ArticleMicrobial cell (Graz, Austria)
Formyl-methionine as a degradation signal at the N-termini of bacterial proteins.
Article in Microbial cell (Graz, Austria). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 86 citations in OpenAlex.
- TRAINSPOTTER: profiling nascent protein N-termini indicative of bacterial translation initiation via deformylation-assisted N-terminomics.Nucleic acids research · 2026Article
- N-terminal formylmethionine as a degron and a specific signal in proteostasis and stress adaptation.Experimental & molecular medicine · 2026Review
- Decreasing peptide deformylase activity is a beneficial strategy for increasing formaldehyde resistance inbioRxiv : the preprint server for biology · 2026Article
- Integrated Phylogenomics and Expression Profiling of the Peptide Deformylase Gene Family inCurrent issues in molecular biology · 2026Article
- Unraveling the Prevalence and Multifaceted Roles of Accessory Peptide Deformylases in Bacterial Adaptation and Resistance.Molecular biology and evolution · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity.Science (New York, N.Y.) · 2025Article
- Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- Global protein turnover quantification in Escherichia coli reveals cytoplasmic recycling under nitrogen limitation.Nature communications · 2024Article
- Prebiotic Synthesis ofJournal of the American Chemical Society · 2023Article
- Revealing Corynebacterium glutamicum proteoforms through top-down proteomics.Scientific reports · 2023Article
- Efficient recombinant production of mouse-derived cryptdin family peptides by a novel facilitation strategy for inclusion body formation.Microbial cell factories · 2023Article
- Article
- System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity.iScience · 2022Article
- Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification.Journal of molecular biology · 2022Article
- How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini.Molecular cell · 2022Review
- A hundred spotlights on microbiology: how microorganisms shape our lives.Microbial cell (Graz, Austria) · 2022Article
- The ins and outs of Bacillus proteases: activities, functions and commercial significance.FEMS microbiology reviews · 2022Review
- Codon usage bias.Molecular biology reports · 2022Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
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Abstract
In bacteria, all nascent proteins bear the pretranslationally formed N-terminal formyl-methionine (fMet) residue. The fMet residue is cotranslationally deformylated by a ribosome-associated deformylase. The formylation of N-terminal Met in bacterial proteins is not strictly essential for either translation or cell viability. Moreover, protein synthesis by the cytosolic ribosomes of eukaryotes does not involve the formylation of N-terminal Met. What, then, is the main biological function of this metabolically costly, transient, and not strictly essential modification of N-terminal Met, and why has Met formylation not been eliminated during bacterial evolution? One possibility is that the similarity of the formyl and acetyl groups, their identical locations in N-terminally formylated (Nt-formylated) and Nt-acetylated proteins, and the recently discovered proteolytic function of Nt-acetylation in eukaryotes might also signify a proteolytic role of Nt-formylation in bacteria. We addressed this hypothesis about fMet-based degradation signals, termed fMet/N-degrons, using specific
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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.