BAIT

NUP116

NSP116, FG-nucleoporin NUP116, L000001293, YMR047C
FG-nucleoporin component of central core of the nuclear pore complex; contributes directly to nucleocytoplasmic transport and maintenance of the nuclear pore complex (NPC) permeability barrier; forms a stable association with Nup82p, Gle2p and two other FG-nucleoporins (Nsp1p and Nup159p); NUP116 has a paralog, NUP100, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

SSA1

YG100, Hsp70 family ATPase SSA1, L000002069, YAL005C
ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, and cell wall; 98% identical with paralog Ssa2p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.

Takano A, Kajita T, Mochizuki M, Endo T, Yoshihisa T

tRNAs are unique among various RNAs in that they shuttle between the nucleus and the cytoplasm, and their localization is regulated by nutrient conditions. Although nuclear export of tRNAs has been well documented, the import machinery is poorly understood. Here, we identified Ssa2p, a major cytoplasmic Hsp70 in Saccharomyces cerevisiae, as a tRNA-binding protein whose deletion compromises nuclear accumulation of ... [more]

Elife Apr. 09, 2015; 4(0); [Pubmed: 25853343]

Throughput

  • Low Throughput

Additional Notes

  • Figure 7

Curated By

  • BioGRID