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Fuz1, a MYND domain protein, is required for cell morphogenesis in Ustilago maydis

Emily Chew1, Yara Aweiss, Ching-Yu Lu

  • 1Department of Chemistry and Biochemistry, California State University, 1250 Bellflower Boulevard, Long Beach, California 90840, USA.

Mycologia
|May 21, 2008
PubMed

Insights

The fuz1 gene is crucial for the development of Ustilago maydis, regulating yeast-to-filament transitions, cell shape, and integrity. This study details its cloning and function in fungal morphogenesis.

Area of Science:

  • Mycology
  • Molecular Biology
  • Genetics

Background:

  • Ustilago maydis transitions between yeast-like and filamentous forms, controlled by mating type loci.
  • Morphological changes, including teliospore formation, are essential for its life cycle.
  • The fuz1 gene's role in these developmental programs was previously unknown.

Purpose of the Study:

  • To clone and sequence the fuz1 gene from Ustilago maydis.
  • To elucidate the function of the Fuz1 protein in fungal development and cell morphogenesis.
  • To investigate Fuz1's role in mating, filamentous growth, and cell integrity.

Main Methods:

  • Gene cloning and sequencing of fuz1.
  • Generation of null mutations in fuz1 strains.
  • Construction of fuz1- diploid strains heterozygous at mating type loci.
  • Microscopic analysis of cell morphology and developmental transitions.

Main Results:

  • The fuz1 gene encodes a 1421-amino acid protein belonging to the MYND Zn finger domain family.
  • fuz1 is essential for pheromone-induced conjugation tube formation.
  • fuz1 is required for maintaining filamentous growth post-fusion and for normal yeast-like cell morphogenesis.
  • fuz1 is critical for cell wall integrity and preventing aberrant pigment secretion.

Conclusions:

  • The Fuz1 protein, a MYND domain-containing protein, plays a multifaceted role in Ustilago maydis development.
  • Fuz1 regulates key morphological transitions, including mating, filamentous growth, and yeast cell shape.
  • The MYND domain likely mediates protein-protein interactions to control cell morphogenesis and integrity.

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