Coding

Part:BBa_K163001:Design

Designed by: Daniel M. Choi   Group: iGEM08_University_of_Chicago   (2008-10-11)


Mussel adhesive protein from Mytilus Edulis (Mefp-5) optimized for Caulobacter


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 1
    Illegal SpeI site found at 318
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 1
    Illegal SpeI site found at 318
    Illegal NotI site found at 7
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 1
    Illegal BglII site found at 338
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 1
    Illegal SpeI site found at 318
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal prefix found in sequence at 1
    Illegal SpeI site found at 318
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

This sequence has been codon-optimized for production in Caulobacter. Mefp-5 contains over 20% molar concentration of L-DOPA, the highest DOPA content of known adhesive proteins secreted by Mytilus Edulis. Mefp-5 also has strong anti-biofouling properties, that could possibly be utilized by such things like pacemakers or heart monitors. Mefp-5 is difficult to obtain from purification of mussel proteins, so being able to obtain Mefp-5 from genetic engineering methods will allow researchers to better learn its properties.


Source

Waite, et al. "Polyphosphoprotein from the adhesive pads of Mytilus edulis" Biochemistry 40 (9), 2887-2893 (2001). Nucleotide sequence from GeneBank, accession number AF333078

References