The need of a dividing cell to partition its contents evenly into two daughter cells is faced by all organisms. It is essentially a two-part process; first a cell must decide where it is going to divide; then it has to distribute the cytoplasmic and nuclear contents appropriately between the two new cells. A family of proteins, called septins, is thought to be essential to the cell division process by marking the cleavage plane, and by serving as a scaffold for the attachment of other proteins that act in cytokinesis. Septins were first described as a series of lOnm rings formed at the base of the daughter cell in the yeast Saccharomyces cerevisiae. Since their initial discovery homologues to septins have been found in other species including fruit flies, mice and humans. They seem to be important developmental proteins, yet very little work has been done with them in filamentous fungi. Three septin homologues have been found in Aspergillus nidulans using degenerate PCR. The current project focuses on characterization of these septins in A. nidulans using both localization studies and the generation of null alleles. To identify its cellular location, antibodies are being raised to aspB (Aspergillus septin B) and fusions with green fluorescent protein are being built. Null alleles of aspB have already been reported, and result in a lethal phenotype. Construction of a null allele by homologous recombination of a marker gene at the aspA locus is currently in progress. In addition, fusion proteins of aspA will be constructed for antibody production, purification, and localization of the gene product.
Fungal Genet. Newsl. 46 (Supl):
Full conference title:
Fungal Genetics Conference 20th
- Fungal Genetics Conference 20th (1999)