Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes.

ABSTRACT: Cytoplasmic dynein is a eukaryotic motor protein complex that, along with its regulatory protein dynactin, is essential to the transport of organelles within cells. The interaction of dynein with dynactin is regulated by binding between the intermediate chain (IC) subunit of dynein and the p150^Glued subunit of dynactin. Even though in the rat versions of these proteins this interaction primarily involves the single α-helix region at the N-terminus of the IC, in Drosophila and yeast ICs the removal of a nascent helix (H2) downstream of the single α-helix considerably diminishes IC-p150^Glued complex stability. We find that for ICs from various species, there is a correlation between disorder in H2 and its contribution to binding affinity, and that sequence variations in

SUBMITTER: Loening NM 

PROVIDER: S-EPMC7474177 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature