ArticleMolecules (Basel, Switzerland)2021
A Uniform Benchmark for Testing SsrA-Derived Degrons in the
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Sequence Display enables large-scale sequence-activity datasets for rapid protein evolution.Nature biotechnology · 2026Article
- Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine.RSC chemical biology · 2026Article
- Approaches to Study Proteins Encoded by Essential Genes.Proteins · 2026Review
- Evaluation of Degron Motifs in Escherichia coli Using a Fluorescent Reporter.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Production of Purified Proteins Tagged with ssrA-Derived Degrons and Their Degradation by the Escherichia coli ClpXP System.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Targeted protein degradation in Escherichia coli using CLIPPERs.EMBO reports · 2025Article
- The final proteolytic step in transmembrane signaling of multiple RsgI anti-σ factors in Clostridium thermocellum.Bioscience reports · 2025Article
- GoldenBraid2.0Synthetic biology (Oxford, England) · 2025Article
- Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.The Plant cell · 2024Review
- 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
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The ssrA degron is commonly used in fusion proteins to control protein stability in bacteria or as an interaction module. These applications often rely on the modular activities of the ssrA tag in binding to the SspB adaptor and in engaging the ClpXP protease. However, a comparison of these activities for a substantial standard set of degron variants has not been conducted previously, which may hinder the development of new variants optimized exclusively for one application. Here, we strive to establish a benchmark that will facilitate the comparison of ssrA variants under uniform conditions. In our workflow, we included methods for expression and purification of ClpX, ClpP, SspB and eGFP-degrons, assays of ClpX ATPase activity, of eGFP-degron binding to SspB and for measuring eGFP-degron degradation in vitro and in vivo. Using uniform, precise and sensitive methods under the same conditions on a range of eGFP-degrons allowed us to determine subtle differences in their properties that can affect their potential applications. Our findings can serve as a reference and a resource for developing targeted protein degradation approaches.
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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.