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Targeted amino-terminal acetylation of recombinant proteins in E. coli.

Johnson, Matthew, Couton, Arthur T., Geeves, Michael A., Mulvihill, Daniel P. (2010) Targeted amino-terminal acetylation of recombinant proteins in E. coli. PLoS ONE, 5 (12). e15801. ISSN 1932-6203. (doi:10.1371/journal.pone.0015801) (KAR id:26186)

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Official URL
http://dx.plos.org/10.1371/journal.pone.0015801

Abstract

One major limitation in the expression of eukaryotic proteins in bacteria is an inability to post-translationally modify the expressed protein. Amino-terminal acetylation is one such modification that can be essential for protein function. By co- expressing the fission yeast NatB complex with the target protein in E.coli, we report a simple and widely applicable method for the expression and purification of functional N-terminally acetylated eukaryotic proteins.

Item Type: Article
DOI/Identification number: 10.1371/journal.pone.0015801
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH426 Genetics
Q Science > QR Microbiology
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Daniel Mulvihill
Date Deposited: 30 Dec 2010 18:10 UTC
Last Modified: 06 Feb 2020 04:05 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/26186 (The current URI for this page, for reference purposes)
Geeves, Michael A.: https://orcid.org/0000-0002-9364-8898
Mulvihill, Daniel P.: https://orcid.org/0000-0003-2502-5274
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