The dynein light chain 8 (LC8) binds predominantly "in-register" to a multivalent intrinsically disordered partner.

ABSTRACT: Dynein light chain 8 (LC8) interacts with intrinsically disordered proteins (IDPs) and influences a wide range of biological processes. It is becoming apparent that among the numerous IDPs that interact with LC8, many contain multiple LC8-binding sites. Although it is established that LC8 forms parallel IDP duplexes with some partners, such as nucleoporin Nup159 and dynein intermediate chain, the molecular details of these interactions and LC8's interactions with other diverse partners remain largely uncharacterized. LC8 dimers could bind in either a paired "in-register" or a heterogeneous off-register manner to any of the available sites on a multivalent partner. Here, using NMR chemical shift perturbation, analytical ultracentrifugation, and native electrospray ionization MS, we show tha

SUBMITTER: Reardon PN 

PROVIDER: S-EPMC7152752 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature