The School ™s new Mass Spectrometry Facility will allow ANU researchers to identify protein and peptide signals that regulate growth and development and identify gene function and gene mutations in all living things.
Specific research which will be undertaken on the facility includes examination of the malaria parasite, study of the legumes to better understand nitrogen fixing in plants and quantifying plant hormones and insect brain transmitters.
The Director of the Research School of Biological Sciences, Professor Jonathan Stone, said the facility will give ANU scientists access to the newest techniques and instrumentation.
The Mass Spectrometry Facility is an important new element of research infrastructure for the biological and biomedical sciences, established and maintained by RSBS. It will provide long-term support for researchers at ANU and in the wider research community of the ACT region.
The new $2.5m Facility was made possible by funding from the Australian Research Council, the ACT Government, the ANU Major Equipment Committee and the Research School of Biological Sciences.
Professor Barry Rolfe, the driving force behind the establishment of the Facility, said: We have seen the description of the human genome ™, our genetic code. Now our challenge is to describe the transcriptome - the total set of messages coded by the genome.
These messages are the building blocks of living tissue and mass spectrometry is the most powerful tool we have for understanding them. The techniques also underpin the development of more and more specifically constructed drugs.
The Facility is located in the Research School of Biological Sciences. It was officially launched today by the Chief Executive Officer of the Australian Research Council, Professor Peter Hoj.
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Experimenting with removal of the worm's lamin protein or its interacting protein partners emerin, MAN1 or BAF, the researchers have described "down-the-line" consequences, including the disruption of various proteins necessary for normal cell reproduction. Even though the C. elegans worm has only one lamin protein and few proteins that interact with it, the processes that occur there are similar to what happens in humans and provide clues to the laminopathic diseases affecting people..
The results seen from these lamin complex disruptions are a halted process of cell division, resulting in a static "bridge" structure between cells that should have separated, plus damage to the gonad cell structure. In both cases, the ability of the organism to grow and to reproduce is severely impaired.
The researchers hope that through further laboratory experimentation with the worm they will be able to better understand the functions of lamin-based complexes, and why mutations in these proteins cause a variety of different laminopathic diseases, such as progeria and muscular dystrophy in humans.
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