Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuléen

Development

Volumn 132, Issue 9, 2005, Pages 2167-2177

  Anne, Joël ^a   Mechler, Bernard M ^a  

^a GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

Author keywords

Drosophila; Oogenesis; Pole plasm assembly; Tudor; Valois

Indexed keywords

CAPSULEEN PROTEIN; CELL PROTEIN; DROSOPHILA PROTEIN; METHYLTRANSFERASE; OSKAR PROTEIN; RIBONUCLEOPROTEIN; TUDOR PROTEIN; UNCLASSIFIED DRUG; VALOIS PROTEIN;

ALLELE; ANIMAL CELL; ARTICLE; BINDING ASSAY; DROSOPHILA; GENE SEQUENCE; IMMUNOCYTOCHEMISTRY; IMMUNOPRECIPITATION; NONHUMAN; OOCYTE DEVELOPMENT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN SYNTHESIS;

AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; DROSOPHILA; DROSOPHILA PROTEINS; FEMALE; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; OOGENESIS; PROTEIN METHYLTRANSFERASES; RECOMBINANT FUSION PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES;

ANIMALIA;

EID: 19744373880     PISSN: 09501991     EISSN: None     Source Type: Journal    
DOI: 10.1242/dev.01809     Document Type: Article

References (65)

1. Akiyama, T. and Okada, M. (1992). Spatial and developmental changes in the respiratory activity of mitochondria in early Drosophila embryos. Development 115, 1175-1182.
2. Amikura, R., Hanyu, K., Kashikawa, M. and Kobayashi, S. (2001). Tudor protein is essential for the localization of mitochondrial RNAs in polar granules of Drosophila embryos. Mech. Dev. 107, 97-104.
3. Bardsley, A., McDonald, K. and Boswell, R. E. (1993). Distribution of Tudor protein in the Drosophila embryo suggests separation of functions based on site of localization. Development 119, 207-219.
4. Boswell, R. E. and Mahowald, A. P. (1985). tudor, a gene required for assembly of the germ plasm in Drosophila melanogaster. Cell 43, 97-104.
5. Breitwieser, W., Markussen, F.-H., Horstmann, H. and Ephrussi, A. (1996). Oskar protein interaction with Vasa represents an essential step in polar granule assembly. Genes Dev. 10, 2179-2188.
6. Brahms, H., Meheus, L., de Brabandere, V., Fischer, U. and Lührmann, R. (2001). Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7, 1531-1542.
7. Branscombe, T. L., Frankel, A., Lee, J.-H., Cook, J. R., Yang, Z.-h., Pestka, S. and Clarke, S. (2001). PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 276, 32971-32976.
8. Bühler, D., Raker, V., Lührmann, R. and Fischer, U. (1999). Essential role fort he tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy. Hum. Mol. Genet. 8, 2351-2357.
9. Callebaut, I. and Mornon, J.-P. (1997). The human EBNA-2 coactivator plOO: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development. Biochem. J. 321, 125-132.
10. Cavey, M., Hijal, S., Zhang, X. and Suter, B. (2005). Drosophila valois encodes a divergent WD protein that is required for Vasa localization and Oskar protein accumulation. Development 132, 459-468.
11. Chothia, C., Hubbard, T., Brenner, S., Barns, H. and Murzin, A. (1997). Protein folds in the all-beta and all-alpha classes. Annu. Rev. Biophys. Biomol. Struct. 26, 597-627.
12. Clegg, N. J., Frost, D. M., Larkin, M. K., Subrahmanyan, L., Bryant, Z. and Ruohola-Baker, H. (1997). maelstrom is required for an early step in the establishment of Drosophila oocyte polarity: posterior localization of grk mRNA. Development 124, 4661-4671.
13. Ephrussi, A. and Lehmann, R. (1992). Induction of germ cell formation by oskar. Nature 358, 387-392.
14. Ephrussi, A., Dickenson, L. K. and Lehmann, R. (1991). oskar organizes the germ plasm and directs localization of the posterior determinant nanos. Cell 66, 37-50.
15. Findley, S. D., Tamanaha, M., Clegg, N. J. and Ruohola-Baker, H. (2003). Maelstrom, a Drosophila spindle-class gene, encodes a protein that colocalizes with Vasa and RDE1/AGO1 homolog, Aubergine, in nuage. Development 130, 859-871.
16. Friesen, W. J., Massenet, S., Paushkin, S., Wyce, A. and Dreyfuss, G. (2001a). SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell 7, 1111-1117.
17. Friesen, W. J., Paushkin, S., Wyce, A., Massenet, S., Pesiridis, G. S., van Duyne, G., Rappsilber, J., Mann, M. and Dreyfuss, G. (2001b). The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. Mol. Cell. Biol. 21, 8289-8300.
