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  Conformation of the signal recognition particle in ribosomal targeting complexes.

Buskiewicz, I. A., Jöckel, J., Rodnina, M. V., & Wintermeyer, W. (2009). Conformation of the signal recognition particle in ribosomal targeting complexes. RNA, 15(1), 44-54. doi:10.1261%2Frna.1285609.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-DBE3-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-8230-E
Genre: Journal Article

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2156328.pdf (Publisher version), 517KB
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 Creators:
Buskiewicz, I. A., Author
Jöckel, J., Author
Rodnina, M. V.1, Author              
Wintermeyer, W.2, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578599              

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Free keywords: trigger factor, SRP, SRP receptor, FtsY, membrane targeting
 Abstract: The bacterial signal recognition particle (SRP) binds to ribosomes synthesizing inner membrane proteins and, by interaction with the SRP receptor, FtsY, targets them to the translocon at the membrane. Here we probe the conformation of SRP and SRP protein, Ffh, at different stages of targeting by measuring fluorescence resonance energy transfer (FRET) between fluorophores placed at various positions within SRP. Distances derived from FRET indicate that SRP binding to nontranslating ribosomes triggers a global conformational change of SRP that facilitates binding of the SRP receptor, FtsY. Binding of SRP to a signal-anchor sequence exposed on a ribosome-nascent chain complex (RNC) causes a further change of the SRP conformation, involving the flexible part of the Ffh(M) domain, which increases the affinity for FtsY of ribosome-bound SRP up to the affinity exhibited by the isolated NG domain of Ffh. This indicates that in the RNC–SRP complex the Ffh(NG) domain is fully exposed for binding FtsY to form the targeting complex. Binding of FtsY to the RNC–SRP complex results in a limited conformational change of SRP, which may initiate subsequent targeting steps.

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Language(s): eng - English
 Dates: 2009-01
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1261%2Frna.1285609
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Title: RNA
Source Genre: Journal
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Pages: - Volume / Issue: 15 (1) Sequence Number: - Start / End Page: 44 - 54 Identifier: -