Erschienen:
American Society for Cell Biology (ASCB), 2011
Erschienen in:
Molecular Biology of the Cell, 22 (2011) 22, Seite 4279-4287
Sprache:
Englisch
DOI:
10.1091/mbc.e11-02-0112
ISSN:
1059-1524;
1939-4586
Entstehung:
Anmerkungen:
Beschreibung:
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.