Novel Approaches to the Characterization of Specific Protein-Protein Interactions Important in Gene Expression.
Abstract
Through the application of a range of techniques in the areas of biochemistry, molecular biology, and microbial physiology, we have purified and characterized the TyrR protein of Haemophilus influenzae. This dimeric protein interacts with specific operator targets associated with promoters that drive the production of proteins essential for aromatic amino acid biosynthesis or transport. Like its E. coli counterpart, the H. influenzae protein is organized into discrete domains that bind either DNA or small molecules that function as coregulators. In separate studies, we showed that the tyrosine phenol lyase-promoter of Citrobacter freundii is regulated not only by the TyrR protein but also by two global transcription factors, namely Integration Host Factor and cyclic AMP receptor protein.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 30, 1998
- Accession Number
- ADA358254
Entities
People
- Ronald L. Somerville
Organizations
- Purdue Research Foundation