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dc.contributor.advisorSaridakis, Vivian
dc.creatorAshurov, Leila
dc.date.accessioned2015-01-26T15:24:33Z
dc.date.available2015-01-26T15:24:33Z
dc.date.copyright2014-08-27
dc.date.issued2015-01-26
dc.identifier.urihttp://hdl.handle.net/10315/28292
dc.description.abstractUbiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme that regulates the turnover of proteins in a cell. To date several interacting partners that are involved in various cellular processes have been identified for USP7. Many of the interacting partners of USP7 contain a P/AxxS motif. We have identified two E2 ubiquitin-conjugating enzymes, UbE2E2 and UbE2E3, which contain the P/AxxS motif. Using a co-immunoprecipitation assay we have shown that these E2 proteins interact with USP7 through their P/AxxS motif. Co-crystal structures of the N-terminal domain of USP7 (USP7-NTD) and the E2 peptides reveal that the interactions are formed between USP7-NTD residues 164DWGF167 and the E2 P/AxxS motifs. It has also been established that USP7 may be involved in regulating the cellular levels of UbE2E2. Overall, our findings suggest USP7, a de-ubiquitinating enzyme, is a regulator of ubiquitin-conjugating enzymes, which are involved in the ubiquitination cascade.
dc.language.isoen
dc.rightsAuthor owns copyright, except where explicitly noted. Please contact the author directly with licensing requests.
dc.subjectBiochemistry
dc.subjectCellular biology
dc.subjectMolecular biology
dc.titleStructural and Functional Analyses of the Interaction Between the USP7-NTD and the E2-Conjugating Enzymes, UbE2E2 and UbE2E3
dc.typeElectronic Thesis or Dissertationen_US
dc.degree.disciplineBiology
dc.degree.nameMSc - Master of Science
dc.degree.levelMaster's
dc.date.updated2015-01-26T15:24:32Z
dc.subject.keywordsUbE2E3en_US
dc.subject.keywordsUbiquitinen_US
dc.subject.keywordsUbiquitinationen_US
dc.subject.keywordsUbiquitin-conjugating enzymesen_US
dc.subject.keywordsDeubiquitinating enzymesen_US
dc.subject.keywordsUSP7en_US
dc.subject.keywordsUbE2E2en_US


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