Hyperproduction of araC protein from Escherichia coli

Hypersynthesis of araC protein from Escherichia coli has been accomplished. The araC gene was cloned on plasmid pBR322, and some of the noncoding DNA preceding the araC gene was removed by exonuclease digestion. Finally, a DNA fragment containing the lac promoter and ribosome binding site was placed...

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Bibliographic Details
Published inBiochemistry (Easton) Vol. 21; no. 4; pp. 778 - 782
Main Authors Schleif, Robert Ferber, Favreau, Margaret Anne
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 16.02.1982
Subjects
AraC Transcription Factor
Bacterial Proteins
Cloning, Molecular
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Genes, Bacterial
Lac Operon
Plasmids
Repressor Proteins - biosynthesis
Repressor Proteins - genetics
Repressor Proteins - isolation & purification
Transcription Factors - biosynthesis
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Summary:Hypersynthesis of araC protein from Escherichia coli has been accomplished. The araC gene was cloned on plasmid pBR322, and some of the noncoding DNA preceding the araC gene was removed by exonuclease digestion. Finally, a DNA fragment containing the lac promoter and ribosome binding site was placed in front the araC gene. By these means the level of araC protein was increased about 5000-fold above the levels found in wild-type cells. This level of protein permits straight forward purification of sizeable quantities of araC protein.
Bibliography:ark:/67375/TPS-KJ42J8T6-3
istex:333CBE4E667477236C993410D115EFAB07F5498F
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00533a031