Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions

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

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Abstract

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.

Item Type:	Article
Subjects:	R Medicine > RK Dentistry > RK1-715 Dentistry
Divisions:	Institut Perubatan & Pergigian Termaju (Advanced Medical & Dental Institute (AMDI)) > Article Zoom Profil Pakar (Expert Profile) > Nurulisa Zulkifle (Advanced Medical & Dental Institute)
Depositing User:	Administrator Automasi
Date Deposited:	06 Dec 2017 03:04
Last Modified:	06 Dec 2017 03:04
URI:	http://eprints.usm.my/id/eprint/37772

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