Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 679-684 |
| Number of pages | 6 |
| Journal | Journal of Cell Biology |
| Volume | 161 |
| DOIs | |
| Publication status | Published - 2003 |
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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 Journal › Article › Academic
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 -