Functional characterization of Aspergillus nidulans RpdA: identification of complex partners and subcellular localization

Ref ID: 18452

Author:

Ingo Bauer, Birgit Faber, Fabian Schuler, Gerald Brosch, Stefan Graessle

Author address:

Biocenter – Division of Molecular Biology, Innsbruck Medical University

Full conference title:

11 th European Conference on Fungal Genetics

Abstract:

In eukaryotic organisms DNA is compacted into an elaborate structure called chromatin, thus enabling regulation
of transcription by controlling the accessibility of the genetic information for transcription factors. Among the key
players involved in the regulation of chromatin structure are histone acetyltransferases and histone deacetylases
(HDACs)- enzymes establishing distinct acetylation patterns in the N8208;terminal tails of core histones. In filamentous
fungi only little is known about the biological functions of these enzymes; nevertheless recent studies have shown
that class 2 HDACs affect the regulation of genes involved in stress response and secondary metabolite production.
Depletion of RpdA, a class 1 HDAC of Aspergillus nidulans, leads to a drastic reduction of growth and sporulation.
Functional studies revealed that a short C8208;terminal motif unique for RpdA8208;type proteins of filamentous fungi is
required for catalytic activity and consequently cannot be deleted without affecting the viability of A. nidulans. In
order to further characterize RpdA we have started to analyze complex formation and localization of the protein
with respect to this motif by expressing TAP8208; and GFP8208;tagged RpdA versions. First results indicate that both tagged
full8208;length proteins are functional and suggest a role of the C8208;terminal motif for proper subcellular localization.

Abstract Number: PR1.24

Conference Year: 2012

Link to conference website: http://www.ecfg.info/images/Abstract_Book_Electronic.pdf

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