Purification and Functional Reconstitution of the Bacterial Protein Translocation Pore, the SecYEG ComplexKusters, I., Bogaart, G. V. D., de Wit, J., Krasnikov, V., Poolman, B. & Driessen, A., 25-Jan-2010, Protein Secretion: Methods and Protocols. Economou, A. (ed.). Humana Press, Vol. 619. p. 131-143 13 p. (Methods in Molecular Biology).
Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review
In bacteria, proteins are secreted across the cytoplasmic membrane by a protein complex termed translocase. The ability to study the activity of the translocase in vitro using purified proteins has been instrumental for our understanding of the mechanisms underlying this process. Here, we describe the protocols for the purification and reconstitution of the SecYEG complex in an active state into liposomes. In addition, fluorescence based in vitro assays are described that allow monitoring translocation activity discontinuously and in real time.
|Title of host publication||Protein Secretion|
|Subtitle of host publication||Methods and Protocols|
|Number of pages||13|
|ISBN (Print)||978-1-60327-167-7, 978-1-4939-5707-1|
|Publication status||Published - 25-Jan-2010|