title: Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis.
abstract: NMR spectroscopy has been used to determine that the dimerization interface of UmuD' in solution is not the homodimer interface originally inferred from crystallographic data. Instead, it resembles an interface that had been hypothesized to be involved in filamentation.
authors.forename: A E
authors.initials: AE
authors.lastname: Ferentz
authors.forename: T
authors.initials: T
authors.lastname: Opperman
authors.forename: G C
authors.initials: GC
authors.lastname: Walker
authors.forename: G
authors.initials: G
authors.lastname: Wagner
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D004259:DNA-Directed DNA Polymerase; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D016296:Mutagenesis; D011487:Protein Conformation; D013014:SOS Response, Genetics / Q000235:genetics*; D012996:Solutions
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D012996:Solutions; D004259:DNA-Directed DNA Polymerase; C055218:UmuD protein, E coli