Back

Functional Anatomy of the TDP-43 Redox Sensor

zhou, x.; Sumrow, L.; Sutherland, L.; Liu, D.; Qin, T.; McKnight, S. L.; Liszczak, G.

2021-12-06 biochemistry
10.1101/2021.12.05.471332 bioRxiv
Show abstract

TAR binding protein 43 (TDP-43) is an RNA binding protein that assists in the maturation, export and sub-cellular localization of mRNA. The carboxyl terminal 153 residues of TDP-43 are of low sequence complexity and allow for self-association of the protein in a manner leading to its phase separation from an aqueous environment. These interactions assist TDP-43 in forming cytoplasmic RNA granules involved in the transport of mRNA for localized translation. Self-association of the TDP-43 low complexity (LC) domain is facilitated by a region of twenty five residues that are of extreme evolutionary conservation. The molecular basis for self-adherence of the protein through this region has been illuminated by a combination of structural and biochemical studies, allowing definition of a morphologically specific cross-{beta} structure predicted to be weakly assembled by main chain hydrogen bonds. In this study we have investigated the importance of individual, Pauling hydrogen bonds hypothesized to facilitate self-adherence of the TDP-43 LC domain.

Matching journals

The top 1 journal accounts for 50% of the predicted probability mass.