Journal of Microbiology

Review

REVIEW] Hgc1-Cdc28–how much does a single protein kinase do in the regulation of hyphal development in Candida albicans?: Yue Wang; J. Microbiol. 2016;54(3):170-177. Published online February 27, 2016; DOI: https://doi.org/10.1007/s12275-016-5550-9

Abstract: The fungal human pathogen Candida albicans can cause invasive infection with high mortality rates. A key virulence factor is its ability to switch between three morphologies: yeast, pseudohyphae and hyphae. In contrast to the ovalshaped unicellular yeast cells, hyphae are highly elongated, tube-like, and multicellular. A long-standing question is what coordinates all the cellular machines to construct cells with distinct shapes. Hyphal-specific genes (HSGs) are thought to hold the answer. Among the numerous HSGs found, only UME6 and HGC1 are required for hyphal development. UME6 encodes a transcription factor that regulates many HSGs including HGC1. HGC1 encodes a G1 cyclin which partners with the Cdc28 cyclin-dependent kinase. Hgc1- Cdc28 simultaneously phosphorylates and regulates multiple substrates, thus controlling multiple cellular apparatuses for morphogenesis. This review is focused on major progresses made in the past decade on Hgc1’s roles and regulation in C. albicans hyphal development and other traits important for infection.

Isolation and Characterization of Bud6p, an Actin Interacting Protein, from Yarrowia lipolytica: Yunkyoung Song , Seon Ah Cheon , So-Yeon Lee , Ji-Sook Hwang , Jeong-Yoon Kim; J. Microbiol. 2003;41(2):121-128.

Abstract: The identification of genes involved in true hypha formation is important in the study of mechanisms underlying the morphogenetic switch in yeast. We isolated a gene responsible for the morphogenetic switch in Yarrowia lipolytica, which forms true hyphae in response to serum or N-acetylglucosamine. The isolated gene, encoding 847 amino acids, had sequence identities of 27% and 25% with the Bud6 (Aip3) proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. Disruption of this gene, designated YlBUD6, in haploid and diploid strains significantly reduced the ability of Y. lipolytica to switch from the yeast form to the hyphal form in hypha-inducing media. It was also found that YlBud6 mutants were rounder than the wild type when grown in the yeast form. These results indicate that the YlBud6 protein is necessary for hyphal growth and cell polarity in both haploid and diploid Y. lipolytica cells.

Search