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

Johnson, M. and Couton, A.T. and Geeves, M.A. and Mulvihill, D.P. (2010) Targeted amino-terminal acetylation of recombinant proteins in E. coli. PLoS One, 5 (12). e15801. ISSN 1932-6203. (Full text available)

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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
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH426 Genetics
Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Dan Mulvihill
Date Deposited: 30 Dec 2010 18:10
Last Modified: 25 Nov 2011 16:41
Resource URI: http://kar.kent.ac.uk/id/eprint/26186 (The current URI for this page, for reference purposes)
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