We are analyzing https://link.springer.com/protocol/10.1007/978-1-62703-032-8_1.

Title:
Functions of Single-Strand DNA-Binding Proteins in DNA Replication, Recombination, and Repair | SpringerLink
Description:
Double-stranded (ds) DNA contains all of the necessary genetic information, although practical use of this information requires unwinding of the duplex DNA. DNA unwinding creates single-stranded (ss) DNA intermediates that serve as templates for myriad cellular...
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Topics {✒️}

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Schema {🗺️}

ScholarlyArticle:
      headline:Functions of Single-Strand DNA-Binding Proteins in DNA Replication, Recombination, and Repair
      pageEnd:21
      pageStart:1
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-62703-032-8.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Single-Stranded DNA Binding Proteins
         isbn:
            978-1-62703-032-8
            978-1-62703-031-1
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Aimee H. Marceau
            affiliation:
                  name:University of Wisconsin School of Medicine and Public Health
                  address:
                     name:Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Single-strand DNA-binding protein, Replication protein A, DNA replication, DNA repair, DNA recombination, DNA replication restart, Protein interactions, DNA binding, OB domain
      description:Double-stranded (ds) DNA contains all of the necessary genetic information, although practical use of this information requires unwinding of the duplex DNA. DNA unwinding creates single-stranded (ss) DNA intermediates that serve as templates for myriad cellular functions. Exposure of ssDNA presents several problems to the cell. First, ssDNA is thermodynamically less stable than dsDNA, which leads to spontaneous formation of duplex secondary structures that impede genome maintenance processes. Second, relative to dsDNA, ssDNA is hypersensitive to chemical and nucleolytic attacks that can cause damage to the genome. Cells deal with these potential problems by encoding specialized ssDNA-binding proteins (SSBs) that bind to and stabilize ssDNA structures required for essential genomic processes. SSBs are essential proteins found in all domains of life. SSBs bind ssDNA with high affinity and in a sequence-independent manner and, in doing so, SSBs help to form the central nucleoprotein complex substrate for DNA replication, recombination, and repair processes. While SSBs are found in every organism, the proteins themselves share surprisingly little sequence similarity, subunit composition, and oligomerization states. All SSB proteins contain at least one DNA-binding oligonucleotide/oligosaccharide binding (OB) fold, which consists minimally of a five stranded beta-sheet arranged as a beta barrel capped by a single alpha helix. The OB fold is responsible for both ssDNA binding and oligomerization (for SSBs that operate as oligomers). The overall organization of OB folds varies between bacteria, eukaryotes, and archaea. As part of SSB/ssDNA cellular structures, SSBs play direct roles in the DNA replication, recombination, and repair. In many cases, SSBs have been found to form specific complexes with diverse genome maintenance proteins, often helping to recruit SSB/ssDNA-processing enzymes to the proper cellular sites of action. This clustering of genome maintenance factors can help to stimulate and coordinate the activities of individual enzymes and is also important for dislodging SSB from ssDNA. These features support a model in which DNA metabolic processes have evolved to work on ssDNA/SSB nucleoprotein filaments rather than on naked ssDNA. In this volume, methods are described to interrogate SSB-DNA and SSB-protein binding functions along with approaches that aim to understand the cellular functions of SSB. This introductory chapter offers a general overview of SSBs that focuses on their structures, DNA-binding mechanisms, and protein-binding partners.
      datePublished:2012
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      name:Single-Stranded DNA Binding Proteins
      isbn:
         978-1-62703-032-8
         978-1-62703-031-1
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      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Wisconsin School of Medicine and Public Health
      address:
         name:Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, USA
         type:PostalAddress
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      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Aimee H. Marceau
      affiliation:
            name:University of Wisconsin School of Medicine and Public Health
            address:
               name:Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
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      name:Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, USA
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