{"doi":"10.1111/febs.12216","title":"Reversibly acetylated lysine residues play important roles in the enzymatic activity of <i><scp>E</scp>scherichia coli <scp>N</scp></i>‐hydroxyarylamine <i><scp>O</scp></i>‐acetyltransferase","abstract":"<jats:p>Cob<jats:styled-content style=\"fixed-case\">B</jats:styled-content> is a bacterial <jats:styled-content style=\"fixed-case\">NAD</jats:styled-content><jats:sup>+</jats:sup>‐dependent protein deacetylase. Although progress has been made in functional studies of this protein in recent years, its substrates and biological functions are still largely unclear. Using proteome microarray technology, potential substrates of <jats:italic>Escherichia coli </jats:italic><jats:styled-content style=\"fixed-case\">C</jats:styled-content>ob<jats:styled-content style=\"fixed-case\">B</jats:styled-content> were screened and nine proteins were identified, including <jats:italic>N</jats:italic>‐hydroxyarylamine <jats:italic>O</jats:italic>‐acetyltransferase (<jats:styled-content style=\"fixed-case\">N</jats:styled-content>ho<jats:styled-content style=\"fixed-case\">A</jats:styled-content>). <jats:italic>In vitro</jats:italic> acetylation/deacetylation of <jats:styled-content style=\"fixed-case\">N</jats:styled-content>ho<jats:styled-content style=\"fixed-case\">A</jats:styled-content> was verified by western blotting and mass spectrometry, and two acetylated lysine residues were identified. Site‐specific mutagenesis experiments showed that mutation of each acetylated lysine decreased the acetylation level of NhoA <jats:italic>in vitro</jats:italic>. Further analysis showed that variant <jats:styled-content style=\"fixed-case\">N</jats:styled-content>ho<jats:styled-content style=\"fixed-case\">A</jats:styled-content> proteins carrying substitutions at the two acetylated lysine residues are involved in both the <jats:italic>O</jats:italic>‐acetyltransferase and <jats:italic>N</jats:italic>‐acetyltransferase activity of NhoA. Structural analyses were also performed to explore the effects of the acetylated lysine residues on the activity of <jats:styled-content style=\"fixed-case\">N</jats:styled-content>ho<jats:styled-content style=\"fixed-case\">A</jats:styled-content>. These results suggest that reversible acetylation may play a role in the activity of <jats:italic><jats:styled-content style=\"fixed-case\">E</jats:styled-content>scherichia coli </jats:italic><jats:styled-content style=\"fixed-case\">N</jats:styled-content>ho<jats:styled-content style=\"fixed-case\">A</jats:styled-content>.</jats:p>","journal":"The FEBS 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