Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis.
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.
Ferentz
A E
AE
Opperman
T
T
Walker
G C
GC
Wagner
G
G
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
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D012996:Solutions; D004259:DNA-Directed DNA Polymerase; C055218:UmuD protein, E coli