C-Terminal Moiety of Tudor Contains Its In Vivo Activity in Drosophila

被引:1
|
作者
Anne, Joel [1 ]
机构
[1] Deutsch Krebsforschungszentrum, Dept Dev Genet, D-6900 Heidelberg, Germany
来源
PLOS ONE | 2010年 / 5卷 / 12期
关键词
POLE PLASM; GERM PLASM; METHYLTRANSFERASE CAPSULEEN; ARGININE RESIDUES; SM PROTEINS; MELANOGASTER; DOMAIN; LOCALIZATION; GENE; METHYLATION;
D O I
10.1371/journal.pone.0014378
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Background: In early Drosophila embryos, the germ plasm is localized to the posterior pole region and is partitioned into the germline progenitors, known as pole cells. Germ plasm, or pole plasm, contains the polar granules which form during oogenesis and are required for germline development. Components of these granules are also present in the perinuclear region of the nurse cells, the nuage. One such component is Tudor (Tud) which is a large protein containing multiple Tudor domains. It was previously reported that specific Tudor domains are required for germ cell formation and Tud localization. Methodology/Principal Findings: In order to better understand the function of Tud the distribution and functional activity of fragments of Tud were analyzed. These fragments were fused to GFP and the fusion proteins were synthesized during oogenesis. Non-overlapping fragments of Tud were found to be able to localize to both the nuage and pole plasm. By introducing these fragments into a tud mutant background and testing their ability to rescue the tud phenotype, I determined that the C-terminal moiety contains the functional activity of Tud. Dividing this fragment into two parts reduces its localization in pole plasm and abolishes its activity. Conclusions/Significance: I conclude that 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. The present results challenge published data and may help refining the functional features of Tud.
引用
收藏
页码:1 / 6
页数:6
相关论文
共 50 条
  • [41] ANALOGS OF THE C-TERMINAL FRAGMENTS OF NEUROKININS WITH MODIFICATIONS AT THEIR C-TERMINAL METHIONYL RESIDUE - STRUCTURE-ACTIVITY STUDIES
    ANTONIOU, M
    POULOS, C
    INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH, 1994, 43 (04): : 344 - 350
  • [42] C-TERMINAL FRAGMENT OF HUMAN GLUTATHIONE-REDUCTASE CONTAINS THE POSTULATED CATALYTIC HISTIDINE
    UNTUCHTGRAU, R
    SCHULZ, GE
    SCHIRMER, RH
    FEBS LETTERS, 1979, 105 (02) : 244 - 248
  • [43] The C-terminal end of R-Ras contains a focal adhesion targeting signal
    Furuhjelm, J
    Peränen, J
    JOURNAL OF CELL SCIENCE, 2003, 116 (18) : 3729 - 3738
  • [44] Diacylglycerol acyltransferase-2 contains a c-terminal sequence that interacts with lipid droplets
    McFie, Pamela J.
    Banman, Shanna L.
    Stone, Scot J.
    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2018, 1863 (09): : 1068 - 1081
  • [45] Cloning and expression of C-terminal of Clostridium perfringens type A enterotoxin and its biological activity
    Fard, Atieyeh Taherian
    Hasan, Fariha
    Bandehpour, Mojgan
    Mosaffa, Nariman
    Abbas, Fatemeh Mashhadi
    Hameed, Abdul
    Shah, Aamer Ali
    Kazemi, Bahram
    AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH, 2010, 4 (14): : 1469 - 1474
  • [46] C-terminal part of α-synuclein mediates its activity in promoting proliferation of dopaminergic cells
    Yin, Juanjuan
    Han, Junyan
    Zhang, Chen
    Ma, Qiu-Lan
    Li, Xin
    Cheng, Furong
    Liu, Guangwei
    Li, Yaohua
    Ueda, Kenji
    Chan, Piu
    Yu, Shun
    JOURNAL OF NEURAL TRANSMISSION, 2011, 118 (08) : 1155 - 1164
  • [47] Regulation of Insulin-Regulated Membrane Aminopeptidase Activity by Its C-Terminal Domain
    Ascher, David B.
    Cromer, Brett A.
    Morton, Craig J.
    Volitakis, Irene
    Cherny, Robert A.
    Albiston, Anthony L.
    Chai, Siew Yeen
    Parker, Michael W.
    BIOCHEMISTRY, 2011, 50 (13) : 2611 - 2622
  • [48] Electrostatic interactions at the C-terminal domain of nucleoplasmin modulate its chromatin decondensation activity
    Hierro, A
    Arizmendi, JM
    Bañuelos, S
    Prado, A
    Muga, A
    BIOCHEMISTRY, 2002, 41 (20) : 6408 - 6413
  • [49] Human interferon gamma: significance of the C-terminal flexible domain for its biological activity
    Nacheva, G
    Todorova, K
    Boyanova, M
    Berzal-Herranz, A
    Karshikoff, A
    Ivanov, I
    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2003, 413 (01) : 91 - 98
  • [50] C-terminal part of α-synuclein mediates its activity in promoting proliferation of dopaminergic cells
    Juanjuan Yin
    Junyan Han
    Chen Zhang
    Qiu-Lan Ma
    Xin Li
    Furong Cheng
    Guangwei Liu
    Yaohua Li
    Kenji Uéda
    Piu Chan
    Shun Yu
    Journal of Neural Transmission , 2011, 118 : 1155 - 1164