Graduation Year

2026

Document Type

Campus Only Senior Thesis

Degree Name

Bachelor of Arts

Department

Biology

Reader 1

Dr. Jennifer Armstrong

Reader 2

Professor Xiao Zhang

Abstract

Several potential interactors of Chromodomain-helicase-DNA-binding-protein-1 (CHD1), an evolutionarily conserved ATP-dependent chromatin remodeling complex implicated in many diseases such as prostate cancer, have been identified through genetic and functional assays. Jarid2 and Virilizer are two of the CHD1 putative interactors that were discovered through this mutagenesis assay. Jarid2 is a member of the Jumonji (Jmj) family of histone demethylase and functions in association with the Polycomb Repressive Complex 2 (PRC2) which mediates the methylation of histone H3 lysine 27. JARID2 facilitates the recruitment of PRC2 to repress transcriptional genes in hemopoietic progenitor cells. Consequently, JARID2 acts as a tumor suppressor in myeloproliferative neoplasms, and its deletion or mutation is linked to many diseases and multiple cancers in humans. Virilizer functions as a sex determination gene in Drosophila melanogaster. It is expressed throughout development in both males and females. In humans, the Virilizer ortholog, VIRMA, functions through RNA splicing and binding activity, making it critical in the progression of cancers. Although these proteins have been identified as potential physical interactors of CHD1 in fly embryos, it remains unclear whether they functionally interact with CHD1. Here, I use an RNAi-based genetic assay to investigate the interaction between these candidate proteins and CHD1. The influence on CHD1 function in the genetic assay is characterized by wing vein defects resulting from the overexpression of CHD1. I observed that the loss of Virilizer is inherently deleterious to the fly, complicating the assessment of its functionality with CHD1. Silencing Jarid2 enhanced the phenotypic wing defects of CHD1 overexpression, suggesting that Jarid2 normally buffers this phenotype.

 

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