Multiple human single-stranded DNA binding proteins function in genome maintenance : structural, biochemical and functional analysis

Richard, Derek, Bolderson, Emma, & Khanna, Kum Kum (2009) Multiple human single-stranded DNA binding proteins function in genome maintenance : structural, biochemical and functional analysis. Critical Reviews in Biochemistry and Molecular Biology, 44(2-3), pp. 98-116.

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DNA exists predominantly in a duplex form that is preserved via specific base pairing. This base pairing affords a considerable degree of protection against chemical or physical damage and preserves coding potential. However, there are many situations, e.g. during DNA damage and programmed cellular processes such as DNA replication and transcription, in which the DNA duplex is separated into two singlestranded DNA (ssDNA) strands. This ssDNA is vulnerable to attack by nucleases, binding by inappropriate proteins and chemical attack. It is very important to control the generation of ssDNA and protect it when it forms, and for this reason all cellular organisms and many viruses encode a ssDNA binding protein (SSB). All known SSBs use an oligosaccharide/oligonucleotide binding (OB)-fold domain for DNA binding. SSBs have multiple roles in binding and sequestering ssDNA, detecting DNA damage, stimulating strand-exchange proteins and helicases, and mediation of protein–protein interactions. Recently two additional human SSBs have been identified that are more closely related to bacterial and archaeal SSBs. Prior to this it was believed that replication protein A, RPA, was the only human equivalent of bacterial SSB. RPA is thought to be required for most aspects of DNA metabolism including DNA replication, recombination and repair. This review will discuss in further detail the biological pathways in which human SSBs function.

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ID Code: 40619
Item Type: Journal Article
Refereed: Yes
Keywords: Homology-directed repair (HDR); nucleotide excision repair (NER); replication fork restart;Homology-directed repair (HDR); nucleotide excision repair (NER); replication fork restart; translesion synthesis; checkpoint control
DOI: 10.1080/10409230902849180
ISSN: 1040-9238
Divisions: Past > Schools > Cell & Molecular Biosciences
Past > QUT Faculties & Divisions > Faculty of Science and Technology
Deposited On: 09 Mar 2011 06:21
Last Modified: 29 Feb 2012 14:31

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