Sso7d is a small, basic, abundant protein from the thermoacidophilic archaeon Sulfolobus solfataricus. Previous research has shown that Sso7d can bind double-stranded DNA without sequence specificity by placing its triple-stranded β-sheet across the minor groove. We previously found RNase activity both in preparations of Sso7d purified from its natural source and in recombinant, purified protein expressed in Escherichia coli. This paper provides conclusive evidence that supports the assignment of RNase activity to Sso7d, shown by the total absence of activity in the single-point mutants E35L and K12L, despite the preservation of their overall structure under the assay conditions. In keeping with our observation that the residues putatively involved in RNase activity and those playing a role in DNA binding are located on different surfaces of the molecule, the activity was not impaired in the presence of DNA. If a small synthetic RNA was used as a substrate, Sso7d attacked both predicted double- and single-stranded RNA stretches, with no evident preference for specific sequences or individual bases. Apparently, the more readily attacked bonds were those intrinsically more unstable. © 2001 Federation of European Biochemical Societies.

Shehi, E., Serina, S., Fumagalli, G., Vanoni, M., Consonni, R., Zetta, L., et al. (2001). The Sso7d DNA-binding protein from Sulfolobus solfataricus has ribonuclease activity. FEBS LETTERS, 497(2-3), 131-136 [10.1016/S0014-5793(01)02455-3].

The Sso7d DNA-binding protein from Sulfolobus solfataricus has ribonuclease activity

VANONI, MARCO ERCOLE;TORTORA, PAOLO
;
FUSI, PAOLA ALESSANDRA
2001

Abstract

Sso7d is a small, basic, abundant protein from the thermoacidophilic archaeon Sulfolobus solfataricus. Previous research has shown that Sso7d can bind double-stranded DNA without sequence specificity by placing its triple-stranded β-sheet across the minor groove. We previously found RNase activity both in preparations of Sso7d purified from its natural source and in recombinant, purified protein expressed in Escherichia coli. This paper provides conclusive evidence that supports the assignment of RNase activity to Sso7d, shown by the total absence of activity in the single-point mutants E35L and K12L, despite the preservation of their overall structure under the assay conditions. In keeping with our observation that the residues putatively involved in RNase activity and those playing a role in DNA binding are located on different surfaces of the molecule, the activity was not impaired in the presence of DNA. If a small synthetic RNA was used as a substrate, Sso7d attacked both predicted double- and single-stranded RNA stretches, with no evident preference for specific sequences or individual bases. Apparently, the more readily attacked bonds were those intrinsically more unstable. © 2001 Federation of European Biochemical Societies.
Articolo in rivista - Articolo scientifico
Sso7d; Ribonuclease; DNA-binding protein; Archaeon; Sulfolobus solfataricus
English
2001
497
2-3
131
136
none
Shehi, E., Serina, S., Fumagalli, G., Vanoni, M., Consonni, R., Zetta, L., et al. (2001). The Sso7d DNA-binding protein from Sulfolobus solfataricus has ribonuclease activity. FEBS LETTERS, 497(2-3), 131-136 [10.1016/S0014-5793(01)02455-3].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/34636
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