메뉴 건너뛰기




Volumn 24, Issue 8, 2010, Pages 2641-2650

Zebrafish dead end possesses ATPase activity that is required for primordial germ cell development

Author keywords

miRNA; Nanos1; Rescue; TDRD7; Vasa

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DEAD END PROTEIN; MAGNESIUM; MESSENGER RNA; MUTANT PROTEIN; NANOS1 PROTEIN; PROTEIN; TDRD7 PROTEIN; UNCLASSIFIED DRUG;

EID: 77955786268     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-148403     Document Type: Article
Times cited : (42)

References (51)
  • 1
    • 0033593291 scopus 로고    scopus 로고
    • Germ cells
    • Wylie, C. (1999) Germ cells. Cell 96, 165-174
    • (1999) Cell , vol.96 , pp. 165-174
    • Wylie, C.1
  • 2
    • 34247489172 scopus 로고    scopus 로고
    • Germ versus soma decisions: Lessons from flies and worms
    • Strome, S., and Lehmann, R. (2007) Germ versus soma decisions: lessons from flies and worms. Science 316, 392-393
    • (2007) Science , vol.316 , pp. 392-393
    • Strome, S.1    Lehmann, R.2
  • 3
    • 0034657873 scopus 로고    scopus 로고
    • Zebrafish vasa RNA but not its protein is a component of the germ plasm and segregates asymmetrically before germline specification
    • Knaut, H., Pelegri, F., Bohmann, Kerstin., Schwarz, H., and Nusslei-Volhard, C. (2000) Zebrafish vasa RNA but not its protein is a component of the germ plasm and segregates asymmetrically before germline specification. J. Cell Biol. 149, 875-888
    • (2000) J. Cell Biol. , vol.149 , pp. 875-888
    • Knaut, H.1    Pelegri, F.2    Bohmann, K.3    Schwarz, H.4    Nusslei-Volhard, C.5
  • 4
    • 0347519176 scopus 로고    scopus 로고
    • Mechanism of germ cell specification across the metazoans: Epigenesist and preformation
    • Extavour, C., and Akam, M. (2003) Mechanism of germ cell specification across the metazoans: epigenesist and preformation. Development 130, 5869-5884
    • (2003) Development , vol.130 , pp. 5869-5884
    • Extavour, C.1    Akam, M.2
  • 5
    • 0042926721 scopus 로고    scopus 로고
    • Dead end, a novel vertebrate germ plasm component, is required for zebrafish primordial germ cell migration and survival
    • Weidinger, G., Stebler, J., Slanchev, K., Dumstrei, K., Wise, C., Lovell-Badge, R., Thisse, C., Thisse, B, and Raz, E. (2003) Dead end, a novel vertebrate germ plasm component, is required for zebrafish primordial germ cell migration and survival. Curr. Biol. 13, 1429-1434
    • (2003) Curr. Biol. , vol.13 , pp. 1429-1434
    • Weidinger, G.1    Stebler, J.2    Slanchev, K.3    Dumstrei, K.4    Wise, C.5    Lovell-Badge, R.6    Thisse, C.7    Thisse, B.8    Raz, E.9
  • 6
    • 0023772979 scopus 로고
    • The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A
    • Lasko, P. F., and Ashburner, M. (1988) The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A. Nature 335, 611-617
    • (1988) Nature , vol.335 , pp. 611-617
    • Lasko, P.F.1    Ashburner, M.2
  • 7
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila vasa
    • Sengoku, T., Nureki, O., Nakamura, A., Kobayashi, S., and Yokoyama, S. (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila vasa. Cell 125, 287-300
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 8
    • 0030885902 scopus 로고    scopus 로고
    • Involvement of the protein of Xenopusvasa homologue (Xenopus vasa-like gene 1, XVLG1) in the differentiation of primordial germ cells
    • Ikenishi, K., and Tanaka, T. S. (1997) Involvement of the protein of Xenopusvasa homologue (Xenopus vasa-like gene 1, XVLG1) in the differentiation of primordial germ cells. Dev. Growth. Differ. 39, 625-633
    • (1997) Dev. Growth. Differ. , vol.39 , pp. 625-633
    • Ikenishi, K.1    Tanaka, T.S.2
  • 10
    • 0033931850 scopus 로고    scopus 로고
    • Combinatorial RNA interference indicates GLH-4 can compensate for GLH-1; these two P granule components are critical for fertility in C-elegans
    • Kuznicki, K. A., Smith, P. A., Leung-Chiu, W. M. A., Estevez, A. O., Scott, H. C., and Bennett, K. L. (2000) Combinatorial RNA interference indicates GLH-4 can compensate for GLH-1; these two P granule components are critical for fertility in C-elegans. Development 127, 2907-2916
    • (2000) Development , vol.127 , pp. 2907-2916
    • Kuznicki, K.A.1    Smith, P.A.2    Leung-Chiu, W.M.A.3    Estevez, A.O.4    Scott, H.C.5    Bennett, K.L.6
  • 12
    • 0030928578 scopus 로고    scopus 로고
    • Zebrafish vasa homologue RNA is localized to the cleavage planes of 2- and 4-cell stage embryos and is expressed in the primordial germ cells
    • Yoon, C., Kawakami, K., and Hopkins, N. (1997) Zebrafish vasa homologue RNA is localized to the cleavage planes of 2- and 4-cell stage embryos and is expressed in the primordial germ cells. Development 124, 3157-3166
