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Dyneins are 1-2 MDa complexes that translocate along microtubules. These enzymes are essential for many intracellular activities and provide the power for ciliary/flagellar motility in eukaryotes. In addition to the motor units themselves, dyneins contain multiple components that are required for the regulation of motor function and for attaching the enzyme to the appropriate intracellular cargo. We will discuss two different studies aimed at understanding dynein function. 1) In Chlamydomonas, three components of the flagellar outer dynein arm are redox-active - two are thioredoxins and the third binds Ca2+ in a redox-sensitive manner. Our recent data suggest that Chlamydomonas flagellar redox poise is linked to light/dark conditions and modulates the redox state of these outer arm proteins. 2) Our laboratory also uses NMR spectroscopy to investigate the high-resolution structure of dynein proteins. Analysis of the solution structure of the Tctex1 light chain has allowed us to propose a model by which this protein attaches various intracellular cargoes to dynein.