Axonemal dynein light chain-1 locates at the microtubule-binding domain of the ? heavy chain.

ABSTRACT: The outer arm dynein (OAD) complex is the main propulsive force generator for ciliary/flagellar beating. In Chlamydomonas and Tetrahymena, the OAD complex comprises three heavy chains (?, ?, and ? HCs) and >10 smaller subunits. Dynein light chain-1 (LC1) is an essential component of OAD. It is known to associate with the Chlamydomonas ? head domain, but its precise localization within the ? head and regulatory mechanism of the OAD complex remain unclear. Here Ni-NTA-nanogold labeling electron microscopy localized LC1 to the stalk tip of the ? head. Single-particle analysis detected an additional structure, most likely corresponding to LC1, near the microtubule-binding domain (MTBD), located at the stalk tip. Pull-down assays confirmed that LC1 bound specifically to the ? MTBD region. Together with observations that LC1 decreased the affinity of the ? MTBD for microtubules, we present a new model in which LC1 regulates OAD activity by modulating ? MTBD's affinity for the doublet microtubule.

SUBMITTER: Ichikawa M 

PROVIDER: S-EPMC4642857 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature