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Background   CDC4 , which encodes an F-box protein that is a member of the Skp1-Cdc53/Cul1-F-box (SCF) ubiquitin E3 ligase, was initially identified in the budding yeast  Saccharomyces cerevisiae  as an essential gene for progression through G1-S transition of the cell cycle. Although  Candida albicans CDC4  ( CaCDC4 ) can release the mitotic defect caused by the loss of  CDC4  in  S. cerevisiae ,  CaCDC4  is nonessential and suppresses filamentation.    Results  To further elucidate the function of  CaCDC4 , a  C. albicans  strain, with one  CaCDC4  allele deleted and the other under the repressible  C. albicans MET3  promoter ( CaMET3 p) control, was made before introducing cassettes capable of doxycycline (Dox)-induced expression of various  C. albicans  Cdc4 ( Ca Cdc4) domains. Cells from each strain could express a specific  Ca Cdc4 domain under Dox-induced, but  CaMET3-CaCDC4  repressed conditions. Cells expressing domains without either the F-box or WD40-repeat exhibited filamentation and flocculation similarly to those lacking  CaCDC4  expression, indicating the functional essentiality of the F-box and WD40-repeat. Notably, cells expressing the N-terminal 85-amino acid truncated  Ca Cdc4 partially reverse the filament-to-yeast and weaken the ability to flocculate compared to those expressing the full-length  Ca Cdc4, suggesting that N-terminal 85-amino acid of  Ca Cdc4 regulates both morphogenesis and flocculation.    Conclusions  The F-box and the WD40-repeat of  Ca Cdc4 are essential in inhibiting yeast-to-filament transition and flocculation. The N-terminal region (1–85) of  Ca Cdc4 also has a positive role for its function, lost of which impairs both the ability to flocculate and to reverse filamentous growth in  C. albicans .

Dissection of the Candida albicans Cdc4 protein reveals the involvement of domains in morphogenesis and cell flocculation