The role of Tudor domains in germline development and polar granule architecture

被引:101
作者
Arkov, Alexey L.
Wang, Ju-Yu S.
Ramos, Andres
Lehmann, Ruth
机构
[1] York Univ, Sch Med, Skirball Inst, Dev Genet Program,HHMI, New York, NY 10016 USA
[2] Natl Inst Med Res, Mol Struct Div, London NW7 1AA, England
来源
DEVELOPMENT | 2006年 / 133卷 / 20期
基金
英国医学研究理事会;
关键词
Drosophila; germline development; nuage; polar granule; Tudor domain; methylosome; PRMT5;
D O I
10.1242/dev.02572
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Tudor domains are found in many organisms and have been implicated in protein-protein interactions in which methylated protein substrates bind to these domains. Here, we present evidence for the involvement of specific Tudor domains in germline development. Drosophila Tudor, the founder of the Tudor domain family, contains 11 Tudor domains and is a component of polar granules and nuage, electron-dense organelles characteristic of the germline in many organisms, including mammals. In this study, we investigated whether the 11 Tudor domains fulfil specific functions for polar granule assembly, germ cell formation and abdomen formation. We find that even a small number of non-overlapping Tudor domains or a substantial reduction in overall Tudor protein is sufficient for abdomen development. In stark contrast, we find a requirement for specific Tudor domains in germ cell formation, Tudor localization and polar granule architecture. Combining genetic analysis with structural modeling of specific Tudor domains, we propose that these domains serve as 'docking platforms' for polar granule assembly.
引用
收藏
页码:4053 / 4062
页数:10
相关论文
共 52 条
  • [1] Tudor protein is essential for the localization of mitochondrial RNAs in polar granules of Drosophila embryos
    Amikura, R
    Hanyu, K
    Kashikawa, M
    Kobayashi, S
    [J]. MECHANISMS OF DEVELOPMENT, 2001, 107 (1-2) : 97 - 104
  • [2] Modularity and homology: Modelling of the titin type I modules and their interfaces
    Amodeo, P
    Fraternali, F
    Lesk, AM
    Pastore, A
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (02) : 283 - 296
  • [3] Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells
    Ancelin, Katia
    Lange, Ulrike C.
    Hajkova, Petra
    Schneider, Robert
    Bannister, Andrew J.
    Kouzarides, Tony
    Surani, M. Azim
    [J]. NATURE CELL BIOLOGY, 2006, 8 (06) : 623 - 630
  • [4] Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuleen
    Anne, J
    Mechler, BM
    [J]. DEVELOPMENT, 2005, 132 (09): : 2167 - 2177
  • [5] BARDSLEY A, 1993, DEVELOPMENT, V119, P207
  • [6] TUDOR, A GENE REQUIRED FOR ASSEMBLY OF THE GERM PLASM IN DROSOPHILA-MELANOGASTER
    BOSWELL, RE
    MAHOWALD, AP
    [J]. CELL, 1985, 43 (01) : 97 - 104
  • [7] Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    Brahms, H
    Meheus, L
    De Brabandere, V
    Fischer, U
    Lührmann, R
    [J]. RNA, 2001, 7 (11) : 1531 - 1542
  • [8] Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly:: implications for spinal muscular atrophy
    Buhler, D
    Raker, V
    Lührmann, R
    Fischer, U
    [J]. HUMAN MOLECULAR GENETICS, 1999, 8 (13) : 2351 - 2357
  • [9] Drosophila valois encodes a divergent WD protein that is required for Vasa localization and Oskar protein accumulation
    Cavey, M
    Hijal, S
    Zhang, XL
    Suter, B
    [J]. DEVELOPMENT, 2005, 132 (03): : 459 - 468
  • [10] The tudor tandem of 53BP1:: A new structural motif involved in DNA and RG-rich peptide binding
    Charier, G
    Couprie, J
    Alpha-Bazin, B
    Meyer, V
    Quéméneur, E
    Guérois, R
    Callebaut, I
    Gilquin, B
    Zinn-Justin, S
    [J]. STRUCTURE, 2004, 12 (09) : 1551 - 1562