sac7d and Sso7d from Sulfolobus
    • Edmondson, S.P. and J.W. Shriver. 2001. DNA binding proteins Sac7d and Sso7d from Sulfolobus. Methods Enzymol. 334:129-145.
    • (2001) Methods Enzymol. , vol.334 , pp. 129-145
    • Edmondson, S.P.1    Shriver, J.W.2
  • 8
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M.R. and C.A. Ghiron. 1981. Fluorescence quenching studies with proteins. Anal. Biochem. 114:199-227.
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 10
    • 0028788591 scopus 로고
    • Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule
    • Guagliardi, A., L. Cerchia and M. Rossi. 1995. Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule. J. Biol. Chem. 270:28,126-28,132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28126-28132
    • Guagliardi, A.1    Cerchia, L.2    Rossi, M.3
  • 11
    • 0031564652 scopus 로고    scopus 로고
    • Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein
    • Guagliardi, A., A. Napoli, M. Rossi and M. Ciaramella. 1997. Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein. J. Mol. Biol. 267:841-848.
    • (1997) J. Mol. Biol. , vol.267 , pp. 841-848
    • Guagliardi, A.1    Napoli, A.2    Rossi, M.3    Ciaramella, M.4
  • 12
    • 0034644686 scopus 로고    scopus 로고
    • The chromosomal protein Sso7d of the crenarchaeon Sulfolobus solfataricus rescues aggregated proteins in an ATP hydrolysis-dependent manner
    • Guagliardi, A., L. Cerchia, M. Moracci and M. Rossi. 2000. The chromosomal protein Sso7d of the crenarchaeon Sulfolobus solfataricus rescues aggregated proteins in an ATP hydrolysis-dependent manner. J. Biol. Chem. 275:31,813-31,818.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31813-31818
    • Guagliardi, A.1    Cerchia, L.2    Moracci, M.3    Rossi, M.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 2642690670 scopus 로고    scopus 로고
    • In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth
    • Lopez-Garcia, P., S. Knapp, R. Ladenstein and P. Forterre. 1998. In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth. Nucleic Acids Res. 26:2322-2328.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2322-2328
    • Lopez-Garcia, P.1    Knapp, S.2    Ladenstein, R.3    Forterre, P.4
  • 16
    • 0035260487 scopus 로고    scopus 로고
    • The molecular chaperone system and other anti-stress mechanisms in archaea
    • Macario, A.J.L. and E. Conway de Macario. 2001. The molecular chaperone system and other anti-stress mechanisms in archaea. Front. Biosci. 6:262-283.
    • (2001) Front. Biosci. , vol.6 , pp. 262-283
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 17
    • 0031709343 scopus 로고    scopus 로고
    • Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus
    • Oppermann, U.C.T., S. Knapp, V. Bonetto, R. Ladenstein and H. Jornvall. 1998. Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. FEBS Lett. 432:141-144.
    • (1998) FEBS Lett. , vol.432 , pp. 141-144
    • Oppermann, U.C.T.1    Knapp, S.2    Bonetto, V.3    Ladenstein, R.4    Jornvall, H.5
  • 20
    • 0034011209 scopus 로고    scopus 로고
    • Structure and functional relationships of archaeal and eukaryal histones and nucleosomes
    • Sandman, K. and J.N. Reeve. 2000. Structure and functional relationships of archaeal and eukaryal histones and nucleosomes. Arch. Microbiol. 173:165-169.
    • (2000) Arch. Microbiol. , vol.173 , pp. 165-169
    • Sandman, K.1    Reeve, J.N.2
  • 21
    • 0029902963 scopus 로고    scopus 로고
    • Locations of functional domains in the RecA protein
    • Takahshi, M., F. Maraboeuf and B. Norden. 1996. Locations of functional domains in the RecA protein. Eur. J. Biochem. 242:20-28.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 20-28
    • Takahshi, M.1    Maraboeuf, F.2    Norden, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.