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Robustness to sub-optimal temperatures of the processes of Tsr Cluster formation and positioning in Escherichia coli

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

Details

Original languageEnglish
Title of host publicationBIOINFORMATICS 2016 - 7th International Conference on Bioinformatics Models, Methods and Algorithms, Proceedings; Part of 9th International Joint Conference on Biomedical Engineering Systems and Technologies, BIOSTEC 2016
PublisherSCITEPRESS
Pages137-141
Number of pages5
ISBN (Print)9789897581700
Publication statusPublished - 2016
Publication typeA4 Article in a conference publication
EventINTERNATIONAL CONFERENCE ON BIOINFORMATICS MODELS, METHODS AND ALGORITHMS -
Duration: 1 Jan 1900 → …

Conference

ConferenceINTERNATIONAL CONFERENCE ON BIOINFORMATICS MODELS, METHODS AND ALGORITHMS
Period1/01/00 → …

Abstract

Clustering and positioning of chemotaxis-associated proteins are believed to be essential steps for their proper functioning. We investigate the robustness of these processes to sub-optimal temperatures by studying the size and location of clusters of Tsr-Venus proteins in live cells. We find that the degree of clustering of Tsr proteins is maximal under optimal temperature. The data further suggests that the weakening of the clustering process in lower-than and higher-than optimal temperatures is not due to the same cause. Meanwhile, the location of the clusters is found to be weakly temperature independent, within the range tested. We conclude that while the clustering of Tsr is heavily temperature dependent, the localization is only weakly dependent, suggesting that the functionality of the proteins responsible for retaining Tsr-clusters at the cell poles, such as the Tol-Pal complex, is robust to suboptimal temperatures.

Keywords

  • Cluster localization, Microscopy, Protein cluster, Tsr proteins

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