Albany 2015:Book of Abstracts
June 9-13 2015
©Adenine Press (2012)
The busy life of nascent chains: Mechanisms of folding of newly synthesized proteins
Protein homeostasis is established by a complex cellular machinery which assists and regulates regular folding pathways and counteracts protein misfolding and aggregation. A particularly critical process in the life of a protein is the native folding of newly synthesized proteins, which therefore is tightly controlled. Already during ongoing synthesis by the ribosome nascent polypeptides are subject to enzymatic processing, chaperone-assisted folding to the native state or targeting to translocation pores at membranes. The ribosome itself plays a key role in these different tasks by serving as platform for the regulated association of enzymes, targeting factors and chaperones that act upon the nascent polypeptides emerging from the exit tunnel. The molecular mechanisms integrating the different co-translational processes leading to the maturation and native folding of nascent chains will be described.
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E. Oh, E., Becker, A.H., Sandikci, A., Huber, D., Chaba, R., Gloge, F., Nichols, R.J., Typas, A., Gross, C.A., Kramer, G., Weissman, J.S. & Bukau, B. (2011). Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. Cell 147, 1295-1308.
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Center for Molecular Biology of the University of Heidelberg