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Co-translational Protein Processing, Folding, Targeting, and Membrane Insertion of Newly Synthesized Proteins

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Abstract

Newly synthesized proteins leave the ribosome through the nascent polypeptide tunnel. Through the coordinated action of the ribosome associated chaperones, nascent chain processing enzymes, the signal recognition particle, and the protein insertion machinery newly synthesized proteins are brought into their native state and proper cellular localization. The interplay of these factors during ongoing synthesis requires spatial and temporal control of their interactions with the ribosome. We used electron microscopy in combination with crystallography and biochemical methods to study the structure of bacterial ribosomes and nascent chain interacting factors.

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Authors and Affiliations

  1. Institute of Molecular Biology and Biophysics, ETH Zurich, Schafmattstr. 20, 8093, Zurich, Switzerland

    Daniel Boehringer & Nenad Ban

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  1. Daniel Boehringer
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  2. Nenad Ban
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Correspondence to Nenad Ban .

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Editors and Affiliations

  1. , Instit.de Technologia Química e Biológia, Universidade Nova de Lisboa, Rua da Quinta Grande , Apartado 127 6, Oeiras, 2781-901, Portugal

    Maria Armenia Carrondo

  2. Dipto. Scienze Chimiche, Università di Padova, Via F. Marzolo 1, Padova, 35131, Italy

    Paola Spadon

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Boehringer, D., Ban, N. (2012). Co-translational Protein Processing, Folding, Targeting, and Membrane Insertion of Newly Synthesized Proteins. In: Carrondo, M., Spadon, P. (eds) Macromolecular Crystallography. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-2530-0_2

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