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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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Main Author: Zulkifle, Nurulisa
Format: Article
Language:English
Published: Academic Journals Inc. 2013
Subjects:
RK1-715 Dentistry
Online Access:http://eprints.usm.my/37772/1/1-14-2.pdf
http://eprints.usm.my/37772/
http://docsdrive.com/pdfs/academicjournals/ijbc/2013/1-14.pdf
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spelling my.usm.eprints.37772 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
institution Universiti Sains Malaysia
building Hamzah Sendut Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Sains Malaysia
content_source USM Institutional Repository
url_provider http://eprints.usm.my/
language English
topic RK1-715 Dentistry
spellingShingle RK1-715 Dentistry
Zulkifle, Nurulisa
Systematic Yeast Two-Hybrid Analysis of Human E2 Ubiquitin-Conjugating Enzyme and Deubiquitin (DUB) Protein Interactions
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.
format Article
author Zulkifle, Nurulisa
author_facet Zulkifle, Nurulisa
author_sort Zulkifle, Nurulisa
title 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_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_sort systematic yeast two-hybrid analysis of human e2 ubiquitin-conjugating enzyme and deubiquitin (dub) protein interactions
publisher Academic Journals Inc.
publishDate 2013
url http://eprints.usm.my/37772/1/1-14-2.pdf
http://eprints.usm.my/37772/
http://docsdrive.com/pdfs/academicjournals/ijbc/2013/1-14.pdf
_version_ 1643709165414121472
score 13.211869

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