Collins, Cynthia H. and Yokobayashi, Yohei and Umeno, Daisuke and Arnold, Frances H. (2003) Engineering proteins that bind, move, make and break DNA. Current Opinion in Biotechnology, 14 (4). pp. 371-378. ISSN 0958-1669. doi:10.1016/S0958-1669(03)00091-0. https://resolver.caltech.edu/CaltechAUTHORS:20180823-074749923
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Abstract
Recent protein engineering efforts have generated artificial transcription factors that bind new target DNA sequences and enzymes that modify DNA at new target sites. Zinc-finger-based transcription factors are favored targets for design; important technological advances in their construction and numerous biotechnological applications have been reported. Other notable advances include the generation of endonucleases and recombinases with altered specificities, made by innovative combinatorial and evolutionary protein engineering strategies. An unexpectedly high tolerance to mutation in the active sites of DNA polymerases is being exploited to engineer polymerases to incorporate artificial nucleotides or to display other, nonnatural activities.
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Additional Information: | © 2003 Elsevier Science Ltd. Available online 20 June 2003. We acknowledge support from the US National Science Foundation (Biological Information Technology and Storage (BITS) Grant EIA-0130613) and the US Defence Advanced Research Project Agency (DARPA) under award N66001-02-1-8929 (Disclaimer: any opinions, findings, and conclusions or recommendations expressed in this publication are those of the author(s) and do not necessarily reflect the views of the DARPA). YY also acknowledges support from a Japan Society for the Promotion of Science Postdoctoral Fellowship for Research Abroad. | |||||||||
Errata: | In this article, published in the August 2003 issue of Current Opinion in Biotechnology, the author’s discussion of engineering α-helical DNA-binding domains failed to note earlier reports of engineering protein–DNA interactions 1., 2., 3.. In particular, two studies reported altering the DNA-binding specificities of the Mnt repressor [1] and catabolite activator protein [2], using genetic selection methods, whereas a third described the substitution of an entire α-helix to alter the DNA-binding specificity of the 434 repressor protein [3]. The authors regret this significant oversight. | |||||||||
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Issue or Number: | 4 | |||||||||
DOI: | 10.1016/S0958-1669(03)00091-0 | |||||||||
Record Number: | CaltechAUTHORS:20180823-074749923 | |||||||||
Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20180823-074749923 | |||||||||
Official Citation: | Cynthia H Collins, Yohei Yokobayashi, Daisuke Umeno, Frances H Arnold, Engineering proteins that bind, move, make and break DNA, Current Opinion in Biotechnology, Volume 14, Issue 4, 2003, Pages 371-378, ISSN 0958-1669, https://doi.org/10.1016/S0958-1669(03)00091-0. (http://www.sciencedirect.com/science/article/pii/S0958166903000910) | |||||||||
Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | |||||||||
ID Code: | 89074 | |||||||||
Collection: | CaltechAUTHORS | |||||||||
Deposited By: | Tony Diaz | |||||||||
Deposited On: | 23 Aug 2018 17:07 | |||||||||
Last Modified: | 01 Jun 2023 22:42 |
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