High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
MetadataShow full item record
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.
Morten , M J , Gamsjaeger , R , Cubeddu , L , Kariawasam , R , Peregrina , J R , Penedo-Esteiro , J C & White , M F 2017 , ' High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein ' Extremophiles , vol. 21 , no. 2 , pp. 369-379 . https://doi.org/10.1007/s00792-016-0910-2
© The Author(s) 2017. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.