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Published online 19 May 2003. doi:10.1083/jcb.200302130
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© The Rockefeller University Press, 0021-9525/2003/5/679 $5.00
The Journal of Cell Biology, Volume 161, Number 4, 679-684

Report

Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome



Ronald S. Ullers1, Edith N.G. Houben1, Amanda Raine2, Corinne M. ten Hagen-Jongman1, Måns Ehrenberg3, Joseph Brunner4, Bauke Oudega1, Nellie Harms1 and Joen Luirink1

1 Department of Molecular Microbiology, Vrije Universiteit, 1081 HV Amsterdam, Netherlands
2 Department of Pharmaceutical Biosciences, Uppsala University, S-7514 Uppsala, Sweden
3 Department of Cell and Molecular Biology, Uppsala University, S-7514 Uppsala, Sweden
4 Institute of Biochemistry, Eidgenössische Technische Hochschule Zürich, CH-8093 Zürich, Switzerland

Address correspondence to Joen Luirink, Dept. Molecular Microbiology, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, Netherlands. Tel.: 31-20-4447175. Fax: 31-20-4446979. E-mail: joen.luirink{at}falw.vu.nl

As newly synthesized polypeptides emerge from the ribosome, they interact with chaperones and targeting factors that assist in folding and targeting to the proper location in the cell. In Escherichia coli, the chaperone trigger factor (TF) binds to nascent polypeptides early in biosynthesis facilitated by its affinity for the ribosomal proteins L23 and L29 that are situated around the nascent chain exit site on the ribosome. The targeting factor signal recognition particle (SRP) interacts specifically with the signal anchor (SA) sequence in nascent inner membrane proteins (IMPs). Here, we have used photocross-linking to map interactions of the SA sequence in a short, in vitro–synthesized, nascent IMP. Both TF and SRP were found to interact with the SA with partially overlapping binding specificity. In addition, extensive contacts with L23 and L29 were detected. Both purified TF and SRP could be cross-linked to L23 on nontranslating ribosomes with a competitive advantage for SRP. The results suggest a role for L23 in the targeting of IMPs as an attachment site for TF and SRP that is close to the emerging nascent chain.

Key Words: signal recognition particle; trigger factor; ribosome; protein targeting; membrane protein

The online version of this manuscript includes supplemental material.

* Abbreviations used in this paper: EDC, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide; Ffh, fifty-four homologue; IMP, inner membrane protein; SA, signal anchor; SRP, signal recognition particle; TF, trigger factor.


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