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PMID:28446197
| Citation |
Yung, MC, Bourguet, FA, Carpenter, TS and Coleman, MA (2017) Re-directing bacterial microcompartment systems to enhance recombinant expression of lysis protein E from bacteriophage ϕX174 in Escherichia coli. Microb. Cell Fact. 16:71 |
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| Abstract |
Recombinant expression of toxic proteins remains a challenging problem. One potential method to shield toxicity and thus improve expression of these proteins is to encapsulate them within protein compartments to sequester them away from their targets. Many bacteria naturally produce so-called bacterial microcompartments (BMCs) in which enzymes comprising a biosynthetic pathway are encapsulated in a proteinaeous shell, which is in part thought to shield the cells from the toxicity of reaction intermediates. As a proof-of-concept, we attempted to encapsulate toxic, lysis protein E (E) from bacteriophage ϕX174 inside recombinant BMCs to enhance its expression and achieve higher yields during downstream purification. |
| Links |
PubMed PMC5405515 Online version:10.1186/s12934-017-0685-x |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004857: enzyme inhibitor activity |
ECO:0000314: |
F |
Table 3 shows the activity levels of B. licheniformis. The activity percentages show how growth is inhibited by 0.5 µM of the E protein when compared to the normal growth of B. licheniformis after 6 hours. The table shows PduP-E from Ec3087 having the greatest inhibition after induction of 0.1 mM Rha. |
complete | ||||
Notes
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