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

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 mu...

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Autores principales: Morten, Michael J., Gamsjaeger, Roland, Cubeddu, Liza, Kariawasam, Ruvini, Peregrina, Jose, Penedo, J. Carlos, White, Malcolm F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Japan 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5346138/
https://www.ncbi.nlm.nih.gov/pubmed/28074284
http://dx.doi.org/10.1007/s00792-016-0910-2
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author Morten, Michael J.
Gamsjaeger, Roland
Cubeddu, Liza
Kariawasam, Ruvini
Peregrina, Jose
Penedo, J. Carlos
White, Malcolm F.
author_facet Morten, Michael J.
Gamsjaeger, Roland
Cubeddu, Liza
Kariawasam, Ruvini
Peregrina, Jose
Penedo, J. Carlos
White, Malcolm F.
author_sort Morten, Michael J.
collection PubMed
description 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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spelling pubmed-53461382017-03-22 High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein Morten, Michael J. Gamsjaeger, Roland Cubeddu, Liza Kariawasam, Ruvini Peregrina, Jose Penedo, J. Carlos White, Malcolm F. Extremophiles Original Paper 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. Springer Japan 2017-01-10 2017 /pmc/articles/PMC5346138/ /pubmed/28074284 http://dx.doi.org/10.1007/s00792-016-0910-2 Text en © The Author(s) 2017 Open AccessThis 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.
spellingShingle Original Paper
Morten, Michael J.
Gamsjaeger, Roland
Cubeddu, Liza
Kariawasam, Ruvini
Peregrina, Jose
Penedo, J. Carlos
White, Malcolm F.
High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
title High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
title_full High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
title_fullStr High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
title_full_unstemmed High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
title_short High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein
title_sort high-affinity rna binding by a hyperthermophilic single-stranded dna-binding protein
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5346138/
https://www.ncbi.nlm.nih.gov/pubmed/28074284
http://dx.doi.org/10.1007/s00792-016-0910-2
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