Assistant Professor Arnon Henn

Research Interests:

Cell biology, biochemistry, biophysics and engineering of molecular motors

Short Synopsis:

Molecular motors couple a chemical energy potential to generate force over a distance that results in mechanical work. They share a common general ATPase mechanism in which the energy from ATP binding, hydrolysis and product release is utilized to drive conformational changes in the motor domain. These conformational changes can be amplified to a relatively large power stroke that is coupled to productive mechanical work. Within this common general ATPase utilization mechanism exists a wide diversity of enzymatic adaptations and unique structural organization. These diversifications of each molecular motor determine their specialization for specific biological functions. For example, the Myosin family of molecular motors shares high structural homology within the motor domain and conserved mechanochemical transduction pathways. However, the time transition between the biochemical intermediates and the dwelling times of the different structural states are diverse among the myosin family members and hence create a repertoire of myosins that are tailored for diverse functions in the cell.

 

1. Henn, A., and De La Cruz, E.M. (2005). Vertebrate myosin VIIb is a high duty ratio motor adapted for generating and maintaining tension. The Journal of biological chemistry  280, 39665-39676. PubMed
2. Henn, A., Cao, W., Hackney, D.D., and De La Cruz, E.M. (2008). The ATPase cycle mechanism  of the DEAD-box rRNA helicase, DbpA. Journal of molecular biology 377, 193-205  PubMed
3. Henn, A., Cao, W., Licciardello, N., Heitkamp, S.E., Hackney, D.D., and De La Cruz, E.M. (2010). Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proceedings of the National Academy of Sciences of the United States of America 107, 4046-4050. PubMed
4. Henn, A., Bradley, M.J., and De La Cruz, E.M. (2012). ATP utilization and RNA conformational rearrangement by DEAD-box proteins. Annual review of biophysics   41, 247-267. PubMed