Rapid isolation of novel FK506 binding proteins from multiple organisms using gDNA and cDNA T7 phage display

Piggott, A. M., Kriegel, A. M., Willows, R. D. and Karuso, P (2009) Rapid isolation of novel FK506 binding proteins from multiple organisms using gDNA and cDNA T7 phage display. Bioorganic & Medicinal Chemistry, 17 19: 6841-6850. doi:10.1016/j.bmc.2009.08.039


Author Piggott, A. M.
Kriegel, A. M.
Willows, R. D.
Karuso, P
Title Rapid isolation of novel FK506 binding proteins from multiple organisms using gDNA and cDNA T7 phage display
Journal name Bioorganic & Medicinal Chemistry   Check publisher's open access policy
ISSN 0968-0896
Publication date 2009-10-01
Year available 2009
Sub-type Article (original research)
DOI 10.1016/j.bmc.2009.08.039
Volume 17
Issue 19
Start page 6841
End page 6850
Total pages 10
Editor Dr. Chi-Huey Wong
Place of publication Oxford, United Kingdom
Publisher Pergamon (Elsevier)
Language eng
Subject C1
Formatted abstract
Reverse chemical proteomics using T7 phage display is a powerful technique for identifying cellular receptors of biologically active small molecules. However, to date this method has generally been limited to cDNA libraries constructed from mRNA isolated from eukaryotes. In this paper, we describe the construction of the first prokaryotic T7 phage display libraries from randomly digested Pseudomonas stutzeri and Vibrio fischeri gDNA, as well as a plant cDNA library from Arabidopsis thaliana. We also describe the use of T7 phage display to identify novel proteins from environmental DNA samples using biotinylated FK506 as a model affinity probe.
Keyword T7 Phage Display
reverse chemical proteomics
Prokaryotic gDNA library
FKBP-FK506
Biotinylation
Natural Product
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 6 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 20 Apr 2010, 07:48:54 EST by Susan Allen on behalf of Institute for Molecular Bioscience