YorkSpace has migrated to a new version of its software. Access our Help Resources to learn how to use the refreshed site. Contact diginit@yorku.ca if you have any questions about the migration.
 

Insight into the Biochemical Interaction of USP7 C-terminal Domain

Simple item page
dc.contributor.advisorSaridakis, Vivian
dc.creatorLacdao, Ira Kay Logatoc
dc.date.accessioned2015-08-28T14:38:17Z
dc.date.available2015-08-28T14:38:17Z
dc.date.copyright2013-12-16
dc.date.issued2015-08-28
dc.date.updated2015-08-28T14:38:17Z
dc.degree.disciplineBiology
dc.degree.levelMaster's
dc.degree.nameMSc - Master of Science
dc.description.abstractUbiquitination is a post-translational modification, involving the covalent attachment of ubiquitin, important for the regulation of cellular pathways. Deubiquitinases reverse this process through the hydrolysis of ubiquitin moieties from substrates. The deubiquitinase, Ubiquitin Specific Protease 7 (USP7), regulates many important nuclear processes. The USP7 N-terminus (USP7-NTD) is a TRAF domain which functions predominantly in substrate-binding while the USP7 C-terminus (USP7- CTD) was predicted to have 4-5 ubiquitin like domains (Ubl1-5). The aims of this thesis are biochemical and structural analyses of the C-terminus of human USP7. Various Ubl domains of human USP7-CTD were cloned, expressed, purified and crystallized. Subsequently, the biochemical interaction of an ICP0 peptide with these Ubl domains was investigated using in vitro GST-pulldown experiments and fluorescence polarization assays where the ICP0 peptide showed tightest interaction with Ubl123. Co-crystals of Ubl123 and ICP0 peptide need further refinement prior to structure determination.
dc.identifier.urihttp://hdl.handle.net/10315/29818
dc.language.isoen
dc.rightsAuthor owns copyright, except where explicitly noted. Please contact the author directly with licensing requests.
dc.subjectMolecular biology
dc.subjectBiochemistry
dc.subject.keywordsDeubiquitination
dc.subject.keywordsUbiquitination
dc.subject.keywordsUbiquitin specific protease 7
dc.subject.keywordsViruses
dc.subject.keywordsProtein x-ray crystallography
dc.titleInsight into the Biochemical Interaction of USP7 C-terminal Domain
dc.typeElectronic Thesis or Dissertationen_US

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Lacdao_Ira_Kay_L_2013_Masters.pdf
Size:
46.58 MB
Format:
Adobe Portable Document Format
Download
License bundle
Now showing 1 - 2 of 2
No Thumbnail Available
Name:
license.txt
Size:
1.83 KB
Format:
Plain Text
Description:
Download
No Thumbnail Available
Name:
YorkU_ETDlicense.txt
Size:
3.38 KB
Format:
Plain Text
Description:
Download

Collections

Biology

All items in the YorkSpace institutional repository are protected by copyright, with all rights reserved except where explicitly noted.