ArticleThe Journal of biological chemistry2011
Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 31 citations in OpenAlex.
- Chemical Proteomics Strategies for Analyzing Protein Lipidation Reveal the BacterialJournal of the American Chemical Society · 2024Article
- High-throughput cell-free screening of eukaryotic membrane protein expression in lipidic mimetics.Protein science : a publication of the Protein Society · 2022Article
- Applications of Cell-Free Synthesized Membrane Protein Precipitates.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cell-Free and Yeast-Based Production of the Malarial Lactate Transporter, PfFNT, Delivers Comparable Yield and Protein Quality.Frontiers in pharmacology · 2019Article
- Identification of specific posttranslationalProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloylation in Corynebacterium glutamicum.PloS one · 2017Article
- Visualization of imbalances in sulfur assimilation and synthesis of sulfur-containing amino acids at the single-cell level.Applied and environmental microbiology · 2013Article
- Identification of a mycoloyl transferase selectively involved in O-acylation of polypeptides in Corynebacteriales.Journal of bacteriology · 2013Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PorA and PorH are two small membrane proteins from the outer membrane of Corynebacterium glutamicum, which have been shown to form heteromeric ion channels and to be post-translationally modified by mycolic acids. Any structural details of the channel could not be analyzed so far due to tremendous difficulties in the production of sufficient amounts of protein samples. Cell-free (CF) expression is a new and remarkably successful strategy for the production of membrane proteins for which toxicity, membrane targeting, and degradation are key issues. In addition, reaction conditions can easily be modified to modulate the quality of synthesized protein samples. We developed an efficient CF expression strategy to produce the channel subunits devoid of post-translational modifications. (15)N-labeled PorA and PorH samples were furthermore characterized by NMR and gave well resolved spectra, opening the way for structural studies. The comparison of ion channel activities of CF-expressed proteins with channels isolated from C. glutamicum gave clear insights on the influence of the mycolic acid modification of the two subunits on their functional properties.
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