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Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes

BACKGROUND: Single-stranded DNA-binding proteins are essential cellular components required for the protection, metabolism and processing of single-stranded DNA. Human single-stranded DNA-binding protein 1 (hSSB1) is one such protein, with described roles in genome stability maintenance and transcri...

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Autores principales: Ashton, Nicholas W., Loo, Dorothy, Paquet, Nicolas, O’Byrne, Kenneth J., Richard, Derek J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5148904/
https://www.ncbi.nlm.nih.gov/pubmed/27938330
http://dx.doi.org/10.1186/s12867-016-0077-5
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author Ashton, Nicholas W.
Loo, Dorothy
Paquet, Nicolas
O’Byrne, Kenneth J.
Richard, Derek J.
author_facet Ashton, Nicholas W.
Loo, Dorothy
Paquet, Nicolas
O’Byrne, Kenneth J.
Richard, Derek J.
author_sort Ashton, Nicholas W.
collection PubMed
description BACKGROUND: Single-stranded DNA-binding proteins are essential cellular components required for the protection, metabolism and processing of single-stranded DNA. Human single-stranded DNA-binding protein 1 (hSSB1) is one such protein, with described roles in genome stability maintenance and transcriptional regulation. As yet, however, the mechanisms through which hSSB1 functions and the binding partners with which it interacts remain poorly understood. RESULTS: In this work, hSSB1 was immunoprecipitated from cell lysate samples that had been enriched for non-soluble nuclear proteins and those associating with hSSB1 identified by mass spectrometry. In doing so, 334 potential hSSB1-associating proteins were identified, with known roles in a range of distinct biological processes. Unexpectedly, whilst hSSB1 has largely been studied in a genome stability context, few other DNA repair or replication proteins were detected. By contrast, a large number of proteins were identified with roles in mRNA metabolism, reflecting a currently emerging area of hSSB1 study. In addition, numerous proteins were detected that comprise various chromatin-remodelling complexes. CONCLUSIONS: These findings provide new insight into the binding partners of hSSB1 and will likely function as a platform for future research. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12867-016-0077-5) contains supplementary material, which is available to authorized users.
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spelling pubmed-51489042016-12-16 Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes Ashton, Nicholas W. Loo, Dorothy Paquet, Nicolas O’Byrne, Kenneth J. Richard, Derek J. BMC Mol Biol Research Article BACKGROUND: Single-stranded DNA-binding proteins are essential cellular components required for the protection, metabolism and processing of single-stranded DNA. Human single-stranded DNA-binding protein 1 (hSSB1) is one such protein, with described roles in genome stability maintenance and transcriptional regulation. As yet, however, the mechanisms through which hSSB1 functions and the binding partners with which it interacts remain poorly understood. RESULTS: In this work, hSSB1 was immunoprecipitated from cell lysate samples that had been enriched for non-soluble nuclear proteins and those associating with hSSB1 identified by mass spectrometry. In doing so, 334 potential hSSB1-associating proteins were identified, with known roles in a range of distinct biological processes. Unexpectedly, whilst hSSB1 has largely been studied in a genome stability context, few other DNA repair or replication proteins were detected. By contrast, a large number of proteins were identified with roles in mRNA metabolism, reflecting a currently emerging area of hSSB1 study. In addition, numerous proteins were detected that comprise various chromatin-remodelling complexes. CONCLUSIONS: These findings provide new insight into the binding partners of hSSB1 and will likely function as a platform for future research. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12867-016-0077-5) contains supplementary material, which is available to authorized users. BioMed Central 2016-12-09 /pmc/articles/PMC5148904/ /pubmed/27938330 http://dx.doi.org/10.1186/s12867-016-0077-5 Text en © The Author(s) 2016 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. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Ashton, Nicholas W.
Loo, Dorothy
Paquet, Nicolas
O’Byrne, Kenneth J.
Richard, Derek J.
Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes
title Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes
title_full Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes
title_fullStr Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes
title_full_unstemmed Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes
title_short Novel insight into the composition of human single-stranded DNA-binding protein 1 (hSSB1)-containing protein complexes
title_sort novel insight into the composition of human single-stranded dna-binding protein 1 (hssb1)-containing protein complexes
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5148904/
https://www.ncbi.nlm.nih.gov/pubmed/27938330
http://dx.doi.org/10.1186/s12867-016-0077-5
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