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The Sm protein methyltransferase PRMT 5 is not required for primordial germ cell specification in mice
Author(s) -
Li Ziwei,
Yu Juehua,
Hosohama Linzi,
Nee Kevin,
Gkountela Sofia,
Chaudhari Sonal,
Cass Ashley A,
Xiao Xinshu,
Clark Amander T
Publication year - 2014
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201489319
Subject(s) - biology , germline , protein arginine methyltransferase 5 , chromatin , methyltransferase , germ cell , dna methylation , methylation , microbiology and biotechnology , epigenetics , histone , cellular differentiation , genetics , gene expression , dna , gene
PRMT 5 is a type II protein arginine methyltransferase with roles in stem cell biology, reprograming, cancer and neurogenesis. During embryogenesis in the mouse, it was hypothesized that PRMT 5 functions with the master germline determinant BLIMP 1 to promote primordial germ cell ( PGC ) specification. Using a Blimp1 ‐ Cre germline conditional knockout, we discovered that Prmt5 has no major role in murine germline specification, or the first global epigenetic reprograming event involving depletion of cytosine methylation from DNA and histone H3 lysine 9 dimethylation from chromatin. Instead, we discovered that PRMT 5 functions at the conclusion of PGC reprograming I to promote proliferation, survival and expression of the gonadal germline program as marked by MVH . We show that PRMT 5 regulates gene expression by promoting methylation of the Sm spliceosomal proteins and significantly altering the spliced repertoire of RNA s in mammalian embryonic cells and primordial cells.