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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases / chemistry*
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Biochemistry / methods
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Carrier Proteins / chemistry*
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Cell Cycle Proteins / chemistry*
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Escherichia coli / enzymology*
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Escherichia coli / metabolism*
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Humans
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Intracellular Signaling Peptides and Proteins
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Protein Binding
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
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Proteins / chemistry*
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Recombinant Proteins / chemistry*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry*
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Schizosaccharomyces / metabolism*
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Schizosaccharomyces pombe Proteins / chemistry*
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Tropomyosin / chemistry*
Substances
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Carrier Proteins
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Cdc8 protein, S pombe
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Cell Cycle Proteins
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Intracellular Signaling Peptides and Proteins
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Proteins
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Recombinant Proteins
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SPART protein, human
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Saccharomyces cerevisiae Proteins
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Schizosaccharomyces pombe Proteins
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Tfs1 protein, S cerevisiae
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Tropomyosin
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Acetyltransferases
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NatB protein, S cerevisiae