Difference between revisions of "Part:BBa K3198003"
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<partinfo>BBa_K3198003 short</partinfo>
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<partinfo>BBa_K3198002 short</partinfo>
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This part contains the toxin component of a type II toxin-antitoxin (TA) system. HicA is a probable translation-independent mRNA interferase.<br><br> -->
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<!-- This part contains the toxin component of a type II toxin-antitoxin (TA) system. HicA is a probable translation-independent mRNA interferase.<br><br> -->
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<br><br>
  
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K3198003 SequenceAndFeatures</partinfo>
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<partinfo>BBa_K3198002 SequenceAndFeatures</partinfo>
  
 
===Usage===
 
===Usage===
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It is demonstrated that the res-xre locus from Photorhabdus luminescens and other bacterial species function as bona fide TA modules in Escherichia coli.
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It is demonstrated that researchers that the RES-Xre locus from </i>Photorhabdus luminescens</i> and other bacterial species function as bona fide TA modules in <i>Escherichia coli</i>.  
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<br><br>
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The activation of the toxin in vivo causes a depletion of intracellular NAD+ levels, eventually leading to inhibition of cell growth in <i>E. coli</i> and inhibition of global macromolecular biosynthesis.  
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It was shown that a RES toxin encoded by the α‐proteobacterium, <i>Sinorhizobium meliloti</i>, is toxic when expressed in Escherichia coli and can be counteracted by its cognate Xre antitoxin.
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<br><br>
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RES toxin from several bacterial species reversibly inhibits cell growth in <i>E. coli</i>, and that expression of the Xre antitoxin neutralizes this toxicity. However, the cellular function of the RES toxin when activated, as well as structure and the antitoxic mechanism of the Xre antitoxin, remain unknown.
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===Biology===
 
===Biology===
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This part is from the res-xre locus from <i>Photorhabdus luminescens</i> and other bacterial species.
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This part is from the res-xre locus from Photorhabdus luminescens and other bacterial species.
  
  
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===Characterisation===
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===Characterization===
 
<!-- Team NUS 2019 has added a new biobrick (BBa_K3198000) into the iGEM repository this year. This biobrick was found to possess a bacteriostatic effect as reported by Gerdes et al in 2008 (doi:10.1128/JB.01013-08) and was therefore used by Team NUS 2019 as part of their sleep-wake module to control the growth of E. coli in their project.
 
<!-- Team NUS 2019 has added a new biobrick (BBa_K3198000) into the iGEM repository this year. This biobrick was found to possess a bacteriostatic effect as reported by Gerdes et al in 2008 (doi:10.1128/JB.01013-08) and was therefore used by Team NUS 2019 as part of their sleep-wake module to control the growth of E. coli in their project.
 
<br><br>(BBa_K3198000) was placed under an IPTG-inducible promoter and various IPTG concentrations were utilized to determine their effect on the growth of native <i>MG1655</i>. In the same plasmid, another cassette containing GFP reporter gene under constitutive promoter was present to enable characterization of the effect of HicA on protein production.   
 
<br><br>(BBa_K3198000) was placed under an IPTG-inducible promoter and various IPTG concentrations were utilized to determine their effect on the growth of native <i>MG1655</i>. In the same plasmid, another cassette containing GFP reporter gene under constitutive promoter was present to enable characterization of the effect of HicA on protein production.   
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===References===
 
===References===
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Milunovic, B., diCenzo, G.C., Morton, R.A.and Finan, T.M. (2014) Cell growth inhibition upon deletion of four toxin‐antitoxin loci from the megaplasmids of Sinorhizobium meliloti. Journal of Bacteriology, 196, 811–824.
 
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<br><br>
 
 
Skjerning, R. B., Senissar, M., Winther, K. S., Gerdes, K., & Brodersen, D. E. (2018). The RES domain toxins of RES-Xre toxin-antitoxin modules induce cell stasis by degrading NAD . Molecular Microbiology, 111(1), 221–236. doi: 10.1111/mmi.14150
 
Skjerning, R. B., Senissar, M., Winther, K. S., Gerdes, K., & Brodersen, D. E. (2018). The RES domain toxins of RES-Xre toxin-antitoxin modules induce cell stasis by degrading NAD . Molecular Microbiology, 111(1), 221–236. doi: 10.1111/mmi.14150
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<br><br>
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Milunovic, B., diCenzo, G.C., Morton, R.A.and Finan, T.M. (2014) Cell growth inhibition upon deletion of four toxin‐antitoxin loci from the megaplasmids of Sinorhizobium meliloti. Journal of Bacteriology, 196, 811–824.
  
 
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Revision as of 10:13, 31 August 2019


RES



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

It is demonstrated that researchers that the RES-Xre locus from </i>Photorhabdus luminescens</i> and other bacterial species function as bona fide TA modules in Escherichia coli. The activation of the toxin in vivo causes a depletion of intracellular NAD+ levels, eventually leading to inhibition of cell growth in E. coli and inhibition of global macromolecular biosynthesis.


Biology

This part is from the res-xre locus from Photorhabdus luminescens and other bacterial species.


Characterization

References

Skjerning, R. B., Senissar, M., Winther, K. S., Gerdes, K., & Brodersen, D. E. (2018). The RES domain toxins of RES-Xre toxin-antitoxin modules induce cell stasis by degrading NAD . Molecular Microbiology, 111(1), 221–236. doi: 10.1111/mmi.14150

Milunovic, B., diCenzo, G.C., Morton, R.A.and Finan, T.M. (2014) Cell growth inhibition upon deletion of four toxin‐antitoxin loci from the megaplasmids of Sinorhizobium meliloti. Journal of Bacteriology, 196, 811–824.