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PMID:20659974

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Citation

Anne, J (2010) Arginine methylation of SmB is required for Drosophila germ cell development. Development 137:2819-28

Abstract

Sm proteins constitute the common core of spliceosomal small nuclear ribonucleoproteins. Although Sm proteins are known to be methylated at specific arginine residues within the C-terminal arginine-glycine dipeptide (RG) repeats, the biological relevance of these modifications remains unknown. In this study, a tissue-specific function of arginine methylation of the SmB protein was identified in Drosophila. Analysis of the distribution of SmB during oogenesis revealed that this protein accumulates at the posterior pole of the oocyte, a cytoplasmic region containing the polar granules, which are necessary for the formation of primordial germ cells. The pole plasm localisation of SmB requires the methylation of arginine residues in its RG repeats by the Capsuléen-Valois methylosome complex. Functional studies showed that the methylation of these arginine residues is essential for distinct processes of the germline life cycle, including germ cell formation, migration and differentiation. In particular, the methylation of a subset of these arginine residues appears essential for the anchoring of the polar granules at the posterior cortex of the oocyte, whereas the methylation of another subset controls germ cell migration during embryogenesis. These results demonstrate a crucial role of arginine methylation in directing the subcellular localisation of SmB and that this modification contributes specifically to the establishment and development of germ cells.

Links

PubMed Online version:10.1242/dev.052944

Keywords

Animals; Animals, Genetically Modified; Arginine/metabolism; Cell Polarity; Drosophila/embryology; Drosophila/genetics; Drosophila/metabolism; Drosophila Proteins/chemistry; Drosophila Proteins/genetics; Drosophila Proteins/metabolism; Green Fluorescent Proteins/genetics; Green Fluorescent Proteins/metabolism; Methylation; Models, Biological; Mutagenesis, Site-Directed; Oocytes/metabolism; Oogenesis/genetics; Oogenesis/physiology; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Ribonucleoproteins, Small Nuclear/chemistry; Ribonucleoproteins, Small Nuclear/genetics; Ribonucleoproteins, Small Nuclear/metabolism; Subcellular Fractions/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DROME:SMD3

located_in

GO:0045495: pole plasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:TUD

located_in

GO:0045495: pole plasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:TUD

located_in

GO:0005737: cytoplasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:TUD

located_in

GO:0043186: P granule

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:RSMB

located_in

GO:0015030: Cajal body

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:RSMB

located_in

GO:0045495: pole plasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:RSMB

located_in

GO:0005634: nucleus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:RSMB

involved_in

GO:0008406: gonad development

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:RSMB

involved_in

GO:0007281: germ cell development

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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