Part:BBa_K5115002
EP
Contents
Introduction
Hpn encodes a nickel-binding protein crucial for maintaining nickel homeostasis in Helicobacter pylori. With its high histidine content, Hpn plays a vital role in sequestering nickel ions, preventing toxicity while ensuring proper nickel transfer to urease. This process is essential for the activation of urease, an enzyme that enables H. pylori to colonize the acidic gastric environment.[1].
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| Figure 1. The biosynthetic pathway of shinorine, porphyra-334, palythine-Ser, and palythine-Thr |
Usage and Biology
We performed codon optimization specifically for the Escherichia coli K12 strain, resulting in the creation of this part. The Hpn protein binds absorbed nickel ions, enhancing E. coli's tolerance to elevated nickel concentrations within E. coli.
Characterization
Nickel tolerance Assay
We.
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| Figure 2. Anti-UV Assay. |
Our experiments demonstrated that expressing Hpn in E. coli significantly enhanced the bacterium's ability to absorb nickel ions. We hypothesize that this increased absorption is due to Hpn’s strong nickel-binding capacity. However, for optimal nickel uptake, other factors, such as the availability of additional nickel transporters or regulatory proteins, may also be necessary.
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| Figure 3. Plates displaying transformed E. coli after anti-UV assay. |
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 228
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
- ↑ Vinella, D., Fischer, F., Vorontsov, E., Gallaud, J., Malosse, C., Michel, V., Cavazza, C., Robbe-Saule, M., Richaud, P., Chamot-Rooke, J., Brochier-Armanet, C., & De Reuse, H. (2015). Evolution of Helicobacter: Acquisition by Gastric Species of Two Histidine-Rich Proteins Essential for Colonization. PLoS pathogens, 11(12), e1005312.
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