Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
Abstract
Variants of lambda repressor and cytochrome b562 translated from messenger RNAs without stop codons were modified by carboxyl terminal addition of an ssrA-encoded peptide tag and subsequently degraded by carboxyl terminal-specific proteases present in both the cytoplasm and periplasm of Escherichia coli. The tag appears to be added to the carboxyl terminus of the nascent polypeptide chain by cotranslational switching of the ribosome from the damaged messenger RNA to ssrA RNA.
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The N-end rule and the SsrA tag are the best characterized mechanisms by which bacterial proteases recognize substrates.
“Currently, the most well characterized mechanisms for substrate recognition by bacterial proteases are the N-end rule and the SsrA tag.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [55]
The SsrA tag is an eleven-amino-acid tag added to the carboxy-terminus of incompletely translated proteins and marks them for degradation.
“The N-end rule relates the half-life of a protein to the N-terminal amino acid while the SsrA tag is an eleven amino acid tag that is added to the carboxy-terminus of incompletely translated proteins relegating them to degradation [54–55].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [55]
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- Authors
- Keiler, K. C., Waller, P. R. H., & Sauer, R. T.
- Affiliations
- Massachusetts Institute of Technology (US)
- Corresponding author
- Sauer, Robert T.
- Venue
- Science
- Published
- 1996-02-16
- Volume
- 271
- Issue
- 5251
- Pages
- 990-993
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2084140927
- Cited by
- 1,125
- References
- 28
- Citations by year
- 2026: 27 · 2025: 24 · 2024: 34 · 2023: 22 · 2022: 33 · 2021: 36 · 2020: 36 · 2019: 27 · 2018: 26 · 2017: 39 · 2016: 27 · 2015: 24 · 2014: 42 · 2013: 31 · 2012: 34
- FWCI
- 15.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI15706, R01AI016892, AI‑16892)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- ssrA, ribosome stalling, protein degradation, lambda repressor, cytochrome b562, Escherichia coli
- MeSH terms
- Alanine, Amino Acid Sequence, Base Sequence, Cloning, Molecular, Cytochrome b Group, DNA-Binding Proteins, Escherichia coli, Molecular Sequence Data, Endopeptidases, Peptides, Protein Processing, Post-Translational, Repressor Proteins, RNA, Bacterial, RNA, Messenger, Protein Biosynthesis, Viral Proteins, Codon, Terminator, Escherichia coli Proteins, Viral Regulatory and Accessory Proteins
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