title: Dcp1-bodies in mouse oocytes.
abstract: Processing bodies (P-bodies) are cytoplasmic granules involved in the storage and degradation of mRNAs. In somatic cells, their formation involves miRNA-mediated mRNA silencing. Many P-body protein components are also found in germ cell granules, such as in mammalian spermatocytes. In fully grown mammalian oocytes, where changes in gene expression depend entirely on translational control, RNA granules have not as yet been characterized. Here we show the presence of P-body-like foci in mouse oocytes, as revealed by the presence of Dcp1a and the colocalization of RNA-associated protein 55 (RAP55) and the DEAD box RNA helicase Rck/p54, two proteins associated with P-bodies and translational control. These P-body-like structures have been called Dcp1-bodies and in meiotically arrested primary oocytes, two types can be distinguished based on their size. They also have different protein partners and sensitivities to the depletion of endogenous siRNA/miRNA and translational inhibitors. However, both type progressively disappear during in vitro meiotic maturation and are virtually absent in metaphase II-arrested secondary oocytes. Moreover, this disassembly of hDcp1a-bodies is concomitant with the posttranslational modification of EGFP-hDcp1a.
authors.affiliation: Department of Genetic Medicine and Development, Faculty of Medicine, University of Geneva, 1211 Geneva 4, Switzerland.
authors.forename: Adam
authors.initials: A
authors.lastname: Swetloff
authors.forename: Beatrice
authors.initials: B
authors.lastname: Conne
authors.forename: Joachim
authors.initials: J
authors.lastname: Huarte
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Pitetti
authors.forename: Serge
authors.initials: S
authors.lastname: Nef
authors.forename: Jean-Dominique
authors.initials: JD
authors.lastname: Vassalli
mesh_terms: D000818:Animals; D002460:Cell Line; D003513:Cycloheximide / Q000494:pharmacology; D003594:Cytoplasmic Granules / Q000378:metabolism*; D053487:DEAD-box RNA Helicases / Q000235:genetics / Q000378:metabolism; D004722:Endoribonucleases / Q000235:genetics / Q000378:metabolism*; D005260:Female; D006801:Humans; D008540:Meiosis / Q000502:physiology; D051379:Mice; D008810:Mice, Inbred C57BL; D008822:Mice, Transgenic; D009865:Oocytes / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D014176:Protein Biosynthesis / Q000187:drug effects; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D011518:Proto-Oncogene Proteins / Q000235:genetics / Q000378:metabolism; D011691:Puromycin / Q000494:pharmacology; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012261:Ribonucleoproteins / Q000235:genetics / Q000378:metabolism; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism*
chemical_list: D011500:Protein Synthesis Inhibitors; D011518:Proto-Oncogene Proteins; D034741:RNA, Small Interfering; D016601:RNA-Binding Proteins; C510649:RNA-associated protein 55, human; C547586:Rap55A protein, mouse; C547587:Rap55B protein, mouse; D011993:Recombinant Fusion Proteins; D012261:Ribonucleoproteins; D015534:Trans-Activators; D011691:Puromycin; D003513:Cycloheximide; C490616:Ddx6 protein, mouse; D004722:Endoribonucleases; C466280:smad4-interacting protein SMIF, mouse; C466279:DCP1A protein, human; D053487:DEAD-box RNA Helicases