The lysA gene of Escherichia coli has been cloned from a lambda transducing phage on various plasmids, present in different copy numbers in bacterial cells. Synthesis of the product of this gene, diaminopimelate (DAP)-decarboxylase, and its regulation have been studied. Expression does not follow a
Regulation of the L-arabinose operon in strains of Escherichia coli containing ColE1-ara hybrid plasmids
✍ Scribed by Wallace, Linda J. ;Wilcox, Gary
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 813 KB
- Volume
- 173
- Category
- Article
- ISSN
- 0026-8925
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✦ Synopsis
Hybrid plasmids were constructed from fragments of F'ara episomes formed by the restriction endonuclease EcoRI and a linear form of the plasmid ColE1 created by cleavage with EcoRI. Hybrid plasmids were constructed containing the entire ara region or the ara region with various parts deleted. E. coli K12 host strains were constructed which contained different deletions of the ara region. The hybrid plasmids were transferred to those strains whose ara deletion complemented that of the plasmid. The initial differential rates of synthesis of L-arabinose isomerase, the product of the araA gene, were determined for the Ara+, plasmid containing strains. These studies demonstrated that strains containing delta(araOIBA)718 produce elevated levels of araC protein, suggesting the araC promoter has been altered by this deletion. Evidence is also presented which suggests that araC protein activates the ara-BAD operon to higher levels when it is present in cis rather than trans. Amplification of the products of the cloned genes is observed when compared to haploid levels in some cases.
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