Part:BBa_K3165007
Gp2 (Optimised for Escherichia coli)
Gp2 is a bacteriophage protein (obtained from T7 bacteriophage naturally affecting E. coli) which hinders bacterial growth by its potent activity on the bacterial RNA Polymerase by binding to the sigma^70 subunit, resulting in the misappropriation of a domain of the RNAP holoenzyme leading to hindered transcription.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Usage and Biology
Biology
Gp2 is a phage protein synthesized by the T7 bacteriophage that naturally infects Escherichia coli. The product of gene 2(Gp2) causes a bacteriostatic effect on the bacteria by its extremely potent activity on the host RNA Polymerase (the E. coli RNA Polymerase in this case). Gp2 interacts reversibly with the sigma^70 domain of the RNA Polymerase preventing the normal withdrawal of the sigma^70 subunit from the RNAP active site.
Owing to the blockage in the active site of the enzyme, the host RNA Polymerase is unable to translate the essential cellular proteins from the mRNA transcripts leading to the obstructed growth. The action of Gp2 is reversible yet extremely effective. Upon stimulation, the effect of the Gp2 protein can be visualised within around 200 seconds. Moreover, due to the low half-life of the Gp2 and its reversible activity, upon withdrawal of stimulus, the effects of Gp2 quickly diminish.
Usage
Gp2 can be used as an effective bacteriostatic growth-inhibitory protein to control bacterial cell populations. In association with an inducible system, this protein can be used as an efficient means to regulate the bacterial populations. This part can be used along with photo-sensitive systems to create optogenetically controlled genetic circuits.
References :
(1) Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ^70 domain 1.1, https://doi.org/10.1073/pnas.1314576110
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