ArticleScientific reports2016
Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 22 citations in OpenAlex.
- The Lrs14-Like AbfR1 Homolog From Metallosphaera sedula Is a Nucleoid-Organizing Protein.MicrobiologyOpen · 2025Article
- Identification, characterization and classification of prokaryotic nucleoid-associated proteins.Molecular microbiology · 2025Review
- The Lrs14 family of DNA-binding proteins as nucleoid-associated proteins in the Crenarchaeal order Sulfolobales.Molecular microbiology · 2025Review
- Effects of genomic location on ectopic integration and gene expression of a reporter gene cassette inFrontiers in microbiology · 2025Article
- Dual dimeric interactions in the nucleic acid-binding protein Sac10b lead to multiple bridging of double-stranded DNA.Heliyon · 2024Article
- Quantitation of DNA Binding Affinity Using Tethered Particle Motion.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Macromolecular Crowding and DNA: Bridging the Gap between In Vitro and In Vivo.International journal of molecular sciences · 2023Review
- Article
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
- Mechanical and structural properties of archaeal hypernucleosomes.Nucleic acids research · 2021Article
- Article
- Structure and function of archaeal histones.PLoS genetics · 2018Review
- The Arginine Pairs and C-Termini of the Sso7c4 from Sulfolobus solfataricus Participate in Binding and Bending DNA.PloS one · 2017Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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