Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization

R.P.C. Driessen, S. Lin, W.J. Waterreus, A.L.H. van der Meulen, R.A. van der Valk, N. Laurens, G.F. Moolenaar, N.S. Pannu, G.J.L. Wuite, N. Goosen, R.T. Dame

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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.
Original languageEnglish
Article number29422
JournalScientific Reports
Volume6
DOIs
Publication statusPublished - 2016

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Chromatin
DNA
Proteins
Helix-Turn-Helix Motifs
Sulfolobus solfataricus
DNA-Binding Proteins
Transcription Factors
Genome

Cite this

Driessen, R.P.C. ; Lin, S. ; Waterreus, W.J. ; van der Meulen, A.L.H. ; van der Valk, R.A. ; Laurens, N. ; Moolenaar, G.F. ; Pannu, N.S. ; Wuite, G.J.L. ; Goosen, N. ; Dame, R.T. / Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization. In: Scientific Reports. 2016 ; Vol. 6.
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abstract = "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.",
author = "R.P.C. Driessen and S. Lin and W.J. Waterreus and {van der Meulen}, A.L.H. and {van der Valk}, R.A. and N. Laurens and G.F. Moolenaar and N.S. Pannu and G.J.L. Wuite and N. Goosen and R.T. Dame",
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Driessen, RPC, Lin, S, Waterreus, WJ, van der Meulen, ALH, van der Valk, RA, Laurens, N, Moolenaar, GF, Pannu, NS, Wuite, GJL, Goosen, N & Dame, RT 2016, 'Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization' Scientific Reports, vol. 6, 29422. https://doi.org/10.1038/srep29422

Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization. / Driessen, R.P.C.; Lin, S.; Waterreus, W.J.; van der Meulen, A.L.H.; van der Valk, R.A.; Laurens, N.; Moolenaar, G.F.; Pannu, N.S.; Wuite, G.J.L.; Goosen, N.; Dame, R.T.

In: Scientific Reports, Vol. 6, 29422, 2016.

Research output: Contribution to JournalArticleAcademicpeer-review

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