5 Interactions found (0.01 seconds)

"Recombinant HRPA-1 FL is capable of LLPS after cleavage of a maltose binding protein solubility tag."

"we analyzed the expression of hsp-12.6, a daf-16 downstream gene, by using qRT-PCR. The results showed that heat stress increased hsp- 12.6 expression (Fig. 2B) as previously reported (Hsu et al., 2003; McColl et al., 2010)."

gld-2 : grif-1

"In yeast, GRIF-1 robustly interacted with GLD-2(FL) but neither of the GLD-3 isoforms."; "GRIF-1 specifically associates with the GLD-2/3 cytoPAP complex, likely on P granules, by binding to the N-terminal IDR of GLD-2, using all of its protein domains for target recognition or stable association."

ife-1 : tbb-2

Using an in vivo reporter assay with an amino-terminal fusion to GFP, gld-1 ORF, and the gld-1 3' UTR, fluorescence microscopy showed that gld-1::gfp mRNA became de-repressed in immature oocytes in syncytium (Figure 4A). Upon depletion of IFE-1 by RNAi, the fluorescence in the whole distal region of the gonad was visibly diminished. Quantifying the mean GFP fluorescence intensity per exposure time (Fl/t), there was a reproducible two-fold increase in GLD-1:GFP expression when IFE-1 is present. Our data show that in immature oocytes, IFE-1 uniquely promotes the translation of gld-1 mRNA.

ife-1 : pos-1

pos-1 (posterior segregation) is natively repressed throughout most of oogenesis. It is de-repressed only in late stage oocytes so newly synthesized POS-1 protein can help to establish early embryonic polarity. The pos-1 3' UTR reporter showed accumulation of the H2B::GFP product only in nuclei of the three largest oocytes of live worms. Following IFE-1 knockdown, H2B:GFP expression was nearly absent from oocytes of all stages. Quantification of GFP (Fl/t) showed a three-fold increase in pos-1 3'UTR reporter translation by IFE-1. This indicates that when the pos-1 mRNA became natively de-repressed in the -3, -2, and -1 oocytes, it was primarily IFE-1 that recruited the mRNA for translation.