How kinesin-2 forms a stalk |
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Authors: | Vukajlovic Marija Dietz Hendrik Schliwa Manfred Ökten Zeynep |
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Institution: | University of Pennsylvania;aCenter for Integrated Protein Science Munich and Institute for Cell Biology, Ludwig-Maximilians-Universität, D-80336 Munich, Germany;bCenter for Integrated Protein Science Munich at the Physics Department and Walter Schottky Institute, Technische Universität München, D-85748 Garching, Germany |
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Abstract: | The heterotrimeric structure of kinesin-2 makes it a unique member of the kinesin superfamily; however, molecular details of the oligomer formation are largely unknown. Here we demonstrate that heterodimerization of the two distinct motor domains KLP11 and KLP20 of Caenorhabditis elegans kinesin-2 requires a dimerization seed of merely two heptads at the C terminus of the stalk. This heterodimeric seed is sufficient to promote dimerization along the entire length of the stalk, as shown by circular dichroism spectroscopy, Förster resonance energy transfer analysis, and electron microscopy. In addition to explaining the formation of the kinesin-2 stalk, the seed sequence identified here bears great potential for generating specific heterodimerization in other protein biochemical applications. |
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