Design and facile production of recombinant resilin-like polypeptides: gene construction and a rapid protein purification method

Lyons, Russell E., Lesieur, Emmanuelle, Kim, Misook, Wong, Darren C. C., Huson, Mickey G., Nairn, Kate M., Brownlee, Alan G., Pearson, Roger D. and Elvin, Christopher M. (2007) Design and facile production of recombinant resilin-like polypeptides: gene construction and a rapid protein purification method. Protein Engineering Design & Selection, 20 1: 25-32. doi:10.1093/protein/gzl050


Author Lyons, Russell E.
Lesieur, Emmanuelle
Kim, Misook
Wong, Darren C. C.
Huson, Mickey G.
Nairn, Kate M.
Brownlee, Alan G.
Pearson, Roger D.
Elvin, Christopher M.
Title Design and facile production of recombinant resilin-like polypeptides: gene construction and a rapid protein purification method
Journal name Protein Engineering Design & Selection   Check publisher's open access policy
ISSN 1741-0126
1741-0134
Publication date 2007-01-11
Year available 2007
Sub-type Article (original research)
DOI 10.1093/protein/gzl050
Open Access Status DOI
Volume 20
Issue 1
Start page 25
End page 32
Total pages 8
Place of publication Oxford (Oxfordshire)
Publisher Oxford University Press
Language eng
Subject 0601 Biochemistry and Cell Biology
Abstract Resilin is an elastic protein found in specialized regions of the cuticle of insects, which displays unique resilience and fatigue lifetime properties. As is the case with many elastomeric proteins, including elastin, gliadin and spider silks, resilin contains distinct repetitive domains that appear to confer elastic properties to the protein. Recent work within our laboratory has demonstrated that cloning and expression of exon 1 of the Drosophila melanogaster CG15920 gene, encoding a putative resilin-like protein, results in a recombinant protein that can be photochemically crosslinked to form a highly resilient, elastic biomaterial (Rec1 resilin). The current study describes a recursive cloning strategy for generating synthetic genes encoding multiple copies of consensus polypeptides, based on the repetitive domains within resilin-like genes from D. melanogaster and Anopheles gambiae. A simple non-chromatographic purification method that can be applied to these synthetic proteins and Rec1 is also reported. These methods for the design and purification of resilin-like periodic polypeptides will facilitate the future investigation of structural and functional properties of resilin, and the development of novel highly resilient biomaterials.
Keyword Biochemistry & Molecular Biology
Biotechnology & Applied Microbiology
Biochemistry & Molecular Biology
Biotechnology & Applied Microbiology
BIOCHEMISTRY & MOLECULAR BIOLOGY
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Q-Index Code C1
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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