The proposed research involves deducing how Crr1, a regulator of copper homeostasis in Chlamydomonas, works. Crr1 is known on genetic criteria to be required for copper homeostasis but nothing is known about it biochemically. Sequence analysis suggests that one domain of Crr1 is related to a conserved but novel domain in a family of plant DNA binding proteins. It is therefore likely that Crr1 is a DNA binding protein. First, site-directed mutagenesis of Crr1 will be done in order to undertake functional studies on copper and/or DNA binding. Following this, expression of one domain of Crr1 in quantities sufficient for structural analysis will be undertaken, and ultimately the structure of Crr1 via NMR and/or crystallography will be determined.