Two separable protein species which both restore uvrABC endonuclease activity in extracts from uvrC mutated cells.
Two different protein species which both complement the detective repair endonuclease (uvrABC endonuclease) in uvrC mutated cells have been detected. These proteins have quite different chromatographic properties and were easily separated by ion exchange chromatography. One has affinity for DEAE cellulose and co-cromatographs with the uvrB protein. The other has strong affinity for phosphocellulose and appears to be the uvrC protein itself. The uvrB associated uvrC+ activity is absent from both uvrC and uvrB mutated cells, indicating that this species result from an interaction between uvrB+ and uvrC+ functions at the protein level.
D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification; D004260:DNA Repair; D004261:DNA Replication; D004591:Electrophoresis, Polyacrylamide Gel; D004706:Endodeoxyribonucleases / Q000235:genetics*; D029968:Escherichia coli Proteins; D008970:Molecular Weight; D009154:Mutation
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D004706:Endodeoxyribonucleases; C036385:endodeoxyribonuclease uvrABC