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BP: Fachverband Biologische Physik
BP 25: Oscillatory Systems
BP 25.3: Talk
Thursday, March 29, 2007, 15:15–15:30, H44
Mobility of Min-proteins in Escherichia coli by fluorescence correlation spectroscopy — Giovanni Meacci1, Jonas Ries2, •Elisabeth Fischer-Friedrich1, Nicoletta Kahya2, Petra Schwille2, and Karsten Kruse1 — 1Max-Planck Institute for the Physics of Complex Systems, Nöthnitzer Str. 38, 01187 Dresden, Germany — 2TU-Dresden, Biotec, Am Tatzberg 47-51, 01307 Dresden, Germany
In the bacterium Escherichia coli, positioning of the division site involves pole-to-pole oscillations of Min-proteins.
Different oscillation mechanisms based on cooperative effects between Min-proteins and the exchange of Min-proteins between the cytoplasm and the cytoplasmic membrane have been proposed.
However, the parameters characterising the dynamics of the Min-proteins in vivo are not known. Therefore, it has been difficult to compare the models quantitatively with experiments.
We have now performed in vivo measurements of the mobility of Min-proteins using fluorescence correlation spectroscopy.
Two distinct time-scales are visible in the correlation curves. While the faster time-scale can be attributed to cytoplasmic diffusion, the slower time-scale could result from diffusion of membrane-bound proteins or from protein exchange between the cytoplasm and the membrane.
We discuss implications of the measured values for the oscillation mechanism.