Robustness to sub-optimal temperatures of the processes of Tsr Cluster formation and positioning in Escherichia coli
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Robustness to sub-optimal temperatures of the processes of Tsr Cluster formation and positioning in Escherichia coli. / Annila, Teppo; Neeli-Venkata, Ramakanth; Ribeiro, Andre S.
BIOINFORMATICS 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. SCITEPRESS, 2016. p. 137-141.Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › Scientific › peer-review
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TY - GEN
T1 - Robustness to sub-optimal temperatures of the processes of Tsr Cluster formation and positioning in Escherichia coli
AU - Annila, Teppo
AU - Neeli-Venkata, Ramakanth
AU - Ribeiro, Andre S.
PY - 2016
Y1 - 2016
N2 - 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.
AB - 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.
KW - Cluster localization
KW - Microscopy
KW - Protein cluster
KW - Tsr proteins
M3 - Conference contribution
SN - 9789897581700
SP - 137
EP - 141
BT - BIOINFORMATICS 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
PB - SCITEPRESS
ER -