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.
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| http://dx.doi.org/10.1038/srep29422 | DOI Listing |
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Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization.
Sci Rep
July 2016
Leiden Institute of Chemistry, Cell Observatory and Centre for Microbial Cell Biology, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
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.
View Article and Find Full Text PDFSolution structure, stability, and flexibility of Sso10a: a hyperthermophile coiled-coil DNA-binding protein.
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March 2005
Biomolecular Nuclear Magnetic Resonance Laboratory, Department of Chemistry, Graduate Program in Biotechnology Science and Engineering, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA.
Sso10a is one of a number of DNA-binding proteins from the hyperthermophile Sulfolobus solfataricus that has been associated with DNA packaging and chromatin regulation. Sequence analysis indicates that it is a member of a conserved group of archaeal transcription regulators (COG3432). We have determined the solution structure of Sso10a and show that it is a homodimer of winged-helix DNA-binding domains.
View Article and Find Full Text PDFThe hyperthermophile protein Sso10a is a dimer of winged helix DNA-binding domains linked by an antiparallel coiled coil rod.
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Laboratory for Structural Biology, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
Sso10a is a member of a group of DNA-binding proteins thought to be important in chromatin structure and regulation in the hyperthermophilic archaeon Sulfolobus solfataricus. We have determined the structure of Sso10a to 1.47A resolution directly with unlabelled native crystals by a novel approach using sulfur single-wavelength anomalous scattering (SAS) from a chromium X-ray source.
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Chemistry Department, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
The gene for the DNA-binding protein Sso10a from the hyperthermophilic archaeon Sulfolobus solfataricus was cloned and overexpressed in Escherichia coli. Crystals of the purified protein have been grown that diffract to beyond 2.15 A resolution.
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