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Biosynthesis of a repressor/nuclease hybrid protein.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1989 Sep 05; Vol. 264 (25), pp. 15066-9. - Publication Year :
- 1989
-
Abstract
- 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.
- Subjects :
- DNA, Superhelical metabolism
Deoxyribonuclease IV (Phage T4-Induced)
Endodeoxyribonucleases genetics
Endodeoxyribonucleases metabolism
Operator Regions, Genetic
Plasmids
Recombinant Proteins genetics
Recombinant Proteins metabolism
Repressor Proteins genetics
Repressor Proteins metabolism
Substrate Specificity
T-Phages enzymology
T-Phages genetics
Endodeoxyribonucleases biosynthesis
Recombinant Proteins biosynthesis
Repressor Proteins biosynthesis
Transcription Factors biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 264
- Issue :
- 25
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 2768253