GROUP DJINOVIC | Biochemistry & Biophysics, Structural & Computational Biology
Structural Biology of the Cytoskeleton
Model of Hfq RNA chaperone function (Nucleic Acids Research, 2012; 10.1093/nar/gks510). The sRNA displayed by the full-atom model with atoms colour-coded is shown bound to the proximal face of E. coli HfqEc (green solvent accessible surface). Through conformational fluctuations the sRNA can cover a larger conformational space (9 representative DsrA34 models are displayed with their solvent accessible surface). The mRNA is bound on the distal side represented by polyA9 orange flat cartoon representation. The model of a hypothetical mRNA chain is displayed in orange oval cartoon. HfqEc acts by restructuring the mRNA, which may be accomplished by the conformationally flexible C-termini. The structural variability of both RNAs in a transient ternary 1:1:1 complex would allow to sample large spaces. In this way HfqEc would not only act as a platform for binding and by increasing the local concentration of both ligands, but would also serve to promote their flexibility, and consequently successful annealing in a stochastic manner.
We are interested in the molecular mechanisms underlying the actin-based cytoskeleton of the striated muscle. A striking feature of muscle proteins, and particularly of the specialised striated muscle sarcomere compartment Z-disk, is the high frequency of multiple protein-protein interactions. We aim to generate detailed structural information on the protein-protein interaction network in the Z-disk, from its basic components - alpha-actinin and filamin C – to macromolecular complexes and the adaptor and regulatory Z-disk proteins centred on them.