- Title Information
- Title
- Ubiquitin-Dependent Proteolysis of the Yeast Mating-Type Regulator Matalpha1
- Name:
Personal
- Name Part
- Nixon, Christina Erin
- Role
- Role Term:
Text
- creator
- Origin Information
- Copyright Date
(keyDate="yes", encoding="w3cdtf")
- 2009
- Physical Description
- Extent
- xiv, 203 p.
- digitalOrigin
- born digital
- Note
- Thesis (Ph.D.) -- Brown University (2010)
- Name:
Personal
- Name Part
- Laney, Jeffrey
- Role
- Role Term:
Text
- director
- Name:
Personal
- Name Part
- Landy, Arthur
- Role
- Role Term:
Text
- reader
- Name:
Personal
- Name Part
- Mowry, Kimberly
- Role
- Role Term:
Text
- reader
- Name:
Personal
- Name Part
- Freiman, Richard
- Role
- Role Term:
Text
- reader
- Name:
Personal
- Name Part
- Johnson, Erica
- Role
- Role Term:
Text
- reader
- Name:
Corporate
- Name Part
- Brown University. Division of Biology and Medicine. Molecular Biology, Cell Biology, and Biochemistry
- Role
- Role Term:
Text
- sponsor
- Genre (aat)
- theses
- Abstract
- Cell type in budding yeast is controlled by the master regulatory transcription factors encoded at the mating-type (MAT) locus Mat?1, Mat?2, and Mata1. In
homothallic strains, the a and ? haploid cell types are unstable states, and cell type switching can occur with high frequency. To facilitate such efficient switching, the Mat
transcription factors are unstable proteins. At least one of these factors, Mat?2, is degraded by the ubiquitin-proteasome system (UPS). It stands to reason that the UPS would also
degrade the other ?-specific regulator, Mat?1. Understanding how Mat?1 is degraded and if it is degraded coordinately with Mat?2 will provide a model to study
other phenotypic switching events. Here, I demonstrate that Mat?1 is a substrate for the UPS and is targeted for proteolysis by multiple E2 and E3 enzymes, including one common pathway
with Mat?2: Ubc4/Ubc5/Slx5-Slx8. Interestingly, Mat?1 turnover requires an intact sumoylation pathway as well as poly-SUMO chains, whereas Mat?2 does not. Using a
series of Mat?1 deletion mutants fused to Ura3 (the normally stable uracil biosynthetic enzyme), I have also isolated several regions within Mat?1 that are necessary for rapid
turnover potentially corresponding to the multiple ubiquitin ligases. Interestingly, a region coinciding with the alpha1 domain (residues 75-150), while not sufficient to confer wild-type levels
of instability to Ura3, is dependent upon Slx5-Slx8. Taken together, these data show that while the degradation pathways of Mat?1 and Mat?2 share commonalities, the details of
the pathways are unique for each factor.
- Subject (Local)
- Topic
- MATalpha1
- Subject (Local)
- Topic
- ubiquitin-proteasome system
- Subject (Local)
- Topic
- protein degradation
- Subject (Local)
- Topic
- mating-type switching
- Subject (Local)
- Topic
- SUMO
- Subject (Local)
- Topic
- Slx5
- Subject (Local)
- Topic
- Slx8
- Subject (Local)
- Topic
- Ufd4
- Subject (Local)
- Topic
- Ubc13
- Subject (Local)
- Topic
- Ubc4
- Subject (Local)
- Topic
- Ubc5
- Subject (FAST)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/1182596")
- Topic
- Yeast
- Subject (FAST)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/1930489")
- Topic
- Proteolysis
- Record Information
- Record Content Source (marcorg)
- RPB
- Record Creation Date
(encoding="iso8601")
- 20091218
- Language
- Language Term:
Code (ISO639-2B)
- eng
- Language Term:
Text
- English
- Identifier:
DOI
- 10.7301/Z0M043PC
- Access Condition:
rights statement
(href="http://rightsstatements.org/vocab/InC/1.0/")
- In Copyright
- Access Condition:
restriction on access
- Collection is open for research.
- Type of Resource (primo)
- dissertations