| Drosophila germ granules are assembled from protein components through different modes of competing interactions with the multi-domain Tudor protein. | Drosophila germ granules are assembled from protein components through different modes of competing interactions with the multi-domain Tudor protein.
Wahiduzzaman, Tindell SJ, Alexander E, Hackney E, Kharel K, Schmidtke R, Arkov AL. | 04/12/2024 |
| Tudor protein's structural flexibility suggests a mechanism for the recruitment of glycolytic enzymes to the granules. | Glycolytic enzymes localize to ribonucleoprotein granules in Drosophila germ cells, bind Tudor and protect from transposable elements.
Gao M, Thomson TC, Creed TM, Tu S, Loganathan SN, Jackson CA, McCluskey P, Lin Y, Collier SE, Weng Z, Lasko P, Ohi MD, Arkov AL., Free PMC Article | 12/12/2015 |
| The overall spatial organization of the tandem domains of Tudor protein, is reported. | Structure and domain organization of Drosophila Tudor.
Ren R, Liu H, Wang W, Wang M, Yang N, Dong YH, Gong W, Lehmann R, Xu RM., Free PMC Article | 09/5/2015 |
| Drosophila TUDOR domain-containing proteins interact with Vreteno and the Tdrd12 family, essential primary piRNA pathway factors | A systematic analysis of Drosophila TUDOR domain-containing proteins identifies Vreteno and the Tdrd12 family as essential primary piRNA pathway factors.
Handler D, Olivieri D, Novatchkova M, Gruber FS, Meixner K, Mechtler K, Stark A, Sachidanandam R, Brennecke J., Free PMC Article | 12/24/2011 |
| Oskar recruits two downstream components of the polar granules, Vasa and Tudor, independently from each other: Vasa directly interacts with Oskar while Valois mediates the recruitment of Tudor by interacting with Oskar and Tudor | Targeting and anchoring Tudor in the pole plasm of the Drosophila oocyte.
Anne J., Free PMC Article | 07/9/2011 |
| the C-terminal moiety of Tud contains all the information necessary for its localization in the nuage and pole plasm and its pole cell-forming activity | C-terminal moiety of Tudor contains its in vivo activity in Drosophila.
Anne J., Free PMC Article | 07/9/2011 |
| Cocrystal structures of an extended Tudor domain (eTud) of Drosophila Tudor with methylated peptides of Aubergine, a Piwi family protein, reveal that sDMA is recognized by an asparagine-gated aromatic cage | Structural basis for methylarginine-dependent recognition of Aubergine by Tudor.
Liu H, Wang JY, Huang Y, Li Z, Gong W, Lehmann R, Xu RM., Free PMC Article | 09/20/2010 |
| maternal tudor mutation was found to increase life span in males but not in females | Identifying sexual differentiation genes that affect Drosophila life span.
Shen J, Ford D, Landis GN, Tower J., Free PMC Article | 03/8/2010 |
| Germ plasm assembly requires symmetrically dimethylated modification of Aub by dPRMT5, which, in turn, is required for binding to Tudor. | Arginine methylation of Aubergine mediates Tudor binding and germ plasm localization.
Kirino Y, Vourekas A, Sayed N, de Lima Alves F, Thomson T, Lasko P, Rappsilber J, Jongens TA, Mourelatos Z., Free PMC Article | 02/8/2010 |
| in germline cells, piRNAs are quality-controlled by dPRMT5 that modifies PIWI proteins, in tight association with Tud | Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines.
Nishida KM, Okada TN, Kawamura T, Mituyama T, Kawamura Y, Inagaki S, Huang H, Chen D, Kodama T, Siomi H, Siomi MC., Free PMC Article | 01/21/2010 |
| colocalized with mitochondrial RNAs(mtrRNAs) at the boundaries between mitochondria and polar granules when the transport of mtrRNAs takes place. | Tudor protein is essential for the localization of mitochondrial RNAs in polar granules of Drosophila embryos.
Amikura R, Hanyu K, Kashikawa M, Kobayashi S. | 10/29/2001 |