Genetically encoding thioacetyl-lysine as a non-deacetylatable analog of lysine acetylation in Escherichia coli.
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ABSTRACT:
SUBMITTER: Venkat S
PROVIDER: S-EPMC5666399 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
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Genetically encoding thioacetyl-lysine as a non-deacetylatable analog of lysine acetylation in <i>Escherichia coli</i>.
Venkat Sumana S Nannapaneni Dharma Theja DT Gregory Caroline C Gan Qinglei Q McIntosh Matt M Fan Chenguang C
FEBS open bio 20171016 11
Reversible lysine acetylation is one of the most widely distributed post-translational modifications; it is involved in a variety of biological processes and can be found in all three domains of life. Acetyltransferases and deacetylases work coordinately to control levels of protein acetylation. In this work, we applied the genetic code expansion strategy to site-specifically incorporate <i>N</i><sup>ε</sup>-thioacetyl-l-lysine (TAcK) as an analog of <i>N</i><sup>ε</sup>-acetyl-l-lysine (AcK) in ...[more]
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