ArticleMycologia
Fuz1, a MYND domain protein, is required for cell morphogenesis in Ustilago maydis.
Article in Mycologia. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Coexistence of genetically different Rhizophagus irregularis isolates induces genes involved in a putative fungal mating response.The ISME journal · 2020Article
- Molecular Mechanisms Involved in the Multicellular Growth of Ustilaginomycetes.Microorganisms · 2020Review
- The cell end marker Tea4 regulates morphogenesis and pathogenicity in the basidiomycete fungus Ustilago maydis.Fungal genetics and biology : FG & B · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Abstract: Ustilago maydis is a Basidiomycete fungus that exhibits a yeast-like nonpathogenic form and a dikaryotic filamentous pathogenic form. Generation of these two forms is controlled by two mating type loci, a and b. The fungus undergoes additional morphological transitions in the plant that result in formation of a third cell type, the teliospore. The fuz1 gene is necessary for this developmental program. Here we report cloning and sequencing of fuz1 and show that it contains an open reading frame with coding capacity for a protein of 1421 amino acids. The Fuz1 protein belongs to the family of MYND Zn finger domain proteins. We generate a null mutation in strains of opposite mating type and show that fuz1 is necessary for conjugation tube formation, a morphological transition that occurs in response to pheromones. We generate fuz1- diploid strains heterozygous at a and b and show that fuz1 is also necessary for postfusion events (maintenance of filamentous growth). We also demonstrate that fuz1 is necessary for cell morphogenesis of the yeast-like cell: normal cell length, location and number of septa, cell separation and constriction of the neck region. Fuz1 is also required for cell wall integrity and to prevent secretion of a dark pigment. We propose that the MYND domain may interact with different proteins to regulate cell morphogenesis.
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