Assembly and Fragmentation of Tat Pores
In this chapter we determine how the formation of transient pores on the membrane depends on the dynamics of its assembly process. We analyse the temporary pores formed by the Tat translocation system, which is responsible for protein transport through the membrane. Its main mechanism is the polymerisation of its subunits, in response to a signal of demand of the transport from a protein in the cell cytoplasm. The direct correlation of the size of the assembled pore and the size of the protein determines the speed of the translocation process. Using a differential equation approach we obtain that the flux of a given protein depends quadratically on its size.
KeywordsExport Rate Subunit Assembly Free Monomer Translocation System Twin Arginine Translocation
- 1.Gohlke, U., Pullan, L., McDevitt, C.A., Porcelli, I., de Leeuw, E., Palmer, T., Saibil, H.R., Berks, B.C.: The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc. Nat. Acad. Sci. U S A 102(30), 10482–10486 (2005)Google Scholar
- 2.Leake, M.C., Greene, N.P., Godun, R.M., Granjon, T., Buchanan, G., Chen, S., Berry, R.M., Palmer, T., Berks B.C.: Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. Proc. Nat. Acad. Sci. U S A 105(40), 15376 –15381 (2008)Google Scholar
- 3.Mullineaux, C.W., Nenninger, A., Ray, N., Robinson C.: Diffusion of green fluorescent protein in three cell environments in Escherichia coli. J. Bacteriol. 188(10), 3442–3448 (2006)Google Scholar