ArticleBMC biotechnology2013
Strategy for successful expression of the Pseudomonas putida nitrile hydratase activator P14K in Escherichia coli.
Article in BMC biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Recent Advances and Promises in Nitrile Hydratase: From Mechanism to Industrial Applications.Frontiers in bioengineering and biotechnology · 2020Review
- Maturation Mechanism of Nitrile Hydratase FromFrontiers in microbiology · 2020Article
- Advances in cloning, structural and bioremediation aspects of nitrile hydratases.Molecular biology reports · 2019Review
- Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.PloS one · 2017Article
- Successful expression of the Bordetella petrii nitrile hydratase activator P14K and the unnecessary role of Ser115.BMC biotechnology · 2016Article
- Construction of a subunit-fusion nitrile hydratase and discovery of an innovative metal ion transfer pattern.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundActivators of Nitrile hydratase (NHase) are essential for functional NHase biosynthesis. However, the activator P14K in P. putida is difficult to heterogeneously express, which retards the clarification of the mechanism of P14K involved in the maturation of NHase. Although a strep tag containing P14K (strep-P14K) was over-expressed, its low expression level and low stability affect the further analysis.
resultsWe successfully expressed P14K through genetic modifications according to N-end rule and analyzed the mechanism for its difficult expression. We found that mutation of the second N-terminal amino-acid of the protein from lysine to alanine or truncating the N-terminal 16 amino-acid sequence resulted in successful expression of P14K. Moreover, fusion of a pelB leader and strep tag together (pelB-strep-P14K) at the N-terminus increased P14K expression. In addition, the pelB-strep-P14K was more stable than the strep-P14K.
conclusionsOur results are not only useful for clarification of the role of P14K involved in the NHase maturation, but also helpful for heterologous expression of other difficult expression proteins.
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