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Blimp1 prmt5

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https://www.readbyqxmd.com/read/25519955/the-sm-protein-methyltransferase-prmt5-is-not-required-for-primordial-germ-cell-specification-in-mice
#1
Ziwei Li, Juehua Yu, Linzi Hosohama, Kevin Nee, Sofia Gkountela, Sonal Chaudhari, Ashley A Cass, Xinshu Xiao, Amander T Clark
PRMT5 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 PRMT5 functions with the master germline determinant BLIMP1 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...
March 12, 2015: EMBO Journal
https://www.readbyqxmd.com/read/19578939/expression-pattern-of-prmt5-in-adult-fish-and-embryos-of-medaka-oryzias-latipes
#2
W Chen, M Cao, Y Yang, Y Nagahama, H Zhao
DNA methylation is an important biochemical epigenetic determinant of gene expression in cells and therefore actively involved in gene regulation, chromosomal conformation, and protein activity. Protein arginine methyltransferases (PRMTs) play a major role in the methylation of proteins that have an arginine residue, catalyzing both the asymmetric dimethylation of arginine (aDMA) and symmetric dimethylation of arginine (sDMA). PRMT5, a type II PRMT which catalyzes sDMA, has been shown to have a pivotal role in pole plasm assembly and germ cell development in Drosophila and also to be an associate factor of Blimp1 for germ cell development in mouse...
August 2009: Fish Physiology and Biochemistry
https://www.readbyqxmd.com/read/18992153/expression-of-blimp1-prmt5-and-concurrent-histone-h2a-h4-arginine-3-dimethylation-in-fetal-germ-cells-cis-igcnu-and-germ-cell-tumors
#3
Dawid Eckert, Katharina Biermann, Daniel Nettersheim, Ad J M Gillis, Klaus Steger, Hans-Martin Jäck, Annette M Müller, Leendert H J Looijenga, Hubert Schorle
BACKGROUND: Most testicular germ cell tumors arise from intratubular germ cell neoplasia unclassified (IGCNU, also referred to as carcinoma in situ), which is thought to originate from a transformed primordial germ cell (PGC)/gonocyte, the fetal germ cell. Analyses of the molecular profile of IGCNU and seminoma show similarities to the expression profile of fetal germ cells/gonocytes. In murine PGCs, expression and interaction of Blimp1 and Prmt5 results in arginine 3 dimethylation of histone H2A and H4...
2008: BMC Developmental Biology
https://www.readbyqxmd.com/read/18953407/reprogramming-primordial-germ-cells-into-pluripotent-stem-cells
#4
Gabriela Durcova-Hills, Fuchou Tang, Gina Doody, Reuben Tooze, M Azim Surani
BACKGROUND: Specification of primordial germ cells (PGCs) results in the conversion of pluripotent epiblast cells into monopotent germ cell lineage. Blimp1/Prmt5 complex plays a critical role in the specification and maintenance of the early germ cell lineage. However, PGCs can be induced to dedifferentiate back to a pluripotent state as embryonic germ (EG) cells when exposed to exogenous signaling molecules, FGF-2, LIF and SCF. METHODOLOGY AND PRINCIPAL FINDINGS: Here we show that Trichostatin A (TSA), an inhibitor of histone deacetylases, is a highly potent agent that can replace FGF-2 to induce dedifferentiation of PGCs into EG cells...
2008: PloS One
https://www.readbyqxmd.com/read/16699504/blimp1-associates-with-prmt5-and-directs-histone-arginine-methylation-in-mouse-germ-cells
#5
Katia Ancelin, Ulrike C Lange, Petra Hajkova, Robert Schneider, Andrew J Bannister, Tony Kouzarides, M Azim Surani
Blimp1, a transcriptional repressor, has a crucial role in the specification of primordial germ cells (PGCs) in mice at embryonic day 7.5 (E7.5). This SET-PR domain protein can form complexes with various chromatin modifiers in a context-dependent manner. Here, we show that Blimp1 has a novel interaction with Prmt5, an arginine-specific histone methyltransferase, which mediates symmetrical dimethylation of arginine 3 on histone H2A and/or H4 tails (H2A/H4R3me2s). Prmt5 has been shown to associate with Tudor, a component of germ plasm in Drosophila melanogaster...
June 2006: Nature Cell Biology
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