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
Institutional Unit:	Schools > School of Natural Sciences > Biosciences
Former Institutional Unit:	Divisions > Division of Natural Sciences > Biosciences
Funders:	Biotechnology and Biological Sciences Research Council (https://ror.org/00cwqg982) Wellcome Trust (https://ror.org/029chgv08)
Depositing User:	Daniel Mulvihill
Date Deposited:	30 Dec 2010 18:10 UTC
Last Modified:	20 May 2025 09:16 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/26186 (The current URI for this page, for reference purposes)

University of Kent Author Information

Johnson, Matthew.

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Geeves, Michael A..

Creator's ORCID:	https://orcid.org/0000-0002-9364-8898
CReDIT Contributor Roles:

Mulvihill, Daniel P..

Creator's ORCID:	https://orcid.org/0000-0003-2502-5274
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