ArticleNature communications2017
Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 54 citations in OpenAlex.
- Tail-specific protease (Tsp)-mediated envelope remodeling and beta-lactam tolerance inMicrobiology spectrum · 2026Article
- Peptidoglycan remodeling improves salt resilience ofApplied and environmental microbiology · 2026Article
- Structures of Helicobacter pylori C-terminal protease CtpA reveal a new mode of self-contained proteolytic processing.Communications biology · 2025Article
- Control of theJournal of bacteriology · 2025Article
- Periplasmic protein quality control at atomic level in live cells.Nature communications · 2025Article
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation inJournal of bacteriology · 2025Article
- A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3Molecular microbiology · 2024Article
- Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.Nature communications · 2024Article
- P. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process.The EMBO journal · 2024Article
- Glycan strand cleavage by a lytic transglycosylase, MltD contributes to the expansion of peptidoglycan in Escherichia coli.PLoS genetics · 2024Article
- Monitoring the Interaction of the Peptidoglycan with the Bacterial β-Barrel Assembly Machinery.Methods in molecular biology (Clifton, N.J.) · 2024Article
- NlpI-Prc Proteolytic Complex Mediates Peptidoglycan Synthesis and Degradation via Regulation of Hydrolases and Synthases inInternational journal of molecular sciences · 2023Article
- In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution.Nature chemical biology · 2023Article
- Article
- Cross-talk between phospholipid synthesis and peptidoglycan expansion by a cell wall hydrolase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Periplasmic Tail-Specific Protease, Tsp, Is Essential for Secondary Differentiation inJournal of bacteriology · 2023Article
- Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host interactions.Cell chemical biology · 2023Review
- Peptidoglycan Remodeling by an L,D-Transpeptidase, LdtD during Cold Shock in Escherichia coli.Journal of bacteriology · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptidoglycan (PG) is a highly cross-linked, protective mesh-like sacculus that surrounds the bacterial cytoplasmic membrane. Expansion of PG is tightly coupled to growth of a bacterial cell and requires hydrolases to cleave the cross-links for insertion of nascent PG material. In Escherichia coli, a proteolytic system comprising the periplasmic PDZ-protease Prc and the lipoprotein adaptor NlpI contributes to PG enlargement by regulating cellular levels of MepS, a cross-link-specific hydrolase. Here, we demonstrate how NlpI binds Prc to facilitate the degradation of its substrate MepS by structural and mutational analyses. An NlpI homodimer binds two molecules of Prc and forms three-sided MepS-docking cradles using its tetratricopeptide repeats. Prc forms a monomeric bowl-shaped structure with a lid-like PDZ domain connected by a substrate-sensing hinge that recognizes the bound C terminus of the substrate. In summary, our study reveals mechanistic details of protein degradation by the PDZ-protease Prc bound to its cognate adaptor protein.
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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.