Evidence for structural conservation of Lon and RcsA.
DNA probes specific to the Escherichia coli genes encoding Lon protease and RcsA hybridized to specific DNA sequences in a number of different microorganisms. Antiserum to either E. coli protein Lon or RcsA reacted with specific proteins in these organisms. These results provide structural evidence of the presence of Lon and RcsA in organisms other than E. coli.
Dierksen
K P
KP
Department of Microbiology, Oregon State University, Corvallis 97331-3804.
Marks
J
J
Chen
D D
DD
Trempy
J E
JE
D049069:ATP-Dependent Proteases; D001419:Bacteria / Q000737:chemistry* / Q000201:enzymology*; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology*; D003429:Cross Reactions; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics / Q000276:immunology*; D008970:Molecular Weight; D049070:Protease La; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000235:genetics / Q000276:immunology*; D013045:Species Specificity
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C067572:RcsA protein, E coli; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La