Structure and Dynamics of the Synaptonemal Complex

Information

  • Research Project
  • 8575009
  • ApplicationId
    8575009
  • Core Project Number
    R15GM104827
  • Full Project Number
    1R15GM104827-01A1
  • Serial Number
    104827
  • FOA Number
    PA-12-006
  • Sub Project Id
  • Project Start Date
    9/1/2013 - 10 years ago
  • Project End Date
    8/31/2016 - 7 years ago
  • Program Officer Name
    CARTER, ANTHONY D.
  • Budget Start Date
    9/1/2013 - 10 years ago
  • Budget End Date
    8/31/2016 - 7 years ago
  • Fiscal Year
    2013
  • Support Year
    01
  • Suffix
    A1
  • Award Notice Date
    8/19/2013 - 10 years ago
Organizations

Structure and Dynamics of the Synaptonemal Complex

DESCRIPTION (provided by applicant): Project Summary/Abstract During meiotic prophase, homology recognition between partner chromosomes is coordinated with the assembly of a proteinaceous scaffold, the synaptonemal complex (SC), along the length of the chromosome pair (synapsis). Interhomolog recombination progresses within the context of assembled SC, and many interhomolog recombination events rely on SC for their proper distribution and/or completion. Our lab investigates SC structure and how SC assembly is coordinated with meiotic prophase chromosomal events. Recently we demonstrated that In S. cerevisiae, at least some components of the SC remain dynamic during meiotic prophase, even after chromosomes are fully synapsed. Moreover we found that recombination sites maintain a different SC dynamic as compared to other sites on the SC. Furthermore, our preliminary studies show that SUMO, which localizes to SC structures, has a mutually dependent relationship with the coiled-coil Zip1 protein to assemble SC on meiotic chromosomes. With pioneering imaging studies using super-resolution light microscopy, we have also shown that SUMO localizes to Zip1 N termini, at the center of SC structure. Finally, the lab has isolated zip1 alleles that assemble on chromosomes independent of canonical regulators. Each zip1 allele represents a single amino acid substitution at the extreme C terminus of Zip1 and may reveal aspects of the mechanism underlying Zip1 assembly. The purpose of this grant proposal is to 1) use our established genetic and microscopy tools to define the molecular architecture and dynamics of all known synapsis proteins within the SC, and 2) to isolate point mutant alleles of synapsis initiation proteins and Zip1 in order to identif molecular features of each protein responsible for their function in synapsis and other meiotic prophase chromosomal events.

IC Name
NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
  • Activity
    R15
  • Administering IC
    GM
  • Application Type
    1
  • Direct Cost Amount
    226962
  • Indirect Cost Amount
    145483
  • Total Cost
    372445
  • Sub Project Total Cost
  • ARRA Funded
    False
  • CFDA Code
    859
  • Ed Inst. Type
    SCHOOLS OF ARTS AND SCIENCES
  • Funding ICs
    NIGMS:372445\
  • Funding Mechanism
    Non-SBIR/STTR RPGs
  • Study Section
    MGA
  • Study Section Name
    Molecular Genetics A Study Section
  • Organization Name
    WESLEYAN UNIVERSITY
  • Organization Department
    BIOCHEMISTRY
  • Organization DUNS
    145683954
  • Organization City
    MIDDLETOWN
  • Organization State
    CT
  • Organization Country
    UNITED STATES
  • Organization Zip Code
    064593208
  • Organization District
    UNITED STATES