The Sso7d protein of <i>Sulfolobus solfataricus</i>: in vitro relationship among different activities

Guagliardi, Annamaria; Cerchia, Laura; Rossi, Mosè

doi:https://doi.org/10.1155/2002/313147

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Research Article | Open Access

Volume 1 | Article ID 313147 | https://doi.org/10.1155/2002/313147

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

Annamaria Guagliardi,¹Laura Cerchia,¹and Mosè Rossi^1,2

Received22 Oct 2001

Accepted08 Jan 2002

Abstract

The physiological role of the nonspecific DNA-binding protein Sso7d from the crenarchaeon Sulfolobus solfataricus is unknown. In vitro studies have shown that Sso7d promotes annealing of complementary DNA strands (Guagliardi et al. 1997), induces negative supercoiling (Lopez-Garcia et al. 1998), and chaperones the disassembly and renaturation of protein aggregates in an ATP hydrolysis-dependent manner (Guagliardi et al. 2000). In this study, we examined the relationships among the binding of Sso7d to double-stranded DNA, its interaction with protein aggregates, and its ATPase activity. Experiments with 1-anilinonaphthalene-8-sulfonic acid as probe demonstrated that exposed hydrophobic surfaces in Sso7d are responsible for interactions with protein aggregates and double-stranded DNA, whereas the site of ATPase activity has a non-hydrophobic character. The interactions of Sso7d with double-stranded DNA and with protein aggregates are mutually exclusive events, suggesting that the disassembly activity and the DNA-related activities of Sso7d may be competitive in vivo. In contrast, the hydrolysis of ATP by Sso7d is independent of the binding of Sso7d to double-stranded DNA or protein aggregates.

References

P.H. Agback, S. Baumann, R. Knapp, R. Ladenstein, and T. Hard, “Architecture of nonspecific protein–DNA interactions in the Sso7d–DNA complex,” Nat. Struct. Biol., vol. 5, pp. 579–584, 1998.
View at: Google Scholar
L.J. Ball, N.V. Murzina, R.W. Broadhurst et al., “Structure of the chromatin binding (chromo) domain from mouse modifier protein 1,” EMBO J., vol. 16, pp. 2473–2481, 1997.
View at: Google Scholar
H. Baumann, S. Knapp, T. Lundback, R. Ladenstein, and T. Hard, “Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus,” Nat. Struct. Biol., vol. 1, pp. 808–819, 1994.
View at: Google Scholar
M.M. Bradford, “A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing dye binding of proteins,” Anal. Biochem., vol. 72, pp. 248–254, 1976.
View at: Google Scholar
C.R. Cantor and P.R. Schimmel, “Biophysical chemistry,” pp. 433–455, Part III: the behavior of biological macromolecules. W.H. Freeman, San Francisco, 1980.
View at: Google Scholar
M. Cardamone and N.K. Puri, “Spectrofluorimetric assessment of the surface hydrophobicity of proteins,” Biochem. J., vol. 282, pp. 589–593, 1992.
View at: Google Scholar
S.P. Edmondson and J.W. Shriver, “DNA binding proteins Sac7d and Sso7d from Sulfolobus,” Methods Enzymol., vol. 334, pp. 129–145, 2001.
View at: Google Scholar
M.R. Eftink and C.A. Ghiron, “Fluorescence quenching studies with proteins,” Anal. Biochem., vol. 114, pp. 199–227, 1981.
View at: Google Scholar
Y.G. Gao, S.Y. Su, and S.Y. Su, “The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA,” Nat. Struct. Biol., vol. 5, pp. 782–786, 1998.
View at: Google Scholar
A. Guagliardi, L. Cerchia, and M. Rossi, “Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule.,” J. Biol. Chem., vol. 270, pp. 28126–28132, 1995.
View at: Google Scholar
A. Guagliardi, A. Napoli, M. Rossi, and M. Ciaramella, “Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein,” J. Mol. Biol., vol. 267, pp. 841–848, 1997.
View at: Google Scholar
A. Guagliardi, L. Cerchia, M. Moracci, and M. Rossi, “The chromosomal protein Sso7d of the crenarchaeon Sulfolobus solfataricus rescues aggregated proteins in an ATP hydrolysis-dependent manner,” J. Biol. Chem., vol. 275, pp. 31813–31818, 2000.
View at: Google Scholar
S. Knapp, P.T. Mattson, and P.T. Mattson, “Thermal unfolding of small proteins with SH3 domain folding pattern,” Proteins, vol. 31, pp. 309–319, 1998.
View at: Google Scholar
U.K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, pp. 680–685, 1970.
View at: Google Scholar
P. Lopez-Garcia, S. Knapp, R. Ladenstein, and P. Forterre, “In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth,” Nucleic Acids Res., vol. 26, pp. 2322–2328, 1998.
View at: Google Scholar
A.J.L. Macario and E. Conway de Macario, “The molecular chaperone system and other anti-stress mechanisms in archaea,” Front. Biosci., vol. 6, pp. 262–283, 2001.
View at: Google Scholar
U.C.T. Oppermann, S. Knapp, V. Bonetto, R. Ladenstein, and H. Jornvall, “Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus,” FEBS Lett., vol. 432, pp. 141–144, 1998.
View at: Google Scholar
H. Robinson, Y.-G. Gao, B.S. Mccrary, S.P. Edmondson, J.W. Shriver, and A.H.-J. Wang, “The hyperthermophile chromosomal protein Sac7d sharply kinks DNA,” Nature, vol. 392, pp. 202–205, 1998.
View at: Google Scholar
J. Sambrook, E.F. Fritsch, and T. Maniatis, “Molecular cloning: a laboratory manual,” Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 2nd Edn. edition, 1989.
View at: Google Scholar
K. Sandman and J.N. Reeve, “Structure and functional relationships of archaeal and eukaryal histones and nucleosomes,” Arch. Microbiol., vol. 173, pp. 165–169, 2000.
View at: Google Scholar
M. Takahshi, F. Maraboeuf, and B. Norden, “Locations of functional domains in the RecA protein,” Eur. J. Biochem., vol. 242, pp. 20–28, 1996.
View at: Google Scholar

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Copyright © 2002 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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