| Chapter title |
Analysis of Nuclear Uracil DNA-Glycosylase (nUDG) Turnover During the Cell Cycle.
|
|---|---|
| Chapter number | 11 |
| Book title |
Cell Cycle Synchronization
|
| Published in |
Methods in molecular biology, January 2017
|
| DOI | 10.1007/978-1-4939-6603-5_11 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6602-8, 978-1-4939-6603-5
|
| Authors |
Jennifer A. Fischer, Salvatore J. Caradonna |
| Editors |
Gaspar Banfalvi |
| Abstract |
Uracil-DNA glycosylases (UDG/UNG) are enzymes that remove uracil from DNA and initiate base-excision repair. These enzymes play a key role in maintaining genomic integrity by reducing the mutagenic events caused by G:C to A:T transition mutations. The recent finding that a family of RNA editing enzymes (AID/APOBECs) can deaminate cytosine in DNA has raised the interest in these base-excision repair enzymes. The methodology presented here focuses on determining the regulation of the nuclear isoform of uracil-DNA glycosylase (nUDG), a 36,000 Da protein. In synchronized HeLa cells, nUDG protein levels decrease to barely detectable levels during the S phase of the cell cycle. Immunoblot analysis of immunoprecipitated or affinity-isolated nUDG reveals ubiquitin-conjugated nUDG when proteolysis is inhibited by agents that block proteasomal-dependent protein degradation. |
Mendeley readers
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|---|---|---|
| Unknown | 5 | 100% |
Demographic breakdown
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|---|---|---|
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| Librarian | 1 | 20% |
| Student > Ph. D. Student | 1 | 20% |
| Researcher | 1 | 20% |
| Unknown | 1 | 20% |
| Readers by discipline | Count | As % |
|---|---|---|
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| Social Sciences | 1 | 20% |
| Unknown | 1 | 20% |