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PMID: 16699504 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells.

Nature cell biology ·Vol. 8 ·No. 6 ·2006-06-00 ·Pages 623-30

Ancelin K, Lange UC, Hajkova P, Schneider R, Bannister AJ, Kouzarides T, Surani MA

Abstract

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. Blimp1-Prmt5 colocalization results in high levels of H2A/H4 R3 methylation in PGCs at E8.5. However, at E11.5, Blimp1-Prmt5 translocates from the nucleus to the cytoplasm, resulting in the loss of H2A/H4 R3 methylation at the time of extensive epigenetic reprogramming of germ cells. Subsequently, Dhx38, a putative target of the Blimp1-Prmt5 complex, is upregulated. Interestingly, expression of Dhx38 is also seen in pluripotent embryonic germ cells that are derived from PGCs when Blimp1 expression is lost. Our study demonstrates that Blimp1 is involved in a novel transcriptional regulatory complex in the mouse germ-cell lineage.

MeSH Terms
Active Transport, Cell Nucleus Adenosine Triphosphatases/genetics Age Factors Animals Arginine/metabolism Embryo, Mammalian Gene Expression Regulation Germ Cells/metabolism Histones/metabolism Methylation Mice Positive Regulatory Domain I-Binding Factor 1 Protein Binding Protein Methyltransferases/metabolism Protein-Arginine N-Methyltransferases Repressor Proteins/metabolism,physiology Transcription Factors/metabolism,physiology Transcription, Genetic
Chemicals
Histones Prdm1 protein, mouse Repressor Proteins Transcription Factors Arginine Positive Regulatory Domain I-Binding Factor 1 Protein Methyltransferases Prmt5 protein, mouse Protein-Arginine N-Methyltransferases Adenosine Triphosphatases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Ancelin Katia
Wellcome Trust/Cancer Research UK Gurdon Institute of Cancer and Developmental Biology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK.
Lange Ulrike C
Hajkova Petra
Schneider Robert
Bannister Andrew J
Kouzarides Tony
Surani M Azim
Article Info
Journal
Nature cell biology
Abbr.
Nat Cell Biol
ISSN
1465-7392
Published
2006-06-00
Epub
2006-00-14
Pages
623-30
Language
English
Region
England
NLM ID
100890575
Subset
IM
Grants
Wellcome Trust · United Kingdom
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