Authors

Matthew Murray

Type

Text

Type

Thesis

Advisor

Sternglanz, Rolf. | Hollingsworth, Nancy

Date

2014-12-01

Keywords

Cellular biology

Department

Department of Biochemistry and Cell Biology.

Language

en_US

Source

This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.

Identifier

http://hdl.handle.net/11401/76924

Publisher

The Graduate School, Stony Brook University: Stony Brook, NY.

Format

application/pdf

Abstract

Recombination is an essential meiotic process to ensure proper chromosome distribution. Recombination is promoted by the synaptonemal complex, a structure which bridges two pairs of homologous sister chromatids, bringing them into close proximity. The synaptonemal complex is formed by condensation of the sister chromatids on protein cores called axial elements. Homologous axial elements are then held together in budding yeast by a protein called Zip1. Zip1 is part of the ZMM group of proteins that work together during meiosis to promote the formation of crossovers which are distributed throughout the genome by interference. Four phosphorylation sites have been identified in the Zip1 C-terminus that are essential for the formation of interfering crossovers. To identify potential binding partners with the phosphorylated Zip1 C-terminus a two-hybrid screen was conducted using a zip1 mutant containing phosphomimetic amino acid substitutions. In this thesis I report the identification of three novel protein-protein interactions with the negatively charged Zip1 C-terminus. | 59 pages

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