Rec mutants of Escherichia coli deficient in subunits of rec BC (D) complex.
The inactivation of rec BC (D) DNase upon chromatography on DEAE-cellulose was observed. Simultaneously DNA-stimulated ATPases (I and II) and DNase activities on single- and double-stranded DNA substrates were measured in Escherichia coli rec+ and rec- cell extracts. Normal levels of ATPase I and II were detected in rec+ cells. Rec A- cells were lacking DNA dependent ATPase I, while rec B single and rec BC double mutants were defective in DNA dependent ATPase II, the second major enzyme of this type. Rec B and C mutations did not change DNase activities. Rec A mutation significantly increased DNase activity on linear single-stranded substrate.
Tenke
E
E
1st Institute of Biochemistry, Semmelweis University Medical School, Budapest, Hungary.
Bánfalvi
G
G
D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D002021:Buffers; D002848:Chromatography, DEAE-Cellulose; D004265:DNA Helicases / Q000235:genetics* / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism; D043211:Exodeoxyribonuclease V; D005090:Exodeoxyribonucleases / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D011938:Rec A Recombinases / Q000235:genetics / Q000378:metabolism
D002021:Buffers; D004269:DNA, Bacterial; D004277:DNA, Single-Stranded; D011938:Rec A Recombinases; D005090:Exodeoxyribonucleases; D043211:Exodeoxyribonuclease V; D000251:Adenosine Triphosphatases; D004265:DNA Helicases