The defective phosphoribosyl diphosphate synthase in a temperature-sensitive prs-2 mutant of Escherichia coli is compensated by increased enzyme synthesis
Article Abstract:
Several prs mutants have been isolated and characterized in Escherichia coli. Included are a mutant with altered kinetic properties of PRPP synthase and genetically engineered prs deletion mutations constructed in vitro and then transferred to the chromosome via homologous recombination. The mutant strain prs-2 was isolated via a localized mutagenesis of the chromosome's prs region after a bacteriophage P1 lysate in a mutD-mutator strain had been prepared and the mutagenized DNA had been transferred to the E. coli chromosome by transduction. An analysis of the prs-2 mutation's biochemical nature is reported.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Physical-genetic map of the erythromycin-producing organism Saccharopolyspora erythraea
Article Abstract:
The restriction enzymes Asel and Dral were used to construct a physical and genetic map of the chromosome of the erythromycin-producing actinomycete Saccharopolyspora erythraea NRRL 2338. The digested fragments of the macrorestriction patterns of the restriction enzyme revealed a chromosome size of around 8Mb. It was also observed that 32% of the chromosome was covered by linking clones for the five contiguous Asel fragments. Moreover, the ribosomal RNA operons of S. erythraea contains an Asel site within the 16S(rrs) gene.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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Effects of signal peptide mutations on processing of Bacillus stearothermophilus alpha-amylase in Escherichia coli
Article Abstract:
A study of the effects of signal peptide mutations on the processing of Bacillus stearothermophilus alpha-amylase in Escherichia coli through site-directed mutagenesis reveals that the signal peptide is tolerant to mutations due to the presence of two alternative signal peptidase processing sites. The choice of the processing site depends on the sequence and length of the region between the cleavage site and the hydrophobic core. Site preference is also influenced by some mutations away from the cleavage site.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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