MYOSIN-V · Single molecule mechanical and imaging studies of myosin-V

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Project objective

The aim of this project is to study the basic mechanisms of myosin-V motility using a combination of single molecule techniques. Many types of cellular motility are based on the cyclical interaction of myosin and actin, coupled to the hydrolysis of ATP. Myosins class V are found in neurons and form dimeric, processive motor molecules moving their cargo along actin filaments for many steps per diffusional encounter. However the basic mechanisms of chemo-mechanical energy transduction and head-head coordination remain unclear. Based on the host lab previous work I will develop an optical tweezers based technique for ultra-high-speed detection of single molecule mechanical interactions. I aim to combine these mechanical measurements with fluorescence microscopy to correlate mechanical and biochemical states during the catalytic cycle of a single motor head. The next step will be to resolve biochemical states during processive movement of the dimeric molecule. Specific immobilisation of myosin on substrate surfaces will be critical in these experiments. I will use atomic force microscopy to image myosin-V molecules bound to substrate surfaces and to actin filaments. The experiments will be carried out using recombinant single and double-headed myosin-V constructs expressed in collaboration with JR Sellers lab at NIH. The combination of highly sensitive mechanical measurements with fluorescence will open up new opportunities to characterise protein interactions on the single molecule level in general.

Original text from CORDIS.

Participants

• MEDICAL RESEARCH COUNCIL · LONDONCoordinatorUnited Kingdom

Links

• View on CORDIS