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 DN...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 264; no. 25; pp. 15066 - 15069
Main Authors Panayotatos, N, Fontaine, A, Baeckman, S
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 05.09.1989
Subjects
Deoxyribonuclease IV (Phage T4-Induced)
DNA, Superhelical - metabolism
Endodeoxyribonucleases - biosynthesis
Endodeoxyribonucleases - genetics
Endodeoxyribonucleases - metabolism
Operator Regions, Genetic
Plasmids
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Repressor Proteins - biosynthesis
Repressor Proteins - genetics
Repressor Proteins - metabolism
Substrate Specificity
T-Phages - enzymology
T-Phages - genetics
Transcription Factors - biosynthesis
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Summary: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.
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ISSN:0021-9258
1083-351X