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Proline Residues at the C Terminus of Nascent Chains Induce SsrA Tagging during Translation Termination
The SsrA or tmRNA quality control system relieves ribosome stalling and directs the addition of a degradation tag to the C terminus of the nascent chain. In some instances, SsrA tagging of otherwise full-length proteins occurs when the ribosome pauses at stop codons during normal translation termina...
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Published in: | The Journal of biological chemistry 2002-09, Vol.277 (37), p.33825-33832 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The SsrA or tmRNA quality control system relieves ribosome stalling and directs the addition of a degradation tag to the C
terminus of the nascent chain. In some instances, SsrA tagging of otherwise full-length proteins occurs when the ribosome
pauses at stop codons during normal translation termination. Here, the identities of the C-terminal residues of the nascent
chain are shown to play an important role in full-length protein tagging. Specifically, a subset of C-terminal Xaa-Pro sequences
caused SsrA tagging of the full-length YbeL protein from Escherichia coli . This tagging increased when a less efficient stop codon was used, increased in cells lacking protein release factor-3, and
decreased when protein release factor-1 was overexpressed. Incorporation of the analog azetidine-2-carboxylic acid in place
of proline suppressed tagging, whereas incorporation of 3,4-dehydroproline increased SsrA tagging of full-length YbeL. These
results suggest that the detailed chemical or conformational properties of the C-terminal residues of the nascent polypeptide
can affect the rate of translation termination, thereby influencing ribosome pausing and SsrA tagging at stop codons. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M205405200 |