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Nucleic Acids Research, 2002, Vol. 30, No. 12 2656-2662
© 2002 Oxford University Press

DNA bending, compaction and negative supercoiling by the architectural protein Sso7d of Sulfolobus solfataricus

Alessandra Napoli, Yvan Zivanovic1, Chantal Bocs1, Cyril Buhler1, Mose’ Rossi, Patrick Forterre1 and Maria Ciaramella*

Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Via Pietro Castellino 111, 80131 Naples, Italy and 1Institut de Génétique et Microbiologie, Université Paris-Sud, Centre Universitaire d’Orsay, 91405 Orsay Cedex, France

Members of the Sso7d/Sac7d family are small, abundant, non-specific DNA-binding proteins of the hyperthermophilic Archaea Sulfolobus. Crystal structures of these proteins in complex with oligonucleotides showed that they induce changes in the helical twist and marked DNA bending. On this basis they have been suggested to play a role in organising chromatin structures in these prokaryotes, which lack histones. We report functional in vitro assays to investigate the effects of the observed Sso7d-induced structural modifications on DNA geometry and topology. We show that binding of multiple Sso7d molecules to short DNA fragments induces significant curvature and reduces the stiffness of the complex. Sso7d induces negative supercoiling of DNA molecules of any topology (relaxed, positively or negatively supercoiled) and in physiological conditions of temperature and template topology. Binding of Sso7d induces compaction of positively supercoiled and relaxed DNA molecules, but not of negatively supercoiled ones. Finally, Sso7d inhibits the positive supercoiling activity of the thermophile-specific enzyme reverse gyrase. The proposed biological relevance of these observations is that these proteins might model the behaviour of DNA in constrained chromatin environments.

* To whom correspondence should be addressed. Tel: +39 081 6132247; Fax: +39 081 6132277; Email: ciaramel{at}dafne.ibpe.na.cnr.it


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