Difference between revisions of "Part:BBa K598018:Design"

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===Design Notes===
 
===Design Notes===
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keep the functional characters of both proteins  
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This part is a translational fusion of TetA and GFPuv linked by a flexible peptide linker. TetA is an inner-membrane protein that consists of 12 transmembrane segments, and its N-terminus and C-terminus are exposed to the cytoplasm. TetA can retain its tetracycline-resistant phenotype when fused to other proteins at the C-terminus. GFPuv has also been fused to membrane proteins in E. coli. A flexible peptide linker sequence encoding (Gly-Gly-Gly-Ser)4 was inserted between TetA and GFPuv to facilitate proper folding of each proteins.
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===Source===
 
===Source===
  
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From Yohei Yokobayashi et al. Nucleic Acids Research, 2009, Vol. 37, No. 5
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From Yohei Yokobayashi et al.
  
 
===References===
 
===References===
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Yohei Yokobayashi et al. (2009)An efficient platform for genetic selection and screening of gene switches in Escherichia coli, Nucleic Acids Research, Vol. 37, No. 5

Latest revision as of 06:04, 5 October 2011

tetA+GFP fused protein


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 165
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 18
    Illegal BamHI site found at 311
    Illegal BamHI site found at 1786
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 337
    Illegal NgoMIV site found at 705
    Illegal NgoMIV site found at 865
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

This part is a translational fusion of TetA and GFPuv linked by a flexible peptide linker. TetA is an inner-membrane protein that consists of 12 transmembrane segments, and its N-terminus and C-terminus are exposed to the cytoplasm. TetA can retain its tetracycline-resistant phenotype when fused to other proteins at the C-terminus. GFPuv has also been fused to membrane proteins in E. coli. A flexible peptide linker sequence encoding (Gly-Gly-Gly-Ser)4 was inserted between TetA and GFPuv to facilitate proper folding of each proteins.

Source

From Yohei Yokobayashi et al.

References

Yohei Yokobayashi et al. (2009)An efficient platform for genetic selection and screening of gene switches in Escherichia coli, Nucleic Acids Research, Vol. 37, No. 5