Domains of the SFL1 protein of yeasts are homologous to Myc oncoproteins or yeast heat-shock transcription factor.

We identified a yeast suppressor gene for flocculation (SFL1), which complemented a newly isolated sfl1 mutant. This mutation causes asexual cell aggregation. SFL1 encodes a 767-amino acid protein which has two domains significantly homologous to Myc oncoproteins and the yeast heat shock transcription factor (HSTF). The Myc homologous region in SFL1 overlaps with the conserved region in a series of interesting proteins: MyoD1, Drosophila achaete-scute, twist, daughterless gene products and immunoglobulin enhancer-binding proteins. In addition, the N-terminal region of the SFL1 gene product shows extensive homology to the DNA-binding domain of HSTF. Mutational analysis of SFL1 demonstrates that it is required for normal cell-surface assembly in vegetative growth. We propose that the SFL1 gene product may be a transcription factor which is involved in regulation of the gene(s) related to yeast flocculation.