Identification and Characterization of mel-43 in C. elegans

  • Author / Creator
    Ataeian, Maryam
  • In the newly fertilized embryo, meiotic and mitotic spindles form
    consecutively within the same egg cytoplasm. The order of events during
    this transition is controlled, in part, via the regulation of the microtubule
    cytoskeleton. Herein, I show that mel-43 is part of a small paralogous
    gene family that is required to specify the meiosis II program of cell
    division in the fertilized egg. RNAi of mel-43 and paralogues resulted in
    failed meiosis I polar body extrusion, followed by direct entry into mitotic
    prophase. Furthermore, the dominant maternal-effect mutation mel-
    43(sb41) showed a meiosis-to-mitosis transition delay and a failure to
    segregate chromatids that exhibited persistent REC-8/kleisin
    immunostaining. Anti-MEL-43 antibodies showed that the MEL-43
    proteins exhibited high cytoplasmic levels in meiosis as well as a fibrous
    staining pattern in the midzone of the anaphase spindle. The protein
    levels were reduced after meiosis, and this was dependent on the CUL-
    2/ZYG-11 E3 ligase complex.

  • Subjects / Keywords
  • Graduation date
    Spring 2013
  • Type of Item
  • Degree
    Master of Science
  • DOI
  • 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
  • Institution
    University of Alberta
  • Degree level
  • Department
  • Specialization
    • Molecular Biology and Genetics
  • Supervisor / co-supervisor and their department(s)
  • Examining committee members and their departments
    • Waskiewicz, Andrew (Department of Biological Sciences)
    • Srayko, Martin (Department of Biological Sciences)
    • Campbell, Shelagh (Department of Biological Sciences)
    • Stuart, David (Department of Biochemistry)