Advisor: Dr. David Segal
My PhD research focused on the C2H2 zinc finger domain, specifically on protein-protein interactions mediated by these domains. C2H2 domains are found in many transcription factors and is well known as a DNA binding domain. For the past 15 years there has been growing recognition that the domain also forms protein-protein interactions. For my thesis, I worked with OAZ, a human protein containing 30 C2H2 domains arranged in 6 clusters, and used biochemical assays to measure the protein and the DNA binding potential of these clusters. In particular, I used the library based CAST assay (aka SELEX) and yeast 2-hybrid assays to examine the DNA and protein binding potential of the domain, and verified my results by mammalian co-immunoprecipitation and/or in vitro pull-down assays. My results indicate that the protein binding potential of C2H2 domains is high, and may be greater than their ability to interact with DNA.
I am currently working at Yale University as a postdoc. Broadly, my current project focuses on the evolution of gene regulation, and how novel gene function arises. Specifically, I am characterizing transcription factor complex formation at the prolactin promoter. This involves determining what factors are binding to the region, and any protein-protein interactions that occur at the promoter. I will also be looking at differences in the formation of transcription factor complexes at this promoter across species, and how complexes have evolved over time.
My PhD research focused on the C2H2 zinc finger domain, specifically on protein-protein interactions mediated by these domains. C2H2 domains are found in many transcription factors and is well known as a DNA binding domain. For the past 15 years there has been growing recognition that the domain also forms protein-protein interactions. For my thesis, I worked with OAZ, a human protein containing 30 C2H2 domains arranged in 6 clusters, and used biochemical assays to measure the protein and the DNA binding potential of these clusters. In particular, I used the library based CAST assay (aka SELEX) and yeast 2-hybrid assays to examine the DNA and protein binding potential of the domain, and verified my results by mammalian co-immunoprecipitation and/or in vitro pull-down assays. My results indicate that the protein binding potential of C2H2 domains is high, and may be greater than their ability to interact with DNA.
I am currently working at Yale University as a postdoc. Broadly, my current project focuses on the evolution of gene regulation, and how novel gene function arises. Specifically, I am characterizing transcription factor complex formation at the prolactin promoter. This involves determining what factors are binding to the region, and any protein-protein interactions that occur at the promoter. I will also be looking at differences in the formation of transcription factor complexes at this promoter across species, and how complexes have evolved over time.
Degree:
PhD
Program:
Pharmacology and Toxicology
Track:
Pharmacology and Toxicology
Employer:
Postdoctoral Fellow, Yale University
Dissertation Title:
“Protein Interactions Mediated by C2H2 Zinc Finger Proteins”
Career Type:
Academia