Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/51986
Title: N-TERMINAL DETERMINANTS OF CYTOSOLIC PROTEIN QUALITY CONTROL
Authors: ANTHONY TRAN
Keywords: CytoQC, Ubr1, Quality, Misfolded, Degradation, N-end
Issue Date: 26-Sep-2013
Source: ANTHONY TRAN (2013-09-26). N-TERMINAL DETERMINANTS OF CYTOSOLIC PROTEIN QUALITY CONTROL. ScholarBank@NUS Repository.
Abstract: In yeast, the San1p and Ubr1p E3 ligases target cytosolic misfolded proteins for degradation. While San1p and Ubr1p are known to exhibit partially overlapping specificity for misfolded substrates, differences in their means of target recognition were unclear. Ubr1p is a mediator of the N-end rule pathway, which relates the half-life of a protein to the identity of its N-terminal residue. In this study, we discovered a link between Ubr1p¿s affinity for specific novel destabilizing N-terminal sequences, or N-degrons, and its function in protein quality control. This led us to propose a new model for Ubr1 quality control in which a subset of proteins that undergo translocation failure, and are thus aberrantly localized to the cytosol, become subject to Ubr1-mediated quality control by virtue of harboring a bi-partite signal comprising a destabilizing N-terminal sequence and conformational aberrancy. Our analysis of several representative mis-translocated mitochondrial and secretory pathway proteins confirms our model.
URI: http://scholarbank.nus.edu.sg/handle/10635/51986
Appears in Collections:Ph.D Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
TranA.pdf7.23 MBAdobe PDF

OPEN

NoneView/Download

Page view(s)

99
checked on Dec 11, 2017

Download(s)

14
checked on Dec 11, 2017

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.