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Permanent link (DOI): https://doi.org/10.7939/R3R962

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The role of YVH1, a dual specificity phosphatase, in the production of alternative oxidase in the filamentous fungus Neurospora crassa Open Access

Descriptions

Other title
Subject/Keyword
Neurospora crassa
DUSP12
DUSP
Ribosome biogenesis factor
Dual specificity phosphatase
phosphatase domain
zinc binding domain
AOX
YVH1
enzyme
Alternative oxidase
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Desaulniers, Adrien, B
Supervisor and department
Nargang, Frank (Biological Sciences)
Examining committee member and department
McKenzie, Debbie (Biological Sciences)
King-Jones, Kirst (Biological Sciences)
McDermid, Heather (Biological Sciences)
Department
Department of Biological Sciences
Specialization
Molecular Biology and Genetics
Date accepted
2013-08-14T17:15:27Z
Graduation date
2013-11
Degree
Master of Science
Degree level
Master's
Abstract
Alternative oxidase (AOX) is a single protein enzyme that carries electrons from ubiquinol to molecular oxygen. AOX is induced in many organisms, including Neurospora crassa, when the standard electron transport chain is blocked through various inhibitors or mutations. A knockout (KO) for a dual specificity phosphatase, termed YVH1, cannot properly induce AOX and has a slow growth phenotype. YVH1 contains a HCX5R phosphatase domain and a zinc-binding domain. YVH1 localizes to the nucleus and cytosol equally under all conditions studied. The phenotype of the KO is rescued with constructs that contain only a functional zinc-binding domain. The phosphatase domain appears to be non-essential. The protein has been shown to play a role in ribosome biogenesis in yeast. Preliminary RNA-seq experiments revealed that expression of 17% of the 10,000 protein coding genes of N. crassa is altered at least 2 fold by loss of yvh1 when grown in inducing conditions.
Language
English
DOI
doi:10.7939/R3R962
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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File title: Microsoft Word - July 19 compiled Final Copy.docx
File author: Beau Desaulniers
Page count: 119
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