Generation and purification of deletion constructs of UBC13 and their interaction with UEV1A

Bisht, Vinod Singh and Raghavendra, N K (2018) Generation and purification of deletion constructs of UBC13 and their interaction with UEV1A. Masters thesis, Indian Institute of Technology Hyderabad.

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Covalent attachment of Ubiquitin to other molecule is known as Ubiquitylation (Ubiquitination) which involves the cascade of reactions that is catalyzed by E1(ubiquitin activating enzyme), E2(Ubiquitin conjugating enzyme), and E3(Ubiquitin ligase) proteins. Ubiquitin conjugating enzyme (E2) like Ubc13 which catalyses the K63 linked polyubiquitin chains synthesis forms heterodimer with E2 variant Uev1A (Ubc13/Uev1A). This heterodimer binds to the RING domain of E3 ligases such as TRAF6 to generate unanchored K63-chains which signal activation of protein kinases involved in innate immune response. Another heterodimer of Ubc13/Uev1A associates with E3 ligase TRIM5α for eliciting anti-HIV response. TRIM5α is a well-characterized anti-retroviral factor that is known to accelerate the rate of uncoating process upon entry of virion core into the susceptible cell, thus preventing formation of DNA copy of viral genome or its integration into human DNA. The present study of my project is to generate and purify the different deletion constructs of Ubc13 and analyze their interaction with UEV1A.

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IITH Creators:
IITH CreatorsORCiD
Raghavendra, N K
Item Type: Thesis (Masters)
Uncontrolled Keywords: UBC13, VEV1A
Subjects: Others > Biotechnology
Divisions: Department of Biotechnology
Depositing User: Team Library
Date Deposited: 29 Jun 2018 11:58
Last Modified: 29 Jun 2018 11:58
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