NMR assignments for the C-terminal domain of human TDP-43.
 

NMR assignments for the C-terminal domain of human TDP-43.

Related Articles NMR assignments for the C-terminal domain of human TDP-43.

Biomol NMR Assign. 2021 Jan 08;:

Authors: Pantoja-Uceda D, Stuani C, Laurents DV, McDermott AE, Buratti E, Mompeán M

Abstract
Transactive response DNA-binding protein of 43*kDa (TDP-43) is a 414-residue protein whose aberrant aggregation is implicated in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) or frontotemporal lobar degeneration (FTLD). Intriguingly, TDP-43 has also been shown to functionally oligomerize to carry out physiological functions. TDP-43 also exists in mixed condensates or granules with other proteins (e.g. neuronal or stress granules), and its large C-terminal domain (CTD, residues 267-414) seems responsible for TDP-43 both homo- and heterotypic interactions underlying such diverse functional and pathological aggregation events. A myriad of distinct triggers may drive TDP-43 oligomerization, including interaction partners or changes in pH or salinity. In this Assignment Note, we report the complete backbone and a wealth of side chain chemical shift assignments for the CTD of TDP-43*at pH 4. The assignments presented here provide a solid starting point to study the aggregation pathway of TDP-43*at pH values below those considered physiological but relevant in pathological settings, and to contrast the aggregation behaviour under distinct conditions and in the presence of interacting partners.


PMID: 33417141 [PubMed - as supplied by publisher]



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