People

Faculty

Henn Arnon, Assistant Professor

Phone:  +972-4-8294839
Fax:  +972-4-8225153

Building/Auditory:  504

Research Interest

   The Action of Molecular Motors in the Cytoskeleton and in RNA Metabolism    
       
       We study the enzymology of diverse molecular motors to explore how they have adapted specific physiochemical properties for their cellular functions. Molecular motors exhibit a wide range of essential cellular function and they are found everywhere! Their timely and regulated function is essential to all cellular aspects of motility, cell division, cytoskeleton remodeling through all nucleic acid metabolism and biochemical pathways such as replication, translation and RNA degradation. Molecular motor enzymes utilize the chemical energy stored in ATP to produce biologically useful work. They share common mechanistic features in which the energy from ATP binding, hydrolysis and product release propagate conformational changes in the motor domain that can be further coupled to directional molecular motion, force and work production. Within this common general mechanism exists a wide diversity of enzymatic adaptations and structural organization differences between and within molecular motor families. For example, the Myosin family of molecular motors shares high structural homology within the motor domain, however individual myosins perform many diverse functions in the cell that require very different Mechanochemical Coupling between the different ligated states in the ATPase cycle. Such enzymatic adaptation can be achieved by modulation of the rate and equilibrium constants in the ATPase cycle. These effects are typically generated by sequence diversity in loops and highly mutation-prone regions in the polypeptide chain. One of the goals of our research is to discover and understand enzymatic adaptations in a variety of molecular motors including myosins, helicases, and polymerases. We intend to leverage this knowledge in the future to engineer novel nano-molecular machines with unique enzymatic properties.
 

More info can be found at the lab web page.