18. Friesen, W. J., Wyce, A., Paushkin, S., Abel, L., Rappsilber, J., Mann, M. and Dreyfuss, G. (2002). A novel WD repeat protein component of the methylosome binds Sm proteins. J. Biol. Chem. 277, 8243-8247.
19. Frohnhöfer, H. G., Lehmann, R. and Nüsslein-Volhard, C. (1986). Manipulating the anteroposterior pattern of the Drosophila embryo. J. Embryol. Exp. Morph. Suppl 97, 169-179.
20. Gavis, E. R., Lunsford, L., Bergsten, S. E. and Lehmann, R. (1996). A conserved 90 nucleotide element mediates translational repression of nanos RNA. Development 122, 2791-2800.
21. Geigy, R. (1931). Action de l'ultraviolet sur le pôle germinal dans l'oeuf de Drosophila melanogaster: castration et mutabilité. Rev. Suisse Zool. 38, 187-288.
22. Golumbeski, G. S., Bardsley, A., Tax, F. and Boswell, R. E. (1991). tudor, a posterior-group gene of Drosophila melanogaster, encodes a novel protein and an mRNA localized during mid-oogenesis. Genes Dev. 5, 2060-2070.
23. González-Reyes, A., Elliott, H. and St Johnston, D. (1997). Oocyte determination and the origin of polarity in Drosophila: the role of the spindle genes. Development 124, 4927-4937.
24. Harris, A. N. and Macdonald, P. M. (2001). Aubergine encodes a Drosophila polar granule component required for pole cell formation and related to eIF2C. Development 128, 2823-2832.
25. Hay, B., Ackerman, L., Barbel, S., Jan, L. Y. and Jan, Y. N. (1988a). Identification of a component of Drosophila polar granules. Development 103, 625-640.
26. Hay, B., Jan, L. Y. and Jan, Y. N. (1988b). A protein component of the Drosophila polar granules is encoded by vasa and has extensive sequence similarity to ATP-dependent helicases. Cell 55, 577-587.
27. Hay, B., Jan, L. Y. and Jan, Y. N. (1990). Localization of vasa, a component of Drosophila polar granules, in maternal-effect mutants that alter embryonic anteroposterior polarity. Development 109, 425-433.
28. Huettner, A. F. (1923). The origin of the germ cells in Drosophila melanogaster. J. Morphol. 37, 385-423.
29. Iida, T. and Kobayashi, S. (1998). Essential role of mitochondrially encoded large rRNA for germ-line formation in Drosophila embryos. Proc. Natl. Acad. Sci. USA 95, 11274-11278.
30. Illmensee, K. and Mahowald, A. P. (1974). Transplantation of posterior polar plasm in Drosophila. Induction of germ cells at the anterior pole of the egg. Proc. Natl. Acad. Sci. USA 71, 1016-1020.
31. Illmensee, K., Mahowald, A. P. and Loomis, M. R. (1976). The ontogeny of germ plasm during oogenesis in Drosophila. Dev. Biol. 49, 40-65.
32. Jongens, T. A., Hay, B., Jan, L. Y. and Jan, Y. N. (1992). The germ cell-less gene product: a posteriorly localized component necessary for germ cell development in Drosophila. Cell 70, 569-584.
33. Jongens, T. A., Ackerman, L. D., Swedlow, J. R., Jan, L. Y. and Jan, Y. N. (1994). Germ cell-less encodes a cell type-specific nuclear pore-associated protein and functions early in the germ-cell specification pathway of Drosophila. Genes Dev. 8, 2123-2136.
34. Kim, J.-S. and Raines, R. T. (1993). Ribonuclease S-peptide as a carrier in fusion proteins. Protein Sci. 2, 348-356.
35. Kim-Ha, J., Smith, J. L. and Macdonald, P. M. (1991). oskar mRNA is localized to the posterior pole of the Drosophila oocyte. Cell 66, 23-35.
36. Lasko, P. and Ashburner, M. (1988). The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A. Nature 335, 611-617.
37. Lasko, P. and Ashburner, M. (1990). Posterior localization of vasa protein correlates with, but is not sufficient for, pole cell development. Genes Dev. 4, 905-921.
38. Lefebvre, S., Bürglen, L., Reboullet, S., Clermont, O., Burlet, P., Viollet, L., Benichou, B., Cruaud, C., Millasseau, P., Zeviani, M. et al. (1995). Identification and characterization of a spinal muscular atrophy-determining gene. Cell 80, 155-165.
39. Lehmann, R. and Nüsslein-Volhard, C. (1986). Abdominal segmentation, pole cell formation, and embryonic polarity require the localized activity of oskar, a maternal gene of Drosophila. Cell 47, 141-152.
40. Lehmann, R. and Nüsslein-Volhard, C. (1991). The maternal gene nanos has a central role in posterior pattern formation in the Drosophila embryo. Development 112, 679-691.
41. Liang, L., Diehl-Jones, W. and Lasko, P. (1994). Localization of vasa protein to the Drosophila pole plasm is independent of its RNA-binding and helicase activities. Development 120, 1201-1211.
42. Liu, Q., Fischer, U., Wang, F. and Dreyfuss, G. (1997). The spinal muscular atrophy disease gene product, SMN, and ist associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell 90, 1013-1021.
43. Mahowald, A. P. (1962). Fine structure of pole cells and polar granules in Drosophila melanogaster. J. Exp. Zool. 151, 201-215.
44. Markussen, F.-H., Michon, A.-M., Breitwieser, W. and Ephrussi, A. (1995). Translational control of oskar generates Short OSK, the isoform that induces pole plasm assembly. Development 121, 3723-3732.
45. Meister, G., Eggert, C., Bühler, D., Brahms, H., Kambach, C. and Fischer, U. (2001). Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr. Biol. 11, 1990-1994.
46. Meister, G., Eggert, C. and Fischer, U. (2002). SMN-mediated assembly of RNPs: a complex story. Trends Cell Biol. 12, 472-478.
47. Okada, M., Kleinman, I. A. and Schneiderman, H. A. (1974). Restoration of fertility in sterilized Drosophila eggs by transplantation of polar cytoplasm. Dev. Biol. 37, 43-54.
48. Pontig, C. P. (1997). Tudor domains in poteins that interact with RNA. Trends Biochem. Sci. 22, 51-52.
49. Rigaut, G, Shevchenko, A., Rutz, B., Wilm, M., Mann, M. and Séraphin, B. (1999). A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032.
50. Rongo, C., Gavis, E. R. and Lehmann, R. (1995). Localization of oskar RNA Regulates oskar translation and requires Oskar protein. Development 121, 2737-2746.
51. Sano, H., Nakamura, A. and Kobayashi, S. (2002). Identification of a transcriptional regulatory region for germline-specific expression of vasa gene in Drosophila melanogaster. Mech. Dev. 112, 129-139.
52. Schüpbach, T. and Wieschaus, E. (1986). Maternal-effect mutations altering the anterior-posterior pattern of the Drosophila embryo. Roux's Arch. Dev. Biol. 195, 302-317.
53. Selenko, P., Sprangers, R., Stier, G., Bühler, D., Fischer, U. and Sattler, M. (2001). SMN Tudor domain structure and its interaction with the Sm proteins. Nat. Struct. Biol. 8, 27-31.
54. Smith, J. L., Wilson, J. E. and Macdonald, P. M. (1992). Overexpression of oskar directs ectopic activation of nanos and presumptive pole cell formation in Drosophila embryos. Cell 70, 849-859.
55. Smith, T. F., Gaitatzes, C., Saxena, K. and Neer, E. J. (1999). The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci. 24, 181-185.
56. Snee, M. J. and Macdonald, P. M. (2003). Live imaging of nuage and polar granules: evidence against a precursor-product relationship and a novel role of Oskar in stabilization of polar granule components. J. Cell Sci. 117, 2109-2120.
57. Styhler, S., Nakamura, A., Swan, A., Suter, B. and Lasko, P. (1998). vasa is required for Gurken accumulation in the oocyte, and is involved in oocyte differentiation and germline cyst development. Development 125, 1569-1578.
58. Styhler, S., Nakamura, A. and Lasko, P. (2002). VASA localization requires the SPRY-domain and SOCS-box containing protein, GUSTAVUS. Dev. Cell 3, 865-876.
59. Thomson, T. and Lasko, P. (2004). Drosophila tudor is essential for polar granule assembly and pole cell specification, but not for posterior patterning. Genesis 40, 164-170.
60. Tomancak, P., Guichet, A., Zavorszky, P. and Ephrussi, A. (1998). Oocyte polarity depends on regulation of gurken by Vasa. Development 125, 1723-1732.
61. Török, I., Herrmann-Horle, D., Kiss, I., Tick, G., Speer, G., Schmitt, R. and Mechler, B. M. (1999). Down-regulation of RpS21, a putative translation initiation factor interacting with P40, produces viable minute imagos and larval lethality with overgrown hematopoietic organs and imaginal discs. Mol. Cell. Biol. 19, 2308-2321.
62. Wang, C. and Lehmann, R. (1991). nanos is the localized posterior determinant in Drosophila. Cell 66, 637-647.
63. Wang, C., Dickinson, L. K. and Lehmann, R. (1994). Genetics of nanos localization in Drosophila. Dev. Dyn. 199, 103-115.
64. Wilson, J. E., Connell, J. E. and Macdonald, P. M. (1996). aubergine enhances oskar translation in the Drosophila ovary. Development 122, 1631-1639.
65. Yu, L., Gaitatzes, C., Neer, E. and Smith, T. F. (2000). Thirty-plus functional families from a single motif. Protein Sci. 9, 2470-2476.