scholarly journals MHY1 Encodes a C2H2-Type Zinc Finger Protein That Promotes Dimorphic Transition in the Yeast Yarrowia lipolytica

1999 ◽  
Vol 181 (10) ◽  
pp. 3051-3057 ◽  
Author(s):  
Cleofe A. R. Hurtado ◽  
Richard A. Rachubinski
Keyword(s):  
Yarrowia Lipolytica ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Pathogenic Fungi ◽  
Response Elements ◽  
Dimorphic Transition ◽  
Adverse Conditions ◽  
Finger Protein ◽  
Yeast Yarrowia Lipolytica ◽  
Hyphal Tip

ABSTRACT The yeast-to-hypha morphological transition (dimorphism) is typical of many pathogenic fungi. Dimorphism has been attributed to changes in temperature and nutritional status and is believed to constitute a mechanism of response to adverse conditions. We have isolated and characterized a gene, MHY1, whose transcription is dramatically increased during the yeast-to-hypha transition inYarrowia lipolytica. Deletion of MHY1 is viable and has no effect on mating, but it does result in a complete inability of cells to undergo mycelial growth. MHY1 encodes a C2H2-type zinc finger protein, Mhy1p, which can bind putative cis-acting DNA stress response elements, suggesting that Mhy1p may act as a transcription factor. Interestingly, Mhy1p tagged with a hemagglutinin epitope was concentrated in the nuclei of actively growing cells found at the hyphal tip.

scholarly journals The CHY-type zinc finger protein FgChy1 regulates polarized growth, pathogenicity, and microtubule assembly in Fusarium graminearum

2020 ◽  
Author(s):  
Shulin Cao ◽  
Wei Li ◽  
Chaohui Li ◽  
Guanghui Wang ◽  
Wenqiang Jiang ◽  
...  
Keyword(s):  
Filamentous Fungi ◽  
Zinc Finger ◽  
Fusarium Graminearum ◽  
Zinc Finger Protein ◽  
Microtubule Assembly ◽  
Polarized Growth ◽  
Wild Type ◽  
Finger Protein ◽  
Associated Proteins ◽  
Hyphal Tip

Microtubules, as transport tracks, play important roles in hyphal tip growth in filamentous fungi, but microtubule-associated proteins involved in polarized growth remain unknown. Here, we found that one novel zinc finger protein, FgChy1, is required for microtubule morphology and polarized growth in Fusarium graminearum. The Fgchy1 mutant presented curved and directionless growth of hyphae. Importantly, the conidia and germ tubes of the Fgchy1 mutant exhibited badly damaged and less organized beta-tubulin cytoskeletons. Compared with the wild type, the Fgchy1 mutant lost the ability to maintain polarity and was also more sensitive to the anti-microtubule drugs carbendazim and nocodazole, likely due to the impaired microtubule cytoskeleton. Indeed, the hyphae of the wild type treated with nocodazole exhibited a morphology consistent with that of the Fgchy1 mutant. Interestingly, the disruption of FgChy1 resulted in the off-center localization of actin patches and the polarity-related polarisome protein FgSpa2 from the hyphal tip axis. A similar defect in FgSpa2 localization was also observed in the nocodazole-treated wild-type strain. In addition, FgChy1 is also required for conidiogenesis, septation, sexual reproduction, pathogenicity and deoxynivalenol production. Overall, this study provides the first demonstrations of the functions of the novel zinc finger protein FgChy1 in polarized growth, development and virulence in filamentous fungi.

Cloning and functional analysis of SCTF-1 encoding a C2H2-type zinc finger protein from soybean

2012 ◽  
Vol 34 (6) ◽  
pp. 749-756 ◽  
Author(s):  
Bing SONG ◽  
Pi-Wu WANG ◽  
Yong-Ping FU ◽  
Xu-Hong FAN ◽  
Hai-Feng XIA ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Finger Protein
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