ArticleExtremophiles : life under extreme conditions2017
High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein.
Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Mechanistic insights into direct DNA and RNA strand transfer and dynamic protein exchange of SSB and RPA.Nucleic acids research · 2025Article
- Capture of RNA-binding proteins across mouse tissues using HARD-AP.Nature communications · 2024Article
- Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger.Nucleic acids research · 2024Article
- The canonical single-stranded DNA-binding protein is not an essential replication factor but an RNA chaperon iniScience · 2023Article
- New Understandings from the Biophysical Study of the Structure, Dynamics, and Function of Nucleic Acids 2.0.International journal of molecular sciences · 2022Article
- Review
- NMR Structure and Biophysical Characterization of Thermophilic Single-Stranded DNA Binding Protein fromInternational journal of molecular sciences · 2022Article
- Single-Stranded DNA-Binding Proteins in the Archaea.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Expression, Purification, and Solution-State NMR Analysis of the Two Human Single-Stranded DNA-Binding Proteins hSSB1 (NABP2/OBFC2B) and hSSB2 (NAPB1/OBFC2A).Methods in molecular biology (Clifton, N.J.) · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.