The site-specific recombination locus of mycobacteriophage Ms6 determines DNA integration at the tRNA(super Ala) gene of Mycobacterium spp
Article Abstract:
A study was undertaken to examine the site-specific integration of the mycobacteriophage Ms6 and show that this system can conduct the insertion of heterologous DNA into the tRNA(super Ala) gene of the Mycobacterium smegmatis. The phage attachment site was localized on the Ms6 genome by comparing the Southern blots of lysogenic genomic DNAs and the DNA derived from mycobacteriophage. Results revealed that the site-specific recombination between the phage DNA and the bacterial genome was at the 26 bp common core site found at the 3' end of the tRNA(super Ala) gene.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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Mycobacterium smegmatis DNA gyrase: cloning and overexpression in Escherichia coli
Article Abstract:
Analysis of the nucleotide sequence of the structural genes from Mycobacterium smegmatis DNA gyrase shows similarity to the gryA and gryB genes from other bacteria. The cloning into a T7 phage and overexpression in E. coli produces GryA and GryB proteins with molecular weights that compare well with calculations from open reading frames. The identity of the genes is confirmed by testing for enzyme activity. Individual extracts from the overexpressing clones show absence of enzyme activity but the combined extract exhibits DNA gyrase and supercoiling activity.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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ppc, the gene for phosphoenolpyruvate carboxylase from an extremely thermophilic bacterium, Rhodothermus obamensis: cloning, sequencing and overexpression in Escherichia coli
Article Abstract:
The phophoenolpyruvate carboxylase (PEPC) gene (ppc) of Rhodothermus obamensis is encoded by the ppc gene. Thermal asymmetric interlaced polymerase chain reaction, used to sequence this gene revealed an open reading frame for a 937-amino acid protein with an estimated molecular mass of 107,848 Daltons. This is consistent with the measured weight of PEPC from electrophoretic analysis. The results and implications of the heterologous expression of ppc in Escherichia coli are discussed.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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