DrBernhard Dichtl

Senior Lecturer

Faculty of Science Engineering and Built Environment/School of Life and Environmental Sciences/Institute for Mental and Physical Health and Clinical Translation

  • Senior Lecturer
    Faculty of Science Engineering and Built Environment/School of Life and Environmental Sciences/Institute for Mental and Physical Health and Clinical Translation
  • +61 3 925 17060 (Work)
  • Melbourne Burwood Campus, 221 Burwood Highway, Burwood, Victoria 3125

RESEARCH INTERESTS

1) The role and regulation of alternative polyadenylation in health and
disease.

Pre-mRNA 3' end formation is an essential RNA maturation step that impacts on
virtually all aspects of mRNA function. The process adds a tail of
approximately 250 adenosines to the 3' end of mRNA and determines the length
of the 3' Un-Translated Region (3'UTR), which is targeted by a large number of
regulatory factors. Control of 3'UTR length via alternative Polyadenylation
(APA) is an important mechanism to control gene expression. We are interested
in the regulation of APA and how it is integrated with cellular signaling
pathways.

2) The function and regulation of the Set1C histone methyltransferase.
Histone modifying enzymes regulate diverse processes that occur in association
with chromatin. We performed extensive yeast two-hybrid screening in order to
identify novel cellular roles for the Set1C chromatin-modifying enzyme. This
resulted in a recent publication in Science (Acquaviva et al., 2013), where we
identified the molecular mechanisms, which link chromatin modification of
histone H3 lysine 4 to the formation of double strand DNA breaks, to initiate
the process of meiotic recombination.

3) Co-translational protein complex formation.
Multi-protein complexes constitute some of the most relevant molecular units
of cellular function. Despite their important role it remains mysterious how
eukaryotic cells manage to assemble with precision hundreds of different
complexes in the crowded cytoplasmic compartment that produces thousands of
nascent proteins at the same time. Recently published work from our laboratory
demonstrated that assembly of protein complexes can be initiated on nascent
proteins as they emerge from the ribosome (Halbach et al, 2009). We are
currently investigating the functional significance of co-translational
protein interactions.

Knowledge Areas
Gene expression, RNA processing, Transcription, Chromatin, Protein Complexes,
yeast, cancer

GRANTS

  • GRANT
    Co-translational protein complex formation: a fundamental pathway of cellular organization?
    30 Jun 2014 - 31 Dec 2017
    People funded by this grant:
    • Dichtl B,
    • Zenklusen D,
    • Oeffinger M
    ARC - Discovery Projects - DP140101509 - $361,719.42
  • GRANT
    Regulation and assembly of the Set1C/COMPASS histone methyltransferase
    31 Jan 2011 - 31 Dec 2011
    People funded by this grant:
    • Bernhard Dichtl
    Swiss National Science Fund Research Grant - $153,758.84