Dataset for: Ifu5, a WW domain-containing protein interacts with Efg1 to achieve coordination of normoxic and hypoxic functions to influence pathogenicity traits in <i>Candida albicans</i>

Hypoxic adaptation pathways, essential for <i>Candida albicans</i> pathogenesis, are tied to its transition from a commensal to a pathogen. Herein, we identify a WW domain-containing protein, Ifu5, as a determinant of hypoxic adaptation that also impacts normoxic responses in this fungus. Ifu5 activity supports glycosylation homeostasis via the Cek1 MAP kinase-dependent upregulation of <i>PMT1</i>, under normoxia. Transcriptome analysis of <i>ifu5</i>Δ/Δ under normoxia shows a significant upregulation of the hypoxic regulator <i>EFG1</i> and -dependent genes. We demonstrate physical interaction between Ifu5 by virtue of its WW domain and Efg1 that represses <i>EFG1</i> expression under normoxia. This interaction is lost under hypoxic growth conditions, relieving <i>EFG1</i> repression. Hypoxic adaptation processes such as filamentation and biofilm formation are affected in <i>ifu5</i>Δ/Δ cells revealing the role of Ifu5 in hypoxic signalling and modulating pathogenicity traits of <i>C. albicans</i> under varied oxygen conditions. Additionally, the WW domain of Ifu5 facilitates its role in hypoxic adaptation, revealing the importance of this domain in providing a platform to integrate various cellular processes. These data forge a relationship between Efg1 and Ifu5 that fosters the role of Ifu5 in hypoxic adaptation, thus illuminating novel strategies to undermine the growth of <i>C. albicans</i>.