Structural highlights
Publication Abstract from PubMed
Sso10a proteins are small DNA-binding proteins expressed by the crenarchaeal model organism Sulfolobus solfataricus. Based on the structure of Sso10a1, which contains a winged helix-turn-helix motif, it is believed that Sso10a proteins function as sequence-specific transcription factors. Here we show that Sso10a1 and Sso10a2 exhibit different distinct DNA-binding modes. While the ability to bend DNA is shared between the two proteins, DNA bridging is observed only for Sso10a1 and only Sso10a2 exhibits filament formation along DNA. The architectural properties of Sso10a proteins suggest that these proteins fulfil generic roles in chromatin organization and compaction. As these proteins exhibit different binding behaviour depending on their DNA binding stoichiometry, altered levels of expression in the cell can be exploited to drive changes in local genome folding, which may operate to modulate transcription.
Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization.,Driessen RP, Lin SN, Waterreus WJ, van der Meulen AL, van der Valk RA, Laurens N, Moolenaar GF, Pannu NS, Wuite GJ, Goosen N, Dame RT Sci Rep. 2016 Jul 11;6:29422. doi: 10.1038/srep29422. PMID:27403582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Driessen RP, Lin SN, Waterreus WJ, van der Meulen AL, van der Valk RA, Laurens N, Moolenaar GF, Pannu NS, Wuite GJ, Goosen N, Dame RT. Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization. Sci Rep. 2016 Jul 11;6:29422. doi: 10.1038/srep29422. PMID:27403582 doi:http://dx.doi.org/10.1038/srep29422
