Temperature dependence of leakiness of transcription repression mechanisms of Escherichia coli

Nadia Goncalves, Samuel M D Oliveira, Vinodh K. Kandavalli, Jose M. Fonseca, Andre S. Ribeiro

    Research output: Chapter in Book/Report/Conference proceedingConference contributionScientificpeer-review

    2 Citations (Scopus)

    Abstract

    In E. coli, transcription repression is essential in cellular functioning. However, its failure rates are non-negligible. We measured the leakiness rate of lacO3O1 promoter with single RNA sensitivity and its temperature dependence in live cells. After finding strong temperature dependence, we dissected the causes. While RNA polymerase numbers and kt, the rate of active transcription, vary weakly with temperature, the repression strength (dependent on number of repressors and binding and unbinding rates of repressors to the promoter) is heavily temperature dependent. We conclude that the lacO3O1 leakiness at low temperatures increases as the repression mechanism’s efficiency hampers.

    Original languageEnglish
    Title of host publicationComputational Methods in Systems Biology - 14th International Conference, CMSB 2016
    PublisherSpringer Verlag
    Pages341-342
    Number of pages2
    ISBN (Print)9783319451763
    Publication statusPublished - 2016
    Publication typeA4 Article in conference proceedings
    EventInternational Conference on Computational Methods in Systems Biology -
    Duration: 1 Jan 1900 → …

    Publication series

    NameLecture Notes in Computer Science
    Volume9859
    ISSN (Print)0302-9743
    ISSN (Electronic)1611-3349

    Conference

    ConferenceInternational Conference on Computational Methods in Systems Biology
    Period1/01/00 → …

    Keywords

    • lacO3O1
    • Leakiness
    • MS2-GFP RNA detection
    • Repression
    • Time-lapse confocal microscopy
    • Transcription

    Publication forum classification

    • Publication forum level 1

    ASJC Scopus subject areas

    • Theoretical Computer Science
    • Computer Science(all)

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