Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding
Nascent polypeptides undergo various cotranslational maturation steps, including N-terminal enzymatic processing, chaperone-assisted folding and membrane targeting. Kinetic analyses now demonstrate that N-terminal processing enzymes have fast ribosome binding kinetics, and premature chaperone recrui...
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| Main Authors: | , , , , , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
16 June 2013
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| In: |
Nature structural & molecular biology
Year: 2013, Volume: 20, Issue: 7, Pages: 843-850 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2615 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb.2615 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb.2615 |
| Author Notes: | Arzu Sandikci, Felix Gloge, Michael Martinez, Matthias P. Mayer, Rebecca Wade, Bernd Bukau & Günter Kramer |
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| 520 | |a Nascent polypeptides undergo various cotranslational maturation steps, including N-terminal enzymatic processing, chaperone-assisted folding and membrane targeting. Kinetic analyses now demonstrate that N-terminal processing enzymes have fast ribosome binding kinetics, and premature chaperone recruitment or folding negatively affects processing efficiency, thereby separating nascent chain processing from later events. | ||
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