Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain.
Mol Biol Cell
; 26(23): 4236-47, 2015 Nov 15.
Article
em En
| MEDLINE
| ID: mdl-26399296
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 (α, ß, and γ HCs) and >10 smaller subunits. Dynein light chain-1 (LC1) is an essential component of OAD. It is known to associate with the Chlamydomonas γ head domain, but its precise localization within the γ 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 γ 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 γ MTBD region. Together with observations that LC1 decreased the affinity of the γ MTBD for microtubules, we present a new model in which LC1 regulates OAD activity by modulating γ MTBD's affinity for the doublet microtubule.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Dineínas do Axonema
/
Microtúbulos
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article