buc interacts with hermes | Interplay of RNA buc interacts with hermes Mechanistically, maternal Tdrd6 interacts with a demethylated tri-RG (arginine-glycine) motif within the C-terminus of Buc protein, which shows no homology to known .
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0 · rbpms2 functions in Balbiani body architecture and ovary fate
1 · The vertebrate Balbiani body, germ plasm, and oocyte polarity
2 · Quantification of Xvelo isoforms in oocytes injected with antisense
3 · Protein Interactions in Xenopus Germ Plasm RNP Particles
4 · Oocyte polarity requires a Bucky ball
5 · Multiplicity of Buc copies in Atlantic salmon contrasts with loss of
6 · Localization in Oogenesis of Maternal Regulators of Embryonic
7 · Interplay of RNA
8 · Functional equivalence of germ plasm organizers
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Vasa interacts with Buc, Buc (1–361) and Buc (1–601). As Osk activates Drosophila Vasa and Vasa triggers germ cell formation in zebrafish, we investigated, whether in vitro translated Osk-GFP binds to zebrafish Vasa. This protein interaction is conserved in Xenopus, where Velo1 (Buc homolog) can interact with Hermes (Rbpms family) (Nijjar and Woodland, 2013). However, Xenopus has a .
rbpms2 functions in Balbiani body architecture and ovary fate
In vertebrates, we identified the zebrafish bucky ball (buc) gene, which appears similar at the genetic level to Osk in Drosophila [17]. Buc mutants fail to assemble germ plasm, .
Organization of the oocyte into a polarized cell is initiated by an aggregate organelle called the Balbiani body (Bb), which sets up its initial asymmetry (Escobar-Aguirre, Elkouby, et .
The novel region interacts with the RNA-binding protein Hermes to initiate Balbiani body assembly probably by recruiting buc and other RNAs, including dazl, to the germ plasm . Mechanistically, maternal Tdrd6 interacts with a demethylated tri-RG (arginine-glycine) motif within the C-terminus of Buc protein, which shows no homology to known . We have identified and validated four proteins that interact with Hermes in germ plasm: two isoforms of Xvelo1 (a homologue of zebrafish Bucky ball) and Rbm24b and . Based on the localization of Buc protein and the dominant phenotypes of the cbuc transgenes, we hypothesize that an RNAbp could specifically interact with the spliced buc .
1 Altmetric. Abstract. Cell polarity generates intracellular asymmetries and functional regionalization in tissues and morphogenetic processes. Cell polarity in .Maternally inherited germline determinants in both vertebrates and invertebrates interact with aggregationprone, intrinsically disordered germ plasm "organizer" proteins, including Bucky ball. Vasa interacts with Buc, Buc (1–361) and Buc (1–601). As Osk activates Drosophila Vasa and Vasa triggers germ cell formation in zebrafish, we investigated, whether in vitro translated Osk-GFP binds to zebrafish Vasa. This protein interaction is conserved in Xenopus, where Velo1 (Buc homolog) can interact with Hermes (Rbpms family) (Nijjar and Woodland, 2013). However, Xenopus has a single reported rbpms gene, hermes, while zebrafish have three rbpms genes: rbpms (rbpms1), rbpms2a and .
In vertebrates, we identified the zebrafish bucky ball (buc) gene, which appears similar at the genetic level to Osk in Drosophila [17]. Buc mutants fail to assemble germ plasm, whereas its overexpression induces ectopic PGCs [17, 18].
Organization of the oocyte into a polarized cell is initiated by an aggregate organelle called the Balbiani body (Bb), which sets up its initial asymmetry (Escobar-Aguirre, Elkouby, et al., 2017; Kloc, Jedrzejowska, Tworzydlo, & Bilinski, 2014). The novel region interacts with the RNA-binding protein Hermes to initiate Balbiani body assembly probably by recruiting buc and other RNAs, including dazl, to the germ plasm [27, 32]. Zebrafish buc mutant oocytes failed to localize dazl mRNAs in the Balbiani body that resulted in embryos without animal-vegetal polarity [ 23 , 26 ]. Mechanistically, maternal Tdrd6 interacts with a demethylated tri-RG (arginine-glycine) motif within the C-terminus of Buc protein, which shows no homology to known proteins but functions as an organizer of the germ plasm (Bontems et al., .
We have identified and validated four proteins that interact with Hermes in germ plasm: two isoforms of Xvelo1 (a homologue of zebrafish Bucky ball) and Rbm24b and Rbm42b, both RNA-binding proteins containing the RRM motif.
Based on the localization of Buc protein and the dominant phenotypes of the cbuc transgenes, we hypothesize that an RNAbp could specifically interact with the spliced buc mRNA to prevent ectopic translation of buc transcripts. 1 Altmetric. Abstract. Cell polarity generates intracellular asymmetries and functional regionalization in tissues and morphogenetic processes. Cell polarity in development often relies on mechanisms of RNA localization to specific subcellular domains to define the identity of future developing tissues.Maternally inherited germline determinants in both vertebrates and invertebrates interact with aggregationprone, intrinsically disordered germ plasm "organizer" proteins, including Bucky ball.
The vertebrate Balbiani body, germ plasm, and oocyte polarity
Quantification of Xvelo isoforms in oocytes injected with antisense
Vasa interacts with Buc, Buc (1–361) and Buc (1–601). As Osk activates Drosophila Vasa and Vasa triggers germ cell formation in zebrafish, we investigated, whether in vitro translated Osk-GFP binds to zebrafish Vasa.
This protein interaction is conserved in Xenopus, where Velo1 (Buc homolog) can interact with Hermes (Rbpms family) (Nijjar and Woodland, 2013). However, Xenopus has a single reported rbpms gene, hermes, while zebrafish have three rbpms genes: rbpms (rbpms1), rbpms2a and . In vertebrates, we identified the zebrafish bucky ball (buc) gene, which appears similar at the genetic level to Osk in Drosophila [17]. Buc mutants fail to assemble germ plasm, whereas its overexpression induces ectopic PGCs [17, 18]. Organization of the oocyte into a polarized cell is initiated by an aggregate organelle called the Balbiani body (Bb), which sets up its initial asymmetry (Escobar-Aguirre, Elkouby, et al., 2017; Kloc, Jedrzejowska, Tworzydlo, & Bilinski, 2014). The novel region interacts with the RNA-binding protein Hermes to initiate Balbiani body assembly probably by recruiting buc and other RNAs, including dazl, to the germ plasm [27, 32]. Zebrafish buc mutant oocytes failed to localize dazl mRNAs in the Balbiani body that resulted in embryos without animal-vegetal polarity [ 23 , 26 ].
Mechanistically, maternal Tdrd6 interacts with a demethylated tri-RG (arginine-glycine) motif within the C-terminus of Buc protein, which shows no homology to known proteins but functions as an organizer of the germ plasm (Bontems et al., . We have identified and validated four proteins that interact with Hermes in germ plasm: two isoforms of Xvelo1 (a homologue of zebrafish Bucky ball) and Rbm24b and Rbm42b, both RNA-binding proteins containing the RRM motif. Based on the localization of Buc protein and the dominant phenotypes of the cbuc transgenes, we hypothesize that an RNAbp could specifically interact with the spliced buc mRNA to prevent ectopic translation of buc transcripts. 1 Altmetric. Abstract. Cell polarity generates intracellular asymmetries and functional regionalization in tissues and morphogenetic processes. Cell polarity in development often relies on mechanisms of RNA localization to specific subcellular domains to define the identity of future developing tissues.
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buc interacts with hermes|Interplay of RNA
