Understanding of chromatin organization and compaction in Archaea is currently limited. The genome of several megabasepairs long is folded by a set of small chromatin proteins to fit into the micron-sized cell. A first step in understanding archaeal chromatin organization is to study the action of individual chromatin proteins on DNA. Characterization of the architectural properties of these proteins is essential to understand how they shape and modulate the archaeal genome. This thesis describes the biophysical characterization of several chromatin proteins from the crenarchaeal model organism Sulfolobus solfataricus: Cren7, Sul7, Alba and Sso10a. The architectural properties of these proteins resemble those of their bacterial counterparts, suggesting that they could play a similar role in chromatin organization and global gene regulation.UBL - phd migration 201
