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Ribosomes pp 405-418 | Cite as

Mechanistic insight into co-translational protein processing, folding, targeting, and membrane insertion

  • Daniel Boehringer
  • Basil Greber
  • Nenad Ban

Abstract

In the cell newly synthesized polypeptides are subjected to enzymatic processing, chaperone-assisted folding, and targeting to translocation pores at membranes concurrently with their synthesis by the ribosome (Figure 1). The major players in these events are, (i) ribosome-associated chaperones, (ii) nascent-chain-processing enzymes, (iii) the signal recognition particle — a complex that recognizes ribosomes that are translating membrane and some secretory proteins and targets them to the membrane — and (iv) the membrane-protein-insertion machinery — a large multi-subunit trans-membrane complex responsible for protein insertion into or translocation across membranes. The ribosome plays a major role in governing the interplay between the various factors involved. Using electron microscopy, crystallography and biochemical approaches, we investigated the structural and mechanistic aspects of the interaction between these factors and the ribosome.

Keywords

Trigger Factor Signal Recognition Particle Membrane Insertion Nascent Polypeptide Tunnel Exit 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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© Springer-Verlag/Wien 2011

Authors and Affiliations

  • Daniel Boehringer
  • Basil Greber
  • Nenad Ban

There are no affiliations available

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