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Gene Review

csul  -  capsuleen

Drosophila melanogaster

Synonyms: CG3730, Csul, DART5, Dart5, Dmel\CG3730, ...
 
 
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Disease relevance of csul

  • Transgenic expression of Dart5 exclusively within the female germline rescues pole-cell formation, whereas ubiquitous expression rescues sDMA modification of Sm proteins and male sterility [1].
 

High impact information on csul

  • In particular, we show that the nuage and pole plasm localization of Tudor, an essential component for germ cell formation, are abolished in csul mutant germ cells [2].
  • Using the Capsuleen (Csul) methyltransferase as bait in the yeast two-hybrid system, we have identified a novel Drosophila protein containing multiple WD repeats and encoded by the valois (vsl) gene, which acts in pole plasm function [3].
  • CONCLUSIONS: We have shown that Dart5-mediated methylation of Sm proteins is not essential for snRNP biogenesis [1].
  • The Sm-protein methyltransferase, dart5, is essential for germ-cell specification and maintenance [1].
  • In the absence of dart5, snRNP biogenesis is surprisingly unaffected, and homozygous mutant animals are completely viable [1].
 

Biological context of csul

  • Because disruption of both dart5 and valois causes the specific loss of sDMA-modified Sm proteins and studies in C. elegans show that Sm proteins are required for germ-granule localization, we propose that Sm protein methylation is a pivotal event in germ-cell development [1].
 

Anatomical context of csul

  • The results uncover a novel role for dart5 in specification of the germline and in spermatocyte maturation [1].
  • Embryos laid by dart5 mutants fail to form pole cells, and Tudor localization is disrupted in stage 10 oocytes [1].
  • Scrib1 synthesis in mesodermal cells was independent of pole cells and occurred in agametic valois and capsuléen embryonic gonads [4].
 

Associations of csul with chemical compounds

  • In addition, JBP1 co-immunoprecipitates with several other proteins, which serve as methyl group acceptors and which may represent physiological targets of this methyltransferase [5].

References

 
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