title: Ammonium sulfate co-precipitation of SSB and interacting proteins.
abstract: Bacterial single-strand DNA-binding protein (SSB) interacts with many proteins involved in the diverse process of genome maintenance. The interactions are mediated by the essential and conserved amphipathic C-terminus (SSB-Ct). SSB plays a critical role in localizing and stimulating the activity of a wide variety of DNA-processing proteins. The interaction partners have been identified and studied using a variety of methods, one of which, ammonium sulfate co-precipitation, is described here.
authors.affiliation: Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI, USA. amarceau@wisc.edu
authors.forename: Aimee H
authors.initials: AH
authors.lastname: Marceau
mesh_terms: D000645:Ammonium Sulfate / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D011232:Chemical Precipitation; D004268:DNA-Binding Proteins / Q000378:metabolism*; D008967:Molecular Biology / Q000379:methods
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D000645:Ammonium Sulfate