TY  - GEN
T1  - Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
AU  - Varikkapulakkal, Amjadudheen
AU  - Ghosh, Anuraag
AU  - Mishra, Shravan Kumar
DO  - 10.17912/micropub.biology.000519
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000519/
AB  - Hub1/UBL5 has been reported to function in pre-mRNA splicing (Chanarat and Mishra, 2018; Wilkinson et al., 2004), DNA repair (Oka et al., 2015) and mitochondrial unfolding responses (Benedetti et al., 2006). It associates with proteins only non-covalently thereby modifying their functional properties (Chanarat, 2021). Through its Asp-22 surface Hub1 binds HIND segments on the splicing factor Snu66/SART1 and through its His-63 surface Hub1 binds the RNA helicase Prp5 required for spliceosome formation (Karaduman et al., 2017; Mishra et al., 2011). An earlier study of Hub1 adducts in S. cerevisiae has indicated that this UBL may also have a larger number of substrates (Lüders et al., 2003). However, identifying Hub1 substrates has been challenging, possibly due to its transient, weak or substoichiometric associations. We have performed a Y2H screen using S. cerevisiae Hub1 as bait fused to the DNA binding domain (BD) of the Gal4 transcription factor at the C-terminus. This fusion raises the possibility of identifying substrates binding through the N-terminal surface. Also, this fusion protein accumulated to higher levels in yeast (Fig. A).
PY  - 2022
JO  - microPublication Biology
ER  -