Difference between revisions of "Part:BBa K422001"
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<partinfo>BBa_K422001 short</partinfo>
 
<partinfo>BBa_K422001 short</partinfo>
  
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===Biological Background===
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<span class='h3bb'>Sequence and Features</span>
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Fusion of the ''Natronobacterium pharaonis'' Np seven-transmembrane retinylidene photoreceptor sensory rhodopsins II NpSRII and their cognate transducer HtrII to the cytoplasmic domain of the chemotaxis transducer EcTsr of ''Escherichia coli'' [1].
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<partinfo>BBa_K422001 SequenceAndFeatures</partinfo>
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Rhodopsins are photoreactive, membrane-embedded proteins, which are found not only in archaea, but in eubacteria and microbes as well. In ''Natronobacterium pharaonis'', the NpSRII contains a domain of seven membrane-spanning helices, which carry out two distinct functions: Firstly, they serve as photo-inducible ion-pumps and secondly, as actors in the chemotaxis signaling network [1].
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All-trans retinal is needed for NpSRII to change it's conformation into an active light absorbing pigment. It can either be added to the growth media or produced by the organism. Phototactic stimuli can be delivered through a light pulse at 500 nm.
  
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===Usage and Biology===
 
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Fusion of the Natronobacterium pharaonis Np seven-transmembrane retinylidene photoreceptor sensory rhodopsins II NpSRII and their cognate transducer HtrII to the cytoplasmic domain of the chemotaxis transducer EcTsr of Escherichia coli.
 
  
 
===Design===
 
===Design===
 
De novo Synthesis by GeneArt. Codon optimized.
 
De novo Synthesis by GeneArt. Codon optimized.
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===Characterization===
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===References===
 
===References===
 
[1] Jung, Spudich, Trivedi and Spudich: An archaeal photosignal-transducing module mediates phototaxis in Escherichia coli. Journal of bacteriology. 2001; 21.
 
[1] Jung, Spudich, Trivedi and Spudich: An archaeal photosignal-transducing module mediates phototaxis in Escherichia coli. Journal of bacteriology. 2001; 21.
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K422001 SequenceAndFeatures</partinfo>

Revision as of 11:53, 27 October 2010

Archeal light receptor fused to bacterial chemotaxis transducer

Biological Background

Fusion of the Natronobacterium pharaonis Np seven-transmembrane retinylidene photoreceptor sensory rhodopsins II NpSRII and their cognate transducer HtrII to the cytoplasmic domain of the chemotaxis transducer EcTsr of Escherichia coli [1].

Rhodopsins are photoreactive, membrane-embedded proteins, which are found not only in archaea, but in eubacteria and microbes as well. In Natronobacterium pharaonis, the NpSRII contains a domain of seven membrane-spanning helices, which carry out two distinct functions: Firstly, they serve as photo-inducible ion-pumps and secondly, as actors in the chemotaxis signaling network [1].

All-trans retinal is needed for NpSRII to change it's conformation into an active light absorbing pigment. It can either be added to the growth media or produced by the organism. Phototactic stimuli can be delivered through a light pulse at 500 nm.


Design

De novo Synthesis by GeneArt. Codon optimized.


Characterization

References

[1] Jung, Spudich, Trivedi and Spudich: An archaeal photosignal-transducing module mediates phototaxis in Escherichia coli. Journal of bacteriology. 2001; 21.



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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 747
    Illegal AgeI site found at 840
  • 1000
    COMPATIBLE WITH RFC[1000]