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  • 1
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In Pseudomonas putida, benzoate and 3-chlorobenzoate are converted to catechol and 3-chlorocatechol, respectively, which are then catabolized to tricarboxylic acid cycle intermediates via the catBCA and clcABD pathways. The catBCA and clcABD operons are regulated by homologous transcriptional activators CatR and ClcR. Previous studies have demonstrated that in addition to sequence similarities, CatR and ClcR share functional similarities which allow catR to complement clcR. In this study, we demonstrate that CatR activates the clcABD promoter in vitro without inducer, but more transcript is produced when inducer is added. DNase I footprinting and DNA-bending analyses demonstrate that CatR binds to and bends the clcABD promoter to the same angle as does ClcR plus its inducer, 2-chloromuconate. This implies that CatR binds to the clc promoter in its active conformation. Transcription of the clcABD promoter by the α-subunit truncation mutant (α-235) of RNA polymerase was sharply reduced, indicating that the α-subunit C-terminal domain is important. However, a small amount of transcript was produced under these conditions, indicating that other contact sites on the RNA polymerase may play a role in activation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 4 (1989), S. 335-340 
    ISSN: 1476-5535
    Keywords: Acetoin ; Lactate ; Acetate ; pH-homeostasis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary While the ability of lactobacilli to catabolize pyruvate to a variety of industrially important catabolites is well known, the mechanisms which regulate pyruvate distribution among alternative catabolic pathways is unclear. This paper demonstrates that environmental acidity regulates the catabolic activities ofLactobacillus plantarum cells in chemostat cultures.L. plantarum cells grown in medium containing 100 mM exogenous pyruvate, diverted pyruvate away from lactate to acetoin. Pyruvate uptake and acetoin generation increased under acidic conditions; on a molar basis, pyruvate utilization increased twice as fast as acetoin production, reflecting the 2∶1 stoichiometry of pyruvate incorporation into acetoin. Lactate production increased under alkaline conditions when glucose was fermented to provide endogenous pyruvate. Acetate was formed only at pH 7.5 and 8.0, although acetoin production decreased at elevated pH values. These data indicate thatL. plantarum adjusts to changes in environmental pH by altering its distribution of pyruvate among various catabolites.
    Type of Medium: Electronic Resource
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