The unusual UBZ domain of Saccharomyces cerevisiae polymerase η
Recent research has revealed the presence of ubiquitin-binding domains in the Y family polymerases. The ubiquitin-binding zinc finger (UBZ) domain of human polymerase η is vital for its regulation, localization, and function. Here, we elucidate structural and functional features of the non-canonical...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | en_US |
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Elsevier
2015
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| Online Access: | http://hdl.handle.net/1721.1/99180 https://orcid.org/0000-0001-7243-8261 |
| _version_ | 1811086840037376000 |
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| author | Woodruff, Rachel V. Bomar, Martha G. Zhou, Pei Walker, Graham C. D'Souza, Sanjay Victor |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Woodruff, Rachel V. Bomar, Martha G. Zhou, Pei Walker, Graham C. D'Souza, Sanjay Victor |
| author_sort | Woodruff, Rachel V. |
| collection | MIT |
| description | Recent research has revealed the presence of ubiquitin-binding domains in the Y family polymerases. The ubiquitin-binding zinc finger (UBZ) domain of human polymerase η is vital for its regulation, localization, and function. Here, we elucidate structural and functional features of the non-canonical UBZ motif of Saccharomyces cerevisiae pol η. Characterization of pol η mutants confirms the importance of the UBZ motif and implies that its function is independent of zinc binding. Intriguingly, we demonstrate that zinc does bind to and affect the structure of the purified UBZ domain, but is not required for its ubiquitin-binding activity. Our finding that this unusual zinc finger is able to interact with ubiquitin even in its apo form adds support to the model that ubiquitin binding is the primary and functionally important activity of the UBZ domain in S. cerevisiae polymerase η. Putative ubiquitin-binding domains, primarily UBZs, are identified in the majority of known pol η homologs. We discuss the implications of our observations for zinc finger structure and pol η regulation. |
| first_indexed | 2024-09-23T13:35:30Z |
| format | Article |
| id | mit-1721.1/99180 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T13:35:30Z |
| publishDate | 2015 |
| publisher | Elsevier |
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| spelling | mit-1721.1/991802022-09-28T14:52:29Z The unusual UBZ domain of Saccharomyces cerevisiae polymerase η Woodruff, Rachel V. Bomar, Martha G. Zhou, Pei Walker, Graham C. D'Souza, Sanjay Victor Massachusetts Institute of Technology. Department of Biology Woodruff, Rachel V. D'Souza, Sanjay Victor Walker, Graham C. Recent research has revealed the presence of ubiquitin-binding domains in the Y family polymerases. The ubiquitin-binding zinc finger (UBZ) domain of human polymerase η is vital for its regulation, localization, and function. Here, we elucidate structural and functional features of the non-canonical UBZ motif of Saccharomyces cerevisiae pol η. Characterization of pol η mutants confirms the importance of the UBZ motif and implies that its function is independent of zinc binding. Intriguingly, we demonstrate that zinc does bind to and affect the structure of the purified UBZ domain, but is not required for its ubiquitin-binding activity. Our finding that this unusual zinc finger is able to interact with ubiquitin even in its apo form adds support to the model that ubiquitin binding is the primary and functionally important activity of the UBZ domain in S. cerevisiae polymerase η. Putative ubiquitin-binding domains, primarily UBZs, are identified in the majority of known pol η homologs. We discuss the implications of our observations for zinc finger structure and pol η regulation. National Institute of Environmental Health Sciences (Grant ES-015818) National Institute of Environmental Health Sciences (Grant P30 ES-002109) American Cancer Society (Research Professorship) 2015-10-07T15:18:04Z 2015-10-07T15:18:04Z 2010-09 2010-07 Article http://purl.org/eprint/type/JournalArticle 15687864 http://hdl.handle.net/1721.1/99180 Woodruff, Rachel V., Martha G. Bomar, Sanjay D’Souza, Pei Zhou, and Graham C. Walker. “The Unusual UBZ Domain of Saccharomyces Cerevisiae Polymerase η.” DNA Repair 9, no. 11 (November 2010): 1130–1141. https://orcid.org/0000-0001-7243-8261 en_US http://dx.doi.org/10.1016/j.dnarep.2010.08.001 DNA Repair Creative Commons Attribution-Noncommercial-NoDerivatives http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier PMC |
| spellingShingle | Woodruff, Rachel V. Bomar, Martha G. Zhou, Pei Walker, Graham C. D'Souza, Sanjay Victor The unusual UBZ domain of Saccharomyces cerevisiae polymerase η |
| title | The unusual UBZ domain of Saccharomyces cerevisiae polymerase η |
| title_full | The unusual UBZ domain of Saccharomyces cerevisiae polymerase η |
| title_fullStr | The unusual UBZ domain of Saccharomyces cerevisiae polymerase η |
| title_full_unstemmed | The unusual UBZ domain of Saccharomyces cerevisiae polymerase η |
| title_short | The unusual UBZ domain of Saccharomyces cerevisiae polymerase η |
| title_sort | unusual ubz domain of saccharomyces cerevisiae polymerase η |
| url | http://hdl.handle.net/1721.1/99180 https://orcid.org/0000-0001-7243-8261 |
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