Function of Motor Proteins and Motor Protein Constructs at the Molecular Level Assessed by Different Single-Molecule Detection Techniques

• Applicant: Professor Dr. Bernhard Brenner (†)
• Subject Area: Biophysics
• Term: from 1999 to 2009
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 5176032

As an integral part of the Schwerpunkt 'Molecular Motors' the contribution of our project is the functional characterization of myosin molecules and myosin molecule fragments. This involves both wild type molecules, as well as chimeras and molecules with well-aimed point mutations expressed in Dictyostelium discoideum. The main goal of these studies is (i) to develop an understanding of the processes associated with ATP-hydrolysis by the catalytic domain which is almost identical for myosins and kinesins, and very similar to that of the F1-ATPase and G-proteins. (ii) We have to evaluate the function of additional structural modules within the myosin head domain, like lever arms, variable loop elements, or binding blocks for regulatory proteins and cytoskeletal structures, as elements for amplification, modulation and regulation of the primary events inside the catalytic domain. (iii) We have to dissect pathways of 'cross-communication' between the catalytic domain and such additional modules. For the current funding period we have to establish additional protocols to expand our spectrum of available parameters to assess functional properties of myosins and myosin-mutants. In close collaboration with the laboratories of M. Bähler and D.J. Manstein we will apply these approaches to characterize functional differences to unconventional myosins, chimeras and mutant myosins as they become available through these collaborations.

• DFG Programme: Priority Programmes
• Subproject of: SPP 1068: Molekulare Motoren