Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja7114019
Title: Identification of the binding of sceptrin to MreB via a bidirectional affinity protocol
Authors: Rodríguez, A.D.
Lear, M.J. 
La Clair, J.J.
Issue Date: 11-Jun-2008
Citation: Rodríguez, A.D., Lear, M.J., La Clair, J.J. (2008-06-11). Identification of the binding of sceptrin to MreB via a bidirectional affinity protocol. Journal of the American Chemical Society 130 (23) : 7256-7258. ScholarBank@NUS Repository. https://doi.org/10.1021/ja7114019
Abstract: A bidirectional affinity system was used to screen for marine natural products that bound to Escherichia coli proteins. A system was developed and applied to isolate the natural product sceptrin from an Agelas conifera extract and its affinity partner MreB from E. coli lysate. The use of a dual immunoaffinity fluorescent (IAF) tag permitted this process to co-immunoprecipitate the bacterial equivalent of actin, MreB, from E. coli lysate. MreB was subsequently validated as a target for sceptrin using a resistance mapping approach. The combination of these studies suggests that natural products and their protein targets can be isolated in concert using a melody of forward and reverse affinity matrices. While the structure of sceptrin was elucidated by NMR analysis, the bulk of effort was conducted without knowing the structure of the natural product, thereby elevating a key bottleneck in the development of high-throughput methods for natural product discovery. Copyright © 2008 American Chemical Society.
Source Title: Journal of the American Chemical Society
URI: http://scholarbank.nus.edu.sg/handle/10635/76339
ISSN: 00027863
DOI: 10.1021/ja7114019
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