Part:BBa_K1317001

CDS for resilin-like polypeptide (RLP)

This part is the coding sequence for the resilin like polypeptide. This sequence was assembled from a consensus of the proresilin exon 1 from Drosophila melanogaster. This protein, in insects, allows resistance and elasticity used for jumping, flapping... The synthetic gene encodes a synthetic protein "resilin-like". The repeated aminoacids allow to retrieve these properties of resistance, resilience and elasticity, but with a minimal pattern of the original protein, which is more suited for downstream applications. It can be used to produce wire presenting these properties after wet-spinning.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal NheI site found at 300
  
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

References

[1] Tamburro A.M. et al. Molecular and supramolecular structural studies on significant repetitive sequences of resilin (2010) Chembiochem., 11(1), 83-93. doi: 10.1002/cbic.200900460.

[2] Linqing Li et Kristi L. Kiick. Resilin-Based Materials for Biomedical Applications (2013) ACS Macro Lett., 2(8), 635–640. doi: 10.1021/mz4002194.

[3] David H. Ardell and Svend Olav Andersen Tentative identification of a resilin gene in Drosophila melanogaster Insect Biochemistry and Molecular Biology 31 (2001) 965–970

[4] Julie N. Renner et al. Characterization of Resilin-Based Materials for Tissue Engineering Applications Biomacromolecules 2012, 13, 3678−3685

[5] Russell E. Lyons et al. Comparisons of Recombinant Resilin-like Proteins: Repetitive Domains Are Sufficient to Confer Resilin-like Properties Biomacromolecules 2009, 10, 3009–3014

[6] M. Kim et al. High yield expression of recombinant pro-resilin: Lactose-induced fermentation in E. coli and facile purification Protein Expression and Purification 52 (2007) 230–236

[7] Christopher M. Elvin et al. Synthesis and properties of crosslinked recombinant pro-resilin Vol 437|13 October 2005|doi:10.1038/nature04085