Background:
Prmt5 plays major role in regulation of gene expression, RNA processing,
cell growth and differentiation, signal transduction, germ cell development, etc., in mammals.
Prmt5 is also related to cancer. Knowing the proteins interacting with Prmt5 is important to understand
Prmt5’s function in cells. Although there have been reports on proteins binding with Prmt5 in
mammals, the partner proteins of Prmt5 in fish are still unclear.
Objectives:
The objective was to obtain proteins that bind with Prmt5 in medaka, a model fish.
Methods:
Yeast two hybridization was adopted to achieve the objective. Medaka Prmt5 was used
as a bait to fish the prey, binding proteins in a cDNA library of medaka. Co-immunoprecipitation
and in silicon analysis were performed to study the interaction of medaka Mep50 and Prmt5.
Results:
Eight proteins were identified to bind with Prmt5 from 69 preliminary positive colonies.
The binding proteins are methylosome protein 50 (Mep50), apolipoprotein A-I-like (Apo-AI), PR
domain containing protein 1a with zinc fingers (Prdm1a), Prdm1b, T-cell immunoglobulin mucin
family member 3 (Tim-3), phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide
synthase (Paics), NADH dehydrogenase subunit 4 (ND4) and
sciellin (Scl). Co-immunoprecipitation confirmed the interaction of medaka Prmt5 and Mep50.
Predicted structures of medaka Prtm5 and Mep50 are similar to that of human PRMT5 and
MEP50.
Conclusion:
Medaka Mep50, Prdm1a, Prdm1b, Apo-AI, Tim-3, Paics, ND4, and Scl bind with
Prmt5.
The N‐terminal domains of the paralogous HycE and Nuo
CD
govern assembly of the respective formate hydrogenlyase and
NADH
dehydrogenase complexes
