The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro.
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.
Castellano
Sabrina
S
Department of Structural and Functional Biology, Faculty of Sciences MM FF NN, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Napoli, Italy.
Farina
Benedetta
B
Faraone-Mennella
Maria Rosaria
MR
D000244:Adenosine Diphosphate / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism*; D019641:DNA, Archaeal / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D048229:Sulfolobus solfataricus / Q000378:metabolism*
D019843:Archaeal Proteins; D019641:DNA, Archaeal; D004268:DNA-Binding Proteins; C093228:Sso7d protein, Sulfolobus; D000244:Adenosine Diphosphate; D011065:Poly(ADP-ribose) Polymerases