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Updated: Jun 25, 2026

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro
Sabrina Castellano1, Benedetta Farina, Maria Rosaria Faraone-Mennella
1Department of Structural and Functional Biology, Faculty of Sciences MM FF NN, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Napoli, Italy.
Abstract:
The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in DNA assembly. This protein undergoes in vitro ADP-ribosylation by an endogenous poly(ADP-ribose) polymerase-like enzyme. The circular dichroism spectrum of purified ADP-ribosylated Sso7 shows that this modification stabilizes the prevalent protein beta-conformation, as suggested by shifting of negative ellipticity minimum to 220 nm. Moreover, a short ADP-ribose chain (up to 6-mers) bound to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, suggesting a possible regulatory role of ADP-ribosylation in sulfolobal DNA organization.
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