RcLS2F - A Novel Fungal Class 1 KDAC Co-repressor Complex in Aspergillus nidulans

Ingo Bauer1, Silke Gross1, Petra Merschak1

  • 1Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.

Insights

Researchers identified a new protein complex, RcLS2F, involving fungal lysine deacetylase RpdA. This complex is crucial for fungal survival, sexual development, and regulating gene expression in Aspergillus nidulans.

Area of Science:

  • Molecular Biology
  • Mycology
  • Biochemistry

Background:

  • Class 1 lysine deacetylases (KDACs), like RpdA in *Aspergillus nidulans*, are essential for fungal survival and form multimeric complexes.
  • The composition of these RpdA-containing complexes in fungi remained largely unknown.
  • RpdA is a potential therapeutic target for invasive fungal infections caused by pathogens like *Aspergillus fumigatus*.

Purpose of the Study:

  • To characterize the composition of RpdA-containing protein complexes in *Aspergillus nidulans*.
  • To identify novel interactors and functional roles of RpdA complexes.

Main Methods:

  • Tandem affinity purification was employed to isolate and identify RpdA-associated proteins.
  • Co-immunoprecipitation and genetic analyses were used to confirm protein interactions and functional dependencies.

Main Results:

  • A novel RpdA-containing complex, termed RcLS2F, was identified.
  • RcLS2F comprises ScrC and the uncharacterized protein FscA, with FscA recruitment dependent on ScrC.
  • Loss of the RcLS2F complex explains the suppression of *crzA* deletion phenotypes by ScrC depletion, indicating a role in transcriptional repression.
  • RcLS2F is essential for fungal sexual development and participates in an autoregulatory feedback loop.

Conclusions:

  • The novel RcLS2F complex plays a critical role in regulating gene expression and is essential for sexual development in *Aspergillus nidulans*.
  • Understanding RpdA complex composition provides insights into fungal biology and potential antifungal strategies.
  • The findings elucidate a mechanism for transcriptional repression involving RcLS2F and its interaction with the transcription factor CrzA.

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