The catalysis of reaction sequences and their integration and regulation in the metabolic pathways of the cell depends on organization at several different levels. These include the organization of protein components in the various organelles and compartments at the cell level, the association of specific protein subunits into enzymes or multienzyme complexes and the organization and association of specific protein domains within the structure of the polypeptide subunits. The long range goal of this project is to define the role of subunit and domain interactions in the structure and function of multifunctional enzyme complexes. By utilizing a specific multi-functional enzyme complex from the tryptophan pathway or Neurospora crassa which is amenable to chemical, physical and genetic analysis, we propose to probe domain structure and organization in this multifunctional protein and the role of the interaction of domains and subunits in the expression of enzyme activities.
| Walker, M S; DeMoss, J A (1990) Deletion analysis of domain independence in the TRP1 gene product of Neurospora crassa. Mol Gen Genet 223:49-57 |
| Pratt, M L; DeMoss, J A (1988) Neurospora tryptophan synthase. Characterization of the pyridoxal phosphate binding site. J Biol Chem 263:6872-6 |
| Matchett, W H; Lacy, A M; DeMoss, J A (1987) Orientation of enzymic domains in tryptophan synthase of Neurospora crassa: an immunoblot analysis of TRP3 mutant products. Mol Gen Genet 208:398-407 |
| Walker, M S; DeMoss, J A (1986) Organization of the functional domains of anthranilate synthase from Neurospora crassa. Limited proteolysis studies. J Biol Chem 261:16073-7 |
