Titlebook: Single-Stranded DNA Binding Proteins; Methods and Protocol James L. Keck Book 2012 Springer Science+Business Media, LLC 2012 DNA-binding pr

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Fluorescent Single-Stranded DNA-Binding Proteins Enable In Vitro and In Vivo Studies, incorporated per tetramer. We describe the use of these tetramers to enable clear visualization of SSB in vivo. Purified chimeras also facilitate single molecule studies (Liu et al., Protein Sci 20:1005–1020, 2011).

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Use of Fluorescently Tagged SSB Proteins in In Vivo Localization Experiments,r of DNA replication. In this chapter I describe how to observe replication of the . chromosome in a strain that synthesizes a fluorescent derivative of SSB. This methodology provides information about the position and dynamics of DNA replication through epifluorescence.

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,Identification of Small Molecules That Disrupt SSB–Protein Interactions Using a High-Throughput Scronuclease I (ExoI) and the final 10 amino acids of the SSB C-terminal tail (SSB-Ct). The strength of the binding between ExoI and the SSB-Ct tail is fundamental to the interaction’s utility in the high-throughput screen.

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Functions of Single-Strand DNA-Binding Proteins in DNA Replication, Recombination, and Repair,x 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 struc

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SSB Binding to ssDNA Using Isothermal Titration Calorimetry, appreciable enthalpy change, ITC studies can yield quantitative information on stoichiometries, binding energetics (affinity, binding enthalpy and entropy) and potential site–site interactions (cooperativity). This can provide a full thermodynamic description of an interacting system which is neces

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Single-Molecule Analysis of SSB Dynamics on Single-Stranded DNA,esses. For subsequent DNA processing, however, SSB needs to be removed and yield to other proteins while avoiding ssDNA exposure to nucleases. Using single-molecule two- and three-color fluorescence resonance energy transfer (FRET) and fluorescence-force spectroscopy, we recently showed that the SSB

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