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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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Bibliographic Details
Main Authors: Sandıkcı, Arzu (Author) , Gloge, Felix (Author) , Martinez, Michael (Author) , Mayer, Matthias P. (Author) , Wade, Rebecca C. (Author) , Bukau, Bernd (Author) , Kramer, Günter (Author)
Format: Article (Journal)
Language:English
Published: 16 June 2013
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
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Author Notes:Arzu Sandikci, Felix Gloge, Michael Martinez, Matthias P. Mayer, Rebecca Wade, Bernd Bukau & Günter Kramer
Description
Summary: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.
Item Description:Gesehen am 28.01.2022
Physical Description:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb.2615

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