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

  • Ribosome biogenesis factor
  • AOX
  • Enzymes
  • Alternative oxidase
  • Dual specificity phosphatase
  • Neurospora-crassa
  • Phosphatase domain
  • DUSP
  • Zinc binding domain
  • DUSP12
  • YVH1

• 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.