Characterization of the role of Ume6 C-terminal tail in morphological plasticity.

is an important human fungal pathogen and filamentation is essential for its virulence. Ume6 is a transcription factor critical for filamentation. Ume6 is composed of three domains, a long N terminal domain, Zn-finger domain, and a C-terminal domain. Previously, it was shown that the Zn-finger domain is essential for filamentation, as removal of this domain led to a lack of filamentation. However, the role for the C-terminal domain has not been defined. We find deletion of the C-terminal domain leads to a filamentation defect and the defect is not as severe as removal of the Zn-finger or deletion. We mutated a number of residues in the C-terminal domain to try to identify specific residues important for filamentation, but all of our mutants displayed wild type filamentation. Alpha fold predictions suggest the C-terminal domain forms a single alpha helix that is predicted to interact with the Zn-finger domain via hydrogen bond. Our data suggests the C-terminal domain binds the Zn-finger domain and through this interaction is important for filamentation.