Cotranslational protein folding
Speaker: Professor Gunnar von Heijne, Department of Biochemistry and Biophysics, Stockholm University
Host: Professor Jakob R. Winther, Section for Biomolecular Sciences
Abstract
Translational arrest peptides (APs) can be used as force sensors to report on cotranslational events during protein synthesis. By analyzing a series of protein constructs where the length of chain between an AP and a force-generating element it is possible to measure “force profiles” that show the variation in the force acting on the nascent chain at every step during translation. Using this approach, we can study the cotranslational insertion membrane proteins into the inner membrane of E. coli, as well as the cotranslational folding of cytoplasmic proteins.
- Ismail, N., Hedman, R., Schiller, N., and von Heijne, G. (2012) A bi-phasic pulling force acts on transmembrane helices during translocon-mediated membrane integration. Nature Struct. Molec. Biol. 19, 1018-1023.
- Nilsson, O.B., Hedman, R., Marino, J., Wickles, S., Bischoff, L., Johansson, M., Müller-Lucks, A., Trovato, F., Puglisi, J.D., O’Brien, E., Beckmann, R., and von Heijne, G. (2015) Cotranslational protein folding inside the ribosome exit tunnel. Cell Reports 12, 1533-1540.
- Nilsson, O.B., Nickson, A.A., Hollins, J.J., Wickles, S., Steward, A., Beckmann, R., von Heijne, G., and Clarke, J. (2017) Cotranslational folding of spectrin domains via partially structured states. Nature Struct Molec Biol 24, 221-225.