Genetically encoding Nε-acetyllysine in recombinant proteins
H Neumann, SY Peak-Chew, JW Chin - Nature chemical biology, 2008 - nature.com
H Neumann, SY Peak-Chew, JW Chin
Nature chemical biology, 2008•nature.comN ε-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 ε-acetyllysine (2) at defined sites. Here we demonstrate the site-
specific incorporation of N ε-acetyllysine in recombinant proteins produced in Escherichia
coli via the evolution of an orthogonal N ε-acetyllysyl-tRNA synthetase/tRNA CUA pair. This
strategy should find wide applications in defining the cellular role of this modification.
role that rivals that of phosphorylation in eukaryotes. No general methods exist to synthesize
proteins containing N ε-acetyllysine (2) at defined sites. Here we demonstrate the site-
specific incorporation of N ε-acetyllysine in recombinant proteins produced in Escherichia
coli via the evolution of an orthogonal N ε-acetyllysyl-tRNA synthetase/tRNA CUA pair. This
strategy should find wide applications in defining the cellular role of this modification.
Abstract
N ε-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 ε-acetyllysine (2) at defined sites. Here we demonstrate the site-specific incorporation of N ε-acetyllysine in recombinant proteins produced in Escherichia coli via the evolution of an orthogonal N ε-acetyllysyl-tRNA synthetase/tRNA CUA pair. This strategy should find wide applications in defining the cellular role of this modification.
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