Human single-stranded DNA binding proteins are essential for maintaining genomic stability

Nicholas W. Ashton, Emma Bolderson, Liza Cubeddu, Kenneth J. O'Byrne, Derek J. Richard

    Research output: Contribution to journalArticlepeer-review

    83 Citations (Scopus)

    Abstract

    The double-stranded conformation of cellular DNA is a central aspect of DNA stabilisation and protection. The helix preserves the genetic code against chemical and enzymatic degradation, metabolic activation, and formation of secondary structures. However, there are various instances where single-stranded DNA is exposed, such as during replication or transcription, in the synthesis of chromosome ends, and following DNA damage. In these instances, single-stranded DNA binding proteins are essential for the sequestration and processing of single-stranded DNA. In order to bind single-stranded DNA, these proteins utilise a characteristic and evolutionary conserved single-stranded DNA-binding domain, the oligonucleotide/oligosaccharide-binding (OB)-fold. In the current review we discuss a subset of these proteins involved in the direct maintenance of genomic stability, an important cellular process in the conservation of cellular viability and prevention of malignant transformation. We discuss the central roles of single-stranded DNA binding proteins from the OB-fold domain family in DNA replication, the restart of stalled replication forks, DNA damage repair, cell cycle-checkpoint activation, and telomere maintenance.
    Original languageEnglish
    Pages (from-to)1-20
    Number of pages20
    JournalBMC Molecular Biology
    Volume14
    Issue number9
    DOIs
    Publication statusPublished - 2013

    Open Access - Access Right Statement

    © 2013 Ashton et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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