Biochemical Basis of E. coli Topoisomerase I Relaxation Activity Reduction by Nonenzymatic Lysine Acetylation
| Autor: | Francisco Fernandez-Lima, Yuk-Ching Tse-Dinh, Mario E. Gomez Hernandez, Qingxuan Zhou |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Lysine acetyl phosphate complex mixtures Catalysis Article Inorganic Chemistry lcsh:Chemistry 03 medical and health sciences chemistry.chemical_compound Escherichia coli Protein–DNA interaction Physical and Theoretical Chemistry DNA Cleavage Molecular Biology lysine acetylation lcsh:QH301-705.5 Spectroscopy chemistry.chemical_classification topoisomerase posttranslational modification biology Topoisomerase Organic Chemistry Acetylation General Medicine DNA DNA supercoiling Enzyme assay Organophosphates DNA–protein interaction Computer Science Applications 030104 developmental biology Enzyme chemistry Biochemistry DNA Topoisomerases Type I lcsh:Biology (General) lcsh:QD1-999 biology.protein DNA supercoil bacteria Protein Processing Post-Translational Protein Binding |
| Zdroj: | International Journal of Molecular Sciences, Vol 19, Iss 5, p 1439 (2018) International Journal of Molecular Sciences; Volume 19; Issue 5; Pages: 1439 International Journal of Molecular Sciences |
| ISSN: | 1422-0067 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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