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

  • Author / Creator
    Desaulniers, Adrien, B
  • 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.

  • Subjects / Keywords
  • Graduation date
    Fall 2013
  • Type of Item
    Thesis
  • Degree
    Master of Science
  • DOI
    https://doi.org/10.7939/R3R962
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
  • Language
    English
  • Institution
    University of Alberta
  • Degree level
    Master's
  • Department
  • Specialization
    • Molecular Biology and Genetics
  • Supervisor / co-supervisor and their department(s)
  • Examining committee members and their departments
    • McKenzie, Debbie (Biological Sciences)
    • McDermid, Heather (Biological Sciences)
    • King-Jones, Kirst (Biological Sciences)