Dr Bernhard Dichtl
|Position:||Senior Lecturer |
|Faculty or Division:||Faculty of Sci Eng & Built Env|
|Department:||School of Life & Env. Sciences|
|Campus:||L2.07, Melbourne Burwood Campus|
|Phone:||+61 3 925 17060 +61 3 925 17060|
Dr Dichtl’s did his PhD studies at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany and at the University of Edinburgh, Scotland working on the molecular toxicity of lithium and the processing of ribosomal RNA and transfer RNA precursors. Supported by an EMBO long-term fellowship he then took up post-doctoral work at the Biocenter, in Basel Switzerland where he studied the mechanisms of pre-mRNA polyadenylation and transcription termination. A highly competitive and prestigious Foerderprofessur grant of the Swiss National Science Foundation (SNF) allowed him to establish his own research group at the Institute of Molecular Life Sciences, University of Zurich, Switzerland. There, he expanded his research activities to the analyses of chromatin modifying enzymes and the assembly of multi-protein complexes. Dr Dichtl’s laboratory relocated to Deakin University at the end of 2010. In 2014 he won an ARC Discovery Project grant to study the mechanisms of protein complex formation.
- Doctor of Philosophy, University of Edinburgh, 1998
- GCHE Exempt, Deakin University, 2011
Subjects and units currently teaching
SLE212 Biochemistry (Campus Coordinator)
SLE222 Biochemical Metabolism (Unit chair)
Several exiting Honours projects as well as SLE314 Research projects are available in my lab! Please write me an email if you would like to have a chat about those projects!
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.
ARC Discovery Project grant, ARC DP140101509, (2014-2016) Co-translational protein complex formation: a fundamental pathway of cellular organization?
1) Acquaviva L§, Székvölgyi L§, Dichtl B¶, Dichtl BS, de La Roche Saint André C¶, Nicolas A¶, Géli V¶. (2013) “The COMPASS subunit Spp1 links histone methylation to initiation of meiotic recombination.”, Science 339, 215-218. §Equal contribution; ¶corresponding author.
2) Holbein S, Scola S, Loll B, Dichtl BS, Hübner W, Meinhart A, Dichtl B. (2011) “The P-loop domain of yeast Clp1 mediates interactions between CF IA and CPF factors in pre-mRNA 3' end formation.”, PLoS ONE 6 (12), e29139.
3) Halbach A., Zhang H., Wengi A., Jablonska Z., Gruber I. M., Halbeisen R., Dehé P.M., Kemmeren P., Holstege F., Geli V., Gerber A. and Dichtl B. (2009) „Cotranslational assembly of the yeast SET1C histone methyltransferase complex.“ EMBO J. (19), 2959-2970.
4) Dichtl, B., Aasland, R. and Keller, W. “Functions for S. cerevisiae Swd2p in 3’ end formation of specific mRNAs and snoRNAs and global histone 3 lysine 4 methylation.” RNA 10 (6), 2004, 965-977.
5) Dichtl, B., Blank, D., Ohnacker, M., Friedlein, A., Roeder, D., Langen, H. and Keller,W. „A role for SSU72 in balancing RNA polymerase II transcription elongation and termination.“ Mol. Cell 10 (5), 2002, 1139-1150.