Difference between revisions of "Part:BBa K3165007"
 
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<partinfo>BBa_K3165007 short</partinfo>
 
<partinfo>BBa_K3165007 short</partinfo>
  
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Gp2 is a bacteriophage protein (obtained from T7 bacteriophage naturally affecting <i>E. coli</i>) 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.
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Gp2 is a bacteriophage protein (obtained from T7 bacteriophage naturally affecting <i>E. coli</i>) which hinders bacterial growth by its potent activity on the bacterial RNA Polymerase by binding to the sigma <html> <sup>70</sup> </html> subunit, resulting in the misappropriation of a domain of the RNAP holoenzyme leading to hindered transcription.
  
  
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<h2> Biology </h2>
 
<h2> Biology </h2>
  
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Gp2 is a phage protein synthesized by the T7 bacteriophage that naturally infects <i>Escherichia coli</i>. The product of gene 2(Gp2) causes a bacteriostatic effect on the bacteria by its extremely potent activity on the host RNA Polymerase (the <i>E. coli</i> 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. <br>
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Gp2 is a phage protein synthesized by the T7 bacteriophage that naturally infects <i>Escherichia coli</i>. The product of gene 2(Gp2) causes a bacteriostatic effect on the bacteria by its extremely potent activity on the host RNA Polymerase (the <i>E. coli</i> RNA Polymerase in this case). Gp2 interacts reversibly with the sigma <html> <sup>70</sup> </html> domain of the RNA Polymerase preventing the normal withdrawal of the sigma <html> <sup>70</sup> </html> subunit from the RNAP active site. <br>
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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.
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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 obstructed growth. The action of Gp2 is reversible yet extremely effective. Upon stimulation, the effect of the Gp2 protein can be visualized 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.
  
 
<h2> Usage </h2>
 
<h2> Usage </h2>
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<h3> References : </h3>
 
<h3> References : </h3>
  
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(1) Phage T7 Gp2 inhibition of <i>Escherichia coli</i> RNA polymerase involves misappropriation of σ^70 domain 1.1, https://doi.org/10.1073/pnas.1314576110
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(1) Phage T7 Gp2 inhibition of <i>Escherichia coli</i> RNA Polymerase involves misappropriation of σ<sup>70</sup> domain 1.1, https://doi.org/10.1073/pnas.1314576110
  
 
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Latest revision as of 22:34, 20 October 2019


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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE 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 obstructed growth. The action of Gp2 is reversible yet extremely effective. Upon stimulation, the effect of the Gp2 protein can be visualized 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 σ70 domain 1.1, https://doi.org/10.1073/pnas.1314576110