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High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein

Research output: Contribution to journalArticle


Michael John Morten, Roland Gamsjaeger, Liza Cubeddu, Ruvini Kariawasam, Jose Ramon Peregrina, Juan Carlos Penedo-Esteiro, Malcolm Frederick White

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Single-stranded DNA-binding proteins (SSBs), including replication protein A (RPA) in eukaryotes, play a central role in DNA replication, recombination, and repair. SSBs utilise an oligonucleotide/oligosaccharide-binding (OB) fold domain to bind DNA, and typically oligomerise in solution to bring multiple OB fold domains together in the functional SSB. SSBs from hyperthermophilic crenarchaea, such as Sulfolobus solfataricus, have an unusual structure with a single OB fold coupled to a flexible C-terminal tail. The OB fold resembles those in RPA, whilst the tail is reminiscent of bacterial SSBs and mediates interaction with other proteins. One paradigm in the field is that SSBs bind specifically to ssDNA and much less strongly to RNA, ensuring that their functions are restricted to DNA metabolism. Here, we use a combination of biochemical and biophysical approaches to demonstrate that the binding properties of S. solfataricus SSB are essentially identical for ssDNA and ssRNA. These features may represent an adaptation to a hyperthermophilic lifestyle, where DNA and RNA damage is a more frequent event.



Original languageEnglish
Pages (from-to)369-379
Number of pages11
Issue number2
Early online date10 Jan 2017
Publication statusPublished - Mar 2017

    Research areas

  • RNA binding proteins, OB fold, Single-molecule dynamics, Förster resonance energy transfer , Nuclear magnetic resonance

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