The hnRNP-like Nab3 termination factor can employ heterologous prion-like domains in place of its own essential low complexity domain.

ABSTRACT: Many RNA-binding proteins possess domains with a biased amino acid content. A common property of these low complexity domains (LCDs) is that they assemble into an ordered amyloid form, juxtaposing RNA recognition motifs in a subcellular compartment in which RNA metabolism is focused. Yeast Nab3 is one such protein that contains RNA-binding domains and a low complexity, glutamine/proline-rich, prion-like domain that can self-assemble. Nab3 also contains a region of structural homology to human hnRNP-C that resembles a leucine zipper which can oligomerize. Here we show that the LCD and the human hnRNP-C homology domains of Nab3 were experimentally separable, as cells were viable with either segment, but not when both were missing. In exploiting the lethality of deleting these regions of Nab3

SUBMITTER: Loya TJ 

PROVIDER: S-EPMC5638401 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature