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Int. J. Mol. Sci. 2018, 19(5), 1439; https://doi.org/10.3390/ijms19051439

Biochemical Basis of E. coli Topoisomerase I Relaxation Activity Reduction by Nonenzymatic Lysine Acetylation

1
Biomolecular Sciences Institute, Florida International University, Miami, FL 33199, USA
2
Department of Chemistry and Biochemistry, Florida International University, Miami, FL 33199, USA
*
Author to whom correspondence should be addressed.
Received: 12 April 2018 / Revised: 8 May 2018 / Accepted: 9 May 2018 / Published: 11 May 2018
(This article belongs to the Special Issue DNA Topoisomerases)
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Abstract

The relaxation activity of E. coli topoisomerase I is required for regulation of global and local DNA supercoiling. The in vivo topoisomerase I enzyme activity is sensitive to lysine acetylation–deacetylation and can affect DNA supercoiling and growth as a result. Nonenzymatic lysine acetylation by acetyl phosphate has been shown to reduce the relaxation activity of E. coli topoisomerase I. In this work, the biochemical consequence of topoisomerase I modification by acetyl phosphate with enzymatic assays was studied. Results showed that noncovalent binding to DNA and DNA cleavage by the enzyme were reduced as a result of the acetylation, with greater effect on DNA cleavage. Four lysine acetylation sites were identified using bottom-up proteomics: Lys13, Lys45, Lys346, and Lys488. The Lys13 residue modified by acetyl phosphate has not been reported previously as a lysine acetylation site for E. coli topoisomerase I. We discuss the potential biochemical consequence of lysine acetylation at this strictly conserved lysine and other lysine residues on the enzyme based on available genetic and structural information. View Full-Text
Keywords: topoisomerase; lysine acetylation; DNA supercoiling; DNA–protein interaction; acetyl phosphate; posttranslational modification topoisomerase; lysine acetylation; DNA supercoiling; DNA–protein interaction; acetyl phosphate; posttranslational modification
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Zhou, Q.; Gomez Hernandez, M.E.; Fernandez-Lima, F.; Tse-Dinh, Y.-C. Biochemical Basis of E. coli Topoisomerase I Relaxation Activity Reduction by Nonenzymatic Lysine Acetylation. Int. J. Mol. Sci. 2018, 19, 1439.

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