News & Announcements
Dr. Alain Stintzi' Research Group
The research group led by Dr. Alain Stintzi, a scientist at the Ottawa Institute of Systems Biology and Department of BMI, has discovered a group of genes that control the bacterial virulence of Campylobacter jejuni (C. jejuni). Campylobacter jejuni is a common gastrointestinal pathogen in humans and a common commensal colonizer of poultry. C. jejuni lacks several common metabolic pathways and was therefore thought not to use fructose as a carbon source for growth. However, Dr. Stintzi’s group has recently identified a group of genes (cj0480c-cj0490) that allow C. jejuni to use fucose as a substrate for growth, thereby linking a new metabolic pathway in C. jejuni with its virulent lifestyle. Their work is published in the Proc Natl Acad Sci U S A. 2011 Apr 26;108(17):7194-9, and highlighted by the Consortium for Functional Glycomics (CFG) and Nature Publishing Group at http://www.functionalglycomics.org/fg/update/2011/110512/full/fg.2011.17.shtml.
Dr. Ilona S. Skerjanc' Research Group
The research group led by Dr. Ilona S. Skerjanc, a professor at the Department of BMI, has identified the first kinase that regulates the expression of two important muscle factors (namely MyoD and Myf5) in embryonic stem cells and muscle progenitor stem cells. In a recent publication at EMBO Journal (http://www.ncbi.nlm.nih.gov/pubmed/21556048), Dr. Al-Madhoun and his colleagues delineated the importance of MEF2C phosphorylation and the recruitment of histone acetyltransferases in the lineage specification of skeletal muscle. They further found a non-myosin phosphorylation substrate for the skeletal muscle myosin light chain kinase (skMLCK), which may control the replenishment of muscle stem cells. Their findings provide new insights into skeletal muscle development and have important impact on the clinical treatment.
Dr. Couture' Research Group
One of the long-standing questions in the field of chromatin biology is how histone-modifying enzymes are tethered to a specific promoter region. Dr. Couture laboratory at OISB and BMI has recently found that Ash2L, a protein interacting with the histone H3 lysine 4 methyltransferase MLL1, harbors a novel helix-wing-helix DNA binding domain that is needed for targeting and H3K4 trimethylation in vivo. Given that MLL1 is linked to acute forms of leukemia, these findings will eventually guide structure-based drug discoveries for the treatment of leukemia and other MLL-linked disorders. Their work is published in Nature Structural and Molecular Biology (Sarvan, et al. 2011 http://www.nature.com/nsmb/journal/v18/n7/full/nsmb.2093.html)
(a) Overall structure of ASH2L N-terminal domain. β-strands and α-helices are rendered in blue and orange, respectively; the zinc atom is depicted in green. (b) ASH2L harbors a structurally conserved helix-wing-helix domain. Evolutionarily conserved surface residues are colored according to the sequence alignment (Supplementary Fig. 1). (c) Superimposition of ASH2L and FOXO4 HWH domains. ASH2L is rendered as in a, and FOXO4 is colored in gray. (d,e) Electrostatic potential surface of FOXO4 (d) and ASH2L (e). DNA carbon atoms are rendered in yellow. Electrostatic potentials are contoured from +10 kBTe−1 (blue) to −10 kBTe−1 (red), where e is the electron, T is temperature and kB is the Boltzmann constant. Arrows indicate the canonical and putative DNA binding α-helix of FOXO4 and ASH2L.