1998
DOI: 10.1101/gad.12.9.1338
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The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

Abstract: Interruption of translation in Escherichia coli can lead to the addition of an 11-residue carboxy-terminal peptide tail to the nascent chain. This modification is mediated by SsrA RNA (also called 10Sa RNA and tmRNA) and marks the tagged polypeptide for proteolysis. Degradation in vivo of repressor amino-terminal domain variants bearing this carboxy-terminal SsrA peptide tag is shown here to depend on the cytoplasmic proteases ClpXP and ClpAP. Degradation in vitro of SsrA-tagged substrates was reproduced with … Show more

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Cited by 763 publications
(823 citation statements)
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“…N-end rule) (Bohley, 1996;Varshavsky et al, 2000;Withey & Friedman, 2003;Devoy et al, 2005). The small stable RNA A (SsrA) proteintagging system is found in all bacterial genomes (Keiler et al, 2000) and employs a transfer-messenger RNA (tmRNA) to add an 11-residue sequence (-AANDE-NYALAA) to the end of stalled translation products, thus conveying a proteolytic targeting signal for Clp proteases (Gottesman et al, 1998;Withey & Friedman, 2003). The N-end rule, described in bacteria and eukaryotes, predicts the half-life of a protein based on its extreme N-terminal residue (N-degron) (Varshavsky et al, 2000).…”
Section: Introductionmentioning
confidence: 99%
“…N-end rule) (Bohley, 1996;Varshavsky et al, 2000;Withey & Friedman, 2003;Devoy et al, 2005). The small stable RNA A (SsrA) proteintagging system is found in all bacterial genomes (Keiler et al, 2000) and employs a transfer-messenger RNA (tmRNA) to add an 11-residue sequence (-AANDE-NYALAA) to the end of stalled translation products, thus conveying a proteolytic targeting signal for Clp proteases (Gottesman et al, 1998;Withey & Friedman, 2003). The N-end rule, described in bacteria and eukaryotes, predicts the half-life of a protein based on its extreme N-terminal residue (N-degron) (Varshavsky et al, 2000).…”
Section: Introductionmentioning
confidence: 99%
“…Numerous experiments have shown that mutation of residues in degrons to aspartic acid also weakens binding to the translocation pore of ClpX. 7,33 Testing these ideas will require further analysis as the Cc SspB variants used in this study are not ideally suited for degradation experiments because they carry N-terminal affinity tags.…”
Section: Discussionmentioning
confidence: 99%
“…37 Moreover, other AAAþ proteases interact with multiple types of peptide signals to identify the correct substrates. 7,[38][39][40][41][42][43][44][45] The AAAþ p97 protein also employs its N domain to interact with disparate sequences in a wide variety of adaptors. 46 The peptide-binding versatility exhibited by the ClpX N domain and SspB ensures that ClpXP can recognize many different substrates and adaptors in different ways but with high specificity.…”
Section: Discussionmentioning
confidence: 99%
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