Journal
PLOS ONE
Volume 5, Issue 12, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0015801
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Funding
- Wellcome Trust [085309]
- BBSRC [BB/F011784/1]
- University of Kent Innovation bursary
- Biotechnology and Biological Sciences Research Council [JF20605, BB/F011784/1] Funding Source: researchfish
- BBSRC [BB/F011784/1] Funding Source: UKRI
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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.
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