Article

 

Interactions of yeast dynein with dynein light chain and dynactin: General implications for intrinsically disordered duplex scaffolds in multi-protein assemblies Public Deposited

Downloadable Content

Download PDF
https://ir.library.oregonstate.edu/concern/articles/wh246x807

Access to this item has been restricted by repository administrators at the request of the publisher until August 7, 2016.

This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by the American Society for Biochemistry and Molecular Biology and can be found at:  http://www.jbc.org/

This research was originally published in the Journal of Biological Chemistry. Jie, J., Löhr, F., & Barbar, E. Interactions of Yeast Dynein with Dynein Light Chain and Dynactin: General implications for intrinsically disordered duplex scaffolds in multi-protein assemblies. Journal of Biological Chemistry. 2015. 290:23863-23874. © the American Society for Biochemistry and Molecular Biology.

Descriptions

Attribute NameValues
Creator
Abstract
  • Intrinsically disordered protein (IDP) duplexes composed of two IDP chains cross-linked by bivalent partner proteins form scaffolds for assembly of multiprotein complexes. The N-terminal domain of dynein intermediate chain (N-IC) is one such IDP that forms a bivalent scaffold with multiple dynein light chains including LC8, a hub protein that promotes duplex formation of diverse IDP partners. N-IC also binds a subunit of the dynein regulator, dynactin. Here we characterize interactions of a yeast ortholog of N-IC (N-Pac11) with yeast LC8 (Dyn2) or with the intermediate chain-binding subunit of yeast dynactin (Nip100). Residue level changes in Pac11 structure are monitored by NMR spectroscopy, and binding energetics are monitored by isothermal titration calorimetry (ITC). N-Pac11 is monomeric and primarily disordered except for a single α-helix (SAH) at the N terminus and a short nascent helix, LH, flanked by the two Dyn2 recognition motifs. Upon binding Dyn2, the only Pac11 residues making direct protein-protein interactions are in and immediately flanking the recognition motifs. Dyn2 binding also orders LH residues of Pac11. Upon binding Nip100, only Pac11 SAH residues make direct protein-protein interactions, but LH residues at a distant sequence position and L1 residues in an adjacent linker are also ordered. The long distance, ligand-dependent ordering of residues reveals new elements of dynamic structure within IDP linker regions.
Resource Type
DOI
Date Available
Date Issued
Citation
  • Jie, J., Löhr, F., & Barbar, E. (2015). Interactions of Yeast Dynein with Dynein Light Chain and Dynactin: General implications for intrinsically disordered duplex scaffolds in multi-protein assemblies. Journal of Biological Chemistry, 290(39), 23863-23874. doi:10.1074/jbc.M115.649715
Series
Keyword
Rights Statement
Funding Statement (additional comments about funding)
  • This work is supported by National Institutes of Health Grant GM 084276 to EB. We acknowledge the support of the protein core facility in the OSU Environmental Health Sciences Center (NIH/NIEHS 00210), and access to the Research Infrastructure activity in the 7th Framework Programme of the EC (Project number: 261863, Bio-NMR) (Frankfurt, Germany).
Publisher
Peer Reviewed
Language
Replaces

Relationships

Parents:

This work has no parents.

Items