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Research Topics, Division of Biological Chemistry, Biocentre,  Innsbruck Medical University

 

Role of nitric oxide in Physarum polycephalum, see text below for more information

Physarum nitric oxide synthase

Physarum polycephalum is a single-cell multi-nuclear model organism used in cell biology because of its naturally synchronous cell cycle and its ability to undergo differentiation. Remarkably, this organism expresses the only thus far known fully functional NO synthase outside the animal kingdom (1), an enzyme required by this organism to gain sporulation competence thus establishing a novel role for the H4-biopterin/NO/cGMP axis in cell differentiation (2). Moreover, we were involved in initiating the Physarum genome project which was started in August 2004 by the National Human Genome Research Institute (NHGRI) following an initiative of an international Physarum genome consortium headed by J. Gott, Cleveland. Together with W. Marwan, Magdeburg, and G. Gloeckner, Jena, a transcriptome project of the plasmodial stage analysed about half of the protein coding genes of Physarum, yielding an important resource for the ongoing genome project (3). In the near future, these projects will allow to study signalling networks and protein expression related to cell differentiation in a systematic large-scale approach.

 

  1. Werner-Felmayer, G., Golderer, G., Werner, E. R., Grobner, P., Wachter, H. (1994) Pteridine biosynthesis and nitric oxide synthase in Physarum polycephalum. Biochem.J. 304 ( Pt 1), 105-111
  2. Golderer G, Werner ER, Leitner S, Gröbner P, Werner-Felmayer G (2001) Nitric oxide synthase is induced in sporulation of Physarum polycephalum. Genes Dev 15:1299-1309 
  3. Gloeckner G, Golderer G, Werner-Felmayer G, Meyer S, Marwan W (2008) A first glimpse in the transcriptome of Physarum polycephalum. BMC Genomics 9:6 doi:10.1186/1471-2164-9-6
  4. Messner S, Leitner S, Bommassar C, Golderer G, Grobner P, Werner ER, Werner-Felmayer G (2009) Physarum nitric oxide synthases: Genomic structures and enzymology of recombinant proteins. Biochem.J.,418: 691-700

Biocenter, Area Biochemistry and Chemistry