ArticleProceedings of the National Academy of Sciences of the United States of America2008
Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
46 citing papers in PubMed, 72 citations in OpenAlex.
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Approaches to Study Proteins Encoded by Essential Genes.Proteins · 2026Review
- Synthetic Biology of Plants and Microbes for Agriculture, Environment, and Future Applications.Chemical reviews · 2026Review
- Assembly of Macromolecular Complexes in the Whole-Cell Model of a Minimal Cell.The journal of physical chemistry. B · 2026Article
- SsrA-Based Targeted Protein Degradation in Escherichia coli.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- State-of-the-art in engineering small molecule biosensors and their applications in metabolic engineering.SLAS technology · 2024Review
- A system for inducible mitochondria-specific protein degradation in vivo.Nature communications · 2024Article
- Review
- Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023Article
- Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.Cell reports · 2023Article
- The Molecular Toolset and Techniques Required to Build Cyanobacterial Cell Factories.Advances in biochemical engineering/biotechnology · 2023Article
- Rewiring cell-free metabolic flux inSynthetic biology (Oxford, England) · 2023Article
- Bacterial degrons in synthetic circuits.Open biology · 2022Review
- Improving the Robustness of Engineered Bacteria to Nutrient Stress Using Programmed Proteolysis.ACS synthetic biology · 2022Article
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
- Widespread ribosome stalling in a genome-reduced bacterium and the need for translational quality control.iScience · 2021Article
- A lysate proteome engineering strategy for enhancing cell-free metabolite production.Metabolic engineering communications · 2021Article
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Impact of C-terminal amino acid composition on protein expression in bacteria.Molecular systems biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Stalled ribosomes in bacteria are rescued by the tmRNA system. In this process, the nascent polypeptide is modified by the addition of a short C-terminal sequence called the ssrA tag, which is encoded by tmRNA and allows normal termination and release of ribosomal subunits. In most bacteria, ssrA-tagged proteins are degraded by the AAA+ protease, ClpXP. However, in bacterial species of the genus Mycoplasma, genes for ClpXP and many other proteins were lost through reductive evolution. Interestingly, Mycoplasma ssrA tag sequences are very different from the tags in other bacteria. We report that ssrA-tagged proteins in Mesoplasma florum, a Mycoplasma species, are efficiently recognized and degraded by the AAA+ Lon protease. Thus, retaining degradation of ssrA-tagged translation products was apparently important enough during speciation of Mycoplasma to drive adaptation of the ssrA tag to a different protease. These results emphasize the importance of coupling proteolysis with tmRNA-mediated tagging and ribosome rescue.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.