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  Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence.

Mercier, E., Holtkamp, W., Rodnina, M. V., & Wintermeyer, W. (2017). Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence. Nucleic Acids Research, 45(20), 11858-11866. doi:10.1093/nar/gkx888.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-F56E-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-3A1C-0
Genre: Journal Article

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 Creators:
Mercier, E.1, Author              
Holtkamp, W.1, Author              
Rodnina, M. V.1, Author              
Wintermeyer, W.2, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, escidoc:578598              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, escidoc:578599              

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Free keywords: amino acids fluorescence peptides ribosomes signal recognition particle translating kinetics affinity binding (molecular function)
 Abstract: The bacterial signal recognition particle (SRP) is part of the machinery that targets ribosomes synthesizing membrane proteins to membrane-embedded translocons co-translationally. Recognition of nascent membrane proteins occurs by virtue of a hydrophobic signal-anchor sequence (SAS) contained in the nascent chain, usually at the N terminus. Here we use fluorescence-based stopped-flow to monitor SRP-ribosome interactions with actively translating ribosomes while an SRP substrate is synthesized and emerges from the peptide exit tunnel. The kinetic analysis reveals that, at cellular concentrations of ribosomes and SRP, SRP rapidly binds to translating ribosomes prior to the emergence of an SAS and forms an initial complex that rapidly rearranges to a more stable engaged complex. When the growing peptide reaches a length of ∼50 amino acids and the SAS is partially exposed, SRP undergoes another conformational change which further stabilizes the complex and initiates targeting of the translating ribosome to the translocon. These results provide a reconciled view on the timing of high-affinity targeting complex formation, while emphasizing the existence of preceding SRP recruitment steps under conditions of ongoing translation.

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Language(s): eng - English
 Dates: 2017-10-092017-11-16
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gkx888
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Title: Nucleic Acids Research
Source Genre: Journal
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Pages: - Volume / Issue: 45 (20) Sequence Number: - Start / End Page: 11858 - 11866 Identifier: -