ArticleProceedings of the National Academy of Sciences of the United States of America2019
Timing and specificity of cotranslational nascent protein modification in bacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- HYPK promotes N-terminal protein acetylation through rapid ribosome exchange of NatA.Molecular cell · 2025Article
- Destined for destruction: The role of methionine aminopeptidases and plant cysteine oxidases in N-degron formation.Plant physiology · 2024Review
- STIC2 selectively binds ribosome-nascent chain complexes in the cotranslational sorting of Arabidopsis thylakoid proteins.The EMBO journal · 2024Article
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- Article
- Hold the fold: how delayed folding aids protein secretion.The EMBO journal · 2022Article
- System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity.iScience · 2022Article
- Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes.Annual review of biomedical data science · 2022Review
- Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification.Journal of molecular biology · 2022Article
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Kinetic control of nascent protein biogenesis by peptide deformylase.Scientific reports · 2021Article
- Regulation of ribosomal protein genes: An ordered anarchy.Wiley interdisciplinary reviews. RNA · 2021Review
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex.Nature communications · 2020Article
- Regulation of translation by one-carbon metabolism in bacteria and eukaryotic organelles.The Journal of biological chemistryReview
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Authors and funding
3 authors.
Funding
Abstract
The nascent polypeptide exit site of the ribosome is a crowded environment where multiple ribosome-associated protein biogenesis factors (RPBs) compete for the nascent polypeptide to influence their localization, folding, or quality control. Here we address how N-terminal methionine excision (NME), a ubiquitous process crucial for the maturation of over 50% of the bacterial proteome, occurs in a timely and selective manner in this crowded environment. In bacteria, NME is mediated by 2 essential enzymes, peptide deformylase (PDF) and methionine aminopeptidase (MAP). We show that the reaction of MAP on ribosome-bound nascent chains approaches diffusion-limited rates, allowing immediate methionine excision of optimal substrates after deformylation. Specificity is achieved by kinetic competition of NME with translation elongation and by regulation from other RPBs, which selectively narrow the processing time window for suboptimal substrates. A mathematical model derived from the data accurately predicts cotranslational NME efficiency in the cytosol. Our results demonstrate how a fundamental enzymatic activity is reshaped by its associated macromolecular environment to optimize both efficiency and selectivity, and provides a platform to study other cotranslational protein biogenesis pathways.
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