Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions
Post-translational modification of proteins via ubiquitination is mediated by three enzyme families; El activating enzymes, E2 conjugating enzymes and E3 ligases, all of which work in a hierarchical manner to facilitate different forms of protein ubiquitin ranging from mono-ubiquitination to the for...
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| Format: | Article |
| Language: | English |
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Academic Journals Inc.
2013
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| Online Access: | http://eprints.usm.my/37772/ http://eprints.usm.my/37772/1/1-14-2.pdf |
| _version_ | 1848878283829018624 |
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| author | Zulkifle, Nurulisa |
| author_facet | Zulkifle, Nurulisa |
| author_sort | Zulkifle, Nurulisa |
| building | USM Institutional Repository |
| collection | Online Access |
| description | Post-translational modification of proteins via ubiquitination is mediated by three enzyme families; El activating enzymes, E2 conjugating enzymes and E3 ligases, all of which work in a hierarchical manner to facilitate different forms of protein ubiquitin ranging from mono-ubiquitination to the formation of different forms of ubiquitin chains. Reversibly, deubiquitinating enzymes (DUBs) act to remove ubiquitin from modified substrates. Apart from the classic interactions within the E1-E2-E3 enzymatic cascade, an unusual non-hierarchical interaction has been observed between some E2 enzymes and a DUB called Otubain-1 (OTUB1). This observation raises interesting questions concerning the order and specificity within the human ubiquitin system. In this study, systematic yeast two-hybrid (Y2H) binary screen is performed between 39 E2 and 60 DUB proteins to analyze the extent of human E2-DUB interactions. As a result, putative partnerships between OTUB1 and UBE2D1, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3 and UBE2N are identified and these data correlate well with data from other independent study by high-throughput Y2H library screen and mass spectrometry. In essence, this study confirmed that E2-DUB interactions within the human ubiquitin system are indeed uncommon and only unique to OTUB1 protein. |
| first_indexed | 2025-11-15T17:28:53Z |
| format | Article |
| id | usm-37772 |
| institution | Universiti Sains Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T17:28:53Z |
| publishDate | 2013 |
| publisher | Academic Journals Inc. |
| recordtype | eprints |
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| spelling | usm-377722017-12-06T03:04:20Z http://eprints.usm.my/37772/ Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions Zulkifle, Nurulisa RK1-715 Dentistry Post-translational modification of proteins via ubiquitination is mediated by three enzyme families; El activating enzymes, E2 conjugating enzymes and E3 ligases, all of which work in a hierarchical manner to facilitate different forms of protein ubiquitin ranging from mono-ubiquitination to the formation of different forms of ubiquitin chains. Reversibly, deubiquitinating enzymes (DUBs) act to remove ubiquitin from modified substrates. Apart from the classic interactions within the E1-E2-E3 enzymatic cascade, an unusual non-hierarchical interaction has been observed between some E2 enzymes and a DUB called Otubain-1 (OTUB1). This observation raises interesting questions concerning the order and specificity within the human ubiquitin system. In this study, systematic yeast two-hybrid (Y2H) binary screen is performed between 39 E2 and 60 DUB proteins to analyze the extent of human E2-DUB interactions. As a result, putative partnerships between OTUB1 and UBE2D1, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3 and UBE2N are identified and these data correlate well with data from other independent study by high-throughput Y2H library screen and mass spectrometry. In essence, this study confirmed that E2-DUB interactions within the human ubiquitin system are indeed uncommon and only unique to OTUB1 protein. Academic Journals Inc. 2013 Article PeerReviewed application/pdf en cc_by http://eprints.usm.my/37772/1/1-14-2.pdf Zulkifle, Nurulisa (2013) Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions. International Journal of Biological Chemistry, 7 (1). pp. 1-14. ISSN 1819-155X http://docsdrive.com/pdfs/academicjournals/ijbc/2013/1-14.pdf |
| spellingShingle | RK1-715 Dentistry Zulkifle, Nurulisa Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions |
| title | Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions |
| title_full | Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions |
| title_fullStr | Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions |
| title_full_unstemmed | Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions |
| title_short | Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions |
| title_sort | systematic yeast two-hybrid analysis of human e2 ubiquitin-conjugating enzyme and deubiquitin (dub) protein interactions |
| topic | RK1-715 Dentistry |
| url | http://eprints.usm.my/37772/ http://eprints.usm.my/37772/ http://eprints.usm.my/37772/1/1-14-2.pdf |