The Evolution and Analysis of the Functional Domains of the Chimeric Proteins that Initiate Pyrimidine Biosynthesis
Abstract
The objective of this research is to test the hypothesis that the complex proteins with novel functions arose in the course of evolution by combining structural domains having partial functions and to discover the rules that govern successful recombinations. The research focuses on the enzymes that catalyze de novo pyrimidine biosynthesis. While the reactions are the same in most organisms, there are striking differences in the structure and regulation of these enzymes. However we postulate that all of these proteins are composed of a small number of functional domains whose basic architecture is very ancient. Our goal is to determine the structural organization of the pyrimidine biosynthetic enzymes in several organisms that represent a broad cross section of the phylogenetic tree. Domain specific synthetic oligonucleotide probes are being used to analyze poly A+ RNA and to screen genomic or cDNA libraries to determine the domain structure of the pyrimidine biosynthetic proteins. The structure and mode of regulation of interesting structural variants will then be analyzed in detail.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 1988
- Accession Number
- ADA198428
Entities
People
- David Evans
Organizations
- Wayne State University