    • (1997) Development , vol.124 , pp. 3157-3166
    • Yoon, C.1    Kawakami, K.2    Hopkins, N.3
  • 13
    • 0034903046 scopus 로고    scopus 로고
    • A zebrafish vasa morphant abolishes vasa protein but does not affect the establishment of the germline
    • Braat, A. K., Water, S., Korving, J., and Zivkovic, D. (2001) A zebrafish vasa morphant abolishes vasa protein but does not affect the establishment of the germline. Genesis 30, 183-185
    • (2001) Genesis , vol.30 , pp. 183-185
    • Braat, A.K.1    Water, S.2    Korving, J.3    Zivkovic, D.4
  • 14
    • 1642387326 scopus 로고    scopus 로고
    • Nanos maintains germline stem cell self-renewal by preventing differentiation
    • Wang, Z., and Lin, H. (2004) Nanos maintains germline stem cell self-renewal by preventing differentiation. Science 303, 2016-2019
    • (2004) Science , vol.303 , pp. 2016-2019
    • Wang, Z.1    Lin, H.2
  • 15
    • 0035500022 scopus 로고    scopus 로고
    • A zebrafish nanos-related gene is essential for the development of primordial germ cells
    • Koprunner, M., Thisse, C., Thisse, B., and Raz, E. (2001) A zebrafish nanos-related gene is essential for the development of primordial germ cells. Genes Dev. 15, 2877-2885
    • (2001) Genes Dev. , vol.15 , pp. 2877-2885
    • Koprunner, M.1    Thisse, C.2    Thisse, B.3    Raz, E.4
  • 16
    • 34248208252 scopus 로고    scopus 로고
    • Nanos1 is required to maintain oocyte production in adult zebrafish
    • Draper, B. W., McCallum, C. M., and Moens, C. B. (2007) nanos1 is required to maintain oocyte production in adult zebrafish. Dev. Biol. 305, 589-598
    • (2007) Dev. Biol. , vol.305 , pp. 589-598
    • Draper, B.W.1    McCallum, C.M.2    Moens, C.B.3
  • 21
    • 48449101265 scopus 로고    scopus 로고
    • Mouse apolipoprotein B editing complex 3 (APOBEC3) is expressed in germ cells and interacts with dead-end (DND1)
    • Bhattacharya, C., Aggarwal, S., Kumar, M., Ali, A., and Matin, A. (2008) Mouse apolipoprotein B editing complex 3 (APOBEC3) is expressed in germ cells and interacts with dead-end (DND1). PLoS ONE 5, e2315
    • (2008) PLoS ONE , vol.5
    • Bhattacharya, C.1    Aggarwal, S.2    Kumar, M.3    Ali, A.4    Matin, A.5
  • 22
    • 36348973030 scopus 로고    scopus 로고
    • Derepression of microRNA-mediated protein translation inhibition by apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G) and its family members
    • Huang, J., Liang, Z., Yang, B., Tian, H., Ma, J., and Zhang, H. (2007) Derepression of microRNA-mediated protein translation inhibition by apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G) and its family members. J. Biol. Chem. 282, 33632-33640
    • (2007) J. Biol. Chem. , vol.282 , pp. 33632-33640
    • Huang, J.1    Liang, Z.2    Yang, B.3    Tian, H.4    Ma, J.5    Zhang, H.6
  • 23
    • 33847193509 scopus 로고    scopus 로고
    • Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules
    • Gallois-Montbrun, S., Kramer, B., Swanson, C. M., Byers, H., Lynham, S., Ward, M., and Malim, M. H. (2007) Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules. J. Virol. 81, 2165-2178
    • (2007) J. Virol. , vol.81 , pp. 2165-2178
    • Gallois-Montbrun, S.1    Kramer, B.2    Swanson, C.M.3    Byers, H.4    Lynham, S.5    Ward, M.6    Malim, M.H.7
  • 25
    • 37348999219 scopus 로고    scopus 로고
    • A dead end for microRNA
    • Ketting, R. (2007) A dead end for microRNA. Cell 131, 1226-1227
    • (2007) Cell , vol.131 , pp. 1226-1227
    • Ketting, R.1
  • 26
    • 60049098346 scopus 로고    scopus 로고
    • Control of dead end localization and activity. Implications for the function of the protein in antagonizing miRNA function
    • Slanchev, K., Stebler, J., Goudarzi, M., Cojocaru, V., Weidinger, G., and Raz, E. (2008) Control of dead end localization and activity. Implications for the function of the protein in antagonizing miRNA function. Mech. Dev. 126, 270-277
    • (2008) Mech. Dev. , vol.126 , pp. 270-277
    • Slanchev, K.1    Stebler, J.2    Goudarzi, M.3    Cojocaru, V.4    Weidinger, G.5    Raz, E.6
  • 27
    • 0842311482 scopus 로고    scopus 로고
    • Expression of a vas::EGFP transgene in primordial germ cells of the zebrafish
    • Krovel, A. V., and Olsen, L. C. (2002) Expression of a vas::EGFP transgene in primordial germ cells of the zebrafish. Mech. Dev. 116, 141-150
    • (2002) Mech. Dev. , vol.116 , pp. 141-150
    • Krovel, A.V.1    Olsen, L.C.2
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0020681165 scopus 로고
    • Inorganic phosphate assay with malachite green: An improvement and evaluation
    • Carter, S., