ArticleProtein science : a publication of the Protein Society2021
Structural basis for the N-degron specificity of ClpS1 from Arabidopsis thaliana.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 19 citations in OpenAlex.
- Structural basis for the recognition and ubiquitylation of type-2 N-degron substrate by PRT1 plant N-recognin.Nature communications · 2025Article
- Revisiting the structure of UBR box from human UBR6.Protein science : a publication of the Protein Society · 2025Article
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis.The Plant cell · 2024Review
- Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini.Molecular cell · 2022Review
- Article
- Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for the N-degron specificity of ClpS1 from Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2021Article
- Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis.The Journal of biological chemistryReview
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7 authors at 2 institutions in 1 country.
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Abstract
The N-degron pathway determines the half-life of proteins in both prokaryotes and eukaryotes by precisely recognizing the N-terminal residue (N-degron) of substrates. ClpS proteins from bacteria bind to substrates containing hydrophobic N-degrons (Leu, Phe, Tyr, and Trp) and deliver them to the caseinolytic protease system ClpAP. This mechanism is preserved in organelles such as mitochondria and chloroplasts. Bacterial ClpS adaptors bind preferentially to Leu and Phe N-degrons; however, ClpS1 from Arabidopsis thaliana (AtClpS1) shows a difference in that it binds strongly to Phe and Trp N-degrons and only weakly to Leu. This difference in behavior cannot be explained without structural information due to the high sequence homology between bacterial and plant ClpS proteins. Here, we report the structure of AtClpS1 at 2.0 Å resolution in the presence of a bound N-degron. The key determinants for α-amino group recognition are conserved among all ClpS proteins, but the α3-helix of eukaryotic AtClpS1 is significantly shortened, and consequently, a loop forming a pocket for the N-degron is moved slightly outward to enlarge the pocket. In addition, amino acid replacement from Val to Ala causes a reduction in hydrophobic interactions with Leu N-degron. A combination of the fine-tuned hydrophobic residues in the pocket and the basic gatekeeper at the entrance of the pocket controls the N-degron selectivity of the plant ClpS protein.
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