Type
Text
Type
Thesis
Advisor
Hollingsworth, Nancy M | Sternglanz, Rolf | Luk, Ed.
Date
2013-12-01
Keywords
Genetics | Sgs1, SUMO, Zip1
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/11401/76917
Publisher
The Graduate School, Stony Brook University: Stony Brook, NY.
Format
application/pdf
Abstract
Meiotic crossovers (COs) are essential for proper chromosomal separation. Interhomologue recombination is promoted by the synaptonemal complex (SC), which connects paired homologous chromosomes together. Zip1, an integral component of the SC, antagonizes Sgs1 helicase function during meiotic recombination to promote COs. Specifically, Zip1 and other ZMM proteins shield strand invasion intermediates from Sgs1 activity, thus preventing Sgs1 from disassembling them. It has been previously discovered that Zip1 interacts with Sgs1 in two-hybrid experiments, and that full length Zip1 binds to Sgs1 in vitro. These interactions suggest that the antagonism may be due to direct interactions between Sgs1 and Zip1. This work shows that a negative charge at Ser801 on Zip1 enhances the interaction between Sgs1 in two-hybrid experiments, and that the N-terminal region of Sgs1 interacts with a small ubiquitin-like modifier interacting motif (SIM) of Zip1. These results suggest that Sgs1 interacts with Zip1 via SUMO chains, and the phosphorylation of Zip1 by Mek1 kinase may enhance the interaction between the SUMOlyated site on Sgs1 and the SIM on Zip1, which further antagonizes Sgs1 helicase activity to enable CO products. | 45 pages
Recommended Citation
Hussain, Sana F., "Analysis of Zip1 and Sgs1 protein interaction in budding yeast" (2013). Stony Brook Theses and Dissertations Collection, 2006-2020 (closed to submissions). 2790.
https://commons.library.stonybrook.edu/stony-brook-theses-and-dissertations-collection/2790