Abstract
N(epsilon)-acetylation of lysine (1) is a reversible post-translational modification with a regulatory role that rivals that of phosphorylation in eukaryotes. No general methods exist to synthesize proteins containing N(epsilon)-acetyllysine (2) at defined sites. Here we demonstrate the site-specific incorporation of N(epsilon)-acetyllysine in recombinant proteins produced in Escherichia coli via the evolution of an orthogonal N(epsilon)-acetyllysyl-tRNA synthetase/tRNA(CUA) pair. This strategy should find wide applications in defining the cellular role of this modification.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acyl-tRNA Synthetases / chemistry
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Amino Acyl-tRNA Synthetases / genetics
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Lysine / analogs & derivatives*
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Lysine / chemistry
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Lysine / genetics
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Methanosarcina barkeri / genetics
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Methanosarcina barkeri / metabolism
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Models, Molecular
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Molecular Conformation
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RNA, Transfer / chemistry
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RNA, Transfer / genetics
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics*
Substances
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Recombinant Proteins
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N-epsilon-acetyllysine
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RNA, Transfer
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Amino Acyl-tRNA Synthetases
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Lysine
Associated data
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PubChem-Substance/46530441
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PubChem-Substance/46530442
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PubChem-Substance/46530443
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PubChem-Substance/46530444
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PubChem-Substance/46530445
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PubChem-Substance/46530446