Biosynthesis of a repressor/nuclease hybrid protein.
The phage T7 endonuclease gene was fused to the 3' end of the lac repressor gene. The hybrid protein exhibits repressor and nuclease functions in a manner dependent on the conformation of the DNA. With supercoiled DNA, nuclease activity is directed to the major cruciform, whereas with linear DNA, the enzyme cleaves preferentially restriction fragments carrying the operator. These properties render the hybrid protein a unique probe of DNA conformation in vitro and in vivo.
Panayotatos
N
N
Michigan Biotechnology Institute, Lansing 48909.
Fontaine
A
A
Bãckman
S
S
D004278:DNA, Superhelical / Q000378:metabolism; D043223:Deoxyribonuclease IV (Phage T4-Induced); D004706:Endodeoxyribonucleases / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D009875:Operator Regions, Genetic; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D013604:T-Phages / Q000201:enzymology / Q000235:genetics; D014157:Transcription Factors / Q000096:biosynthesis*
D004278:DNA, Superhelical; D011994:Recombinant Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D004706:Endodeoxyribonucleases; D043223:Deoxyribonuclease IV (Phage T4-Induced)