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

R.S. Ullers, E.N.G. Houben, A. Raine, C.M. ten Hagen-Jongman ten, M. Ehrenberg, J Brunner, B. Oudega, N. Harms, S. Luirink

Research output: Contribution to JournalArticleAcademic

Abstract

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 non-translating 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.
Original languageEnglish
Pages (from-to)679-684
Number of pages6
JournalJournal of Cell Biology
Volume161
DOIs
Publication statusPublished - 2003

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Signal Recognition Particle
Ribosomes
Escherichia coli
Membrane Proteins
Protein Sorting Signals
Peptides

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title = "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome",
abstract = "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 non-translating 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.",
author = "R.S. Ullers and E.N.G. Houben and A. Raine and {ten Hagen-Jongman ten}, C.M. and M. Ehrenberg and J Brunner and B. Oudega and N. Harms and S. Luirink",
year = "2003",
doi = "10.1083/jcb.200302130",
language = "English",
volume = "161",
pages = "679--684",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",

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Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome. / Ullers, R.S.; Houben, E.N.G.; Raine, A.; ten Hagen-Jongman ten, C.M.; Ehrenberg, M.; Brunner, J; Oudega, B.; Harms, N.; Luirink, S.

In: Journal of Cell Biology, Vol. 161, 2003, p. 679-684.

Research output: Contribution to JournalArticleAcademic

TY - JOUR

T1 - Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome

AU - Ullers, R.S.

AU - Houben, E.N.G.

AU - Raine, A.

AU - ten Hagen-Jongman ten, C.M.

AU - Ehrenberg, M.

AU - Brunner, J

AU - Oudega, B.

AU - Harms, N.

AU - Luirink, S.

PY - 2003

Y1 - 2003

N2 - 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 non-translating 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.

AB - 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 non-translating 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.

U2 - 10.1083/jcb.200302130

DO - 10.1083/jcb.200302130

M3 - Article

VL - 161

SP - 679

EP - 684

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

ER -