ArticleThe Journal of biological chemistry2012
Multiple post-translational modifications affect heterologous protein synthesis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 89 citations in OpenAlex.
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- Bacterial two-hybrid systems evolved: innovations for protein-protein interaction research.Journal of bacteriology · 2025Review
- Theoretical Investigation of the Material Usage During On-Bead Enrichment of Post-Translationally Modified Peptides in Suspension Systems.Molecules (Basel, Switzerland) · 2025Article
- Harnessing Transient Expression Systems with Plant Viral Vectors for the Production of Biopharmaceuticals inInternational journal of molecular sciences · 2025Review
- The Bioengineering of Insect Cell Lines for Biotherapeutics and Vaccine Production: An Updated Review.Vaccines · 2025Review
- The Application of DNA Viruses to Biotechnology.Viruses · 2025Review
- Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost.Protein science : a publication of the Protein Society · 2025Article
- Nonenzymatic Posttranslational Modifications and Peptide Cleavages Observed in Peptide Epimers.Journal of the American Society for Mass Spectrometry · 2023Article
- Usage of Cell-Free Protein Synthesis in Post-Translational Modification of μ-Conopeptide PIIIA.Marine drugs · 2023Article
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- Optimization, characterization, comparison of self-assembly VLP of capsid protein L1 in yeast and reverse vaccinology design against human papillomavirus type 52.Journal, genetic engineering & biotechnology · 2023Article
- Fundamental concepts of protein therapeutics and spacing in oncology: an updated comprehensive review.Medical oncology (Northwood, London, England) · 2023Review
- Steric pressure between glycosylated transmembrane proteins inhibits internalization by endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Heterologous Expression of Xylanase xAor from Aspergillus oryzae in Komagataella phaffii T07International journal of molecular sciences · 2022Article
- Pseudomonas response regulators produced in an E. coli heterologous expression host exhibit host-derived post-translational phosphorylation.Scientific reports · 2022Article
- Cortactin in Lung Cell Function and Disease.International journal of molecular sciences · 2022Review
- Reductive site-selective atypicalScience advances · 2022Article
- Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications (PTMs) are required for proper folding of many proteins. The low capacity for PTMs hinders the production of heterologous proteins in the widely used prokaryotic systems of protein synthesis. Until now, a systematic and comprehensive study concerning the specific effects of individual PTMs on heterologous protein synthesis has not been presented. To address this issue, we expressed 1488 human proteins and their domains in a bacterial cell-free system, and we examined the correlation of the expression yields with the presence of multiple PTM sites bioinformatically predicted in these proteins. This approach revealed a number of previously unknown statistically significant correlations. Prediction of some PTMs, such as myristoylation, glycosylation, palmitoylation, and disulfide bond formation, was found to significantly worsen protein amenability to soluble expression. The presence of other PTMs, such as aspartyl hydroxylation, C-terminal amidation, and Tyr sulfation, did not correlate with the yield of heterologous protein expression. Surprisingly, the predicted presence of several PTMs, such as phosphorylation, ubiquitination, SUMOylation, and prenylation, was associated with the increased production of properly folded soluble proteins. The plausible rationales for the existence of the observed correlations are presented. Our findings suggest that identification of potential PTMs in polypeptide sequences can be of practical use for predicting expression success and optimizing heterologous protein synthesis. In sum, this study provides the most compelling evidence so far for the role of multiple PTMs in the stability and solubility of heterologously expressed recombinant proteins.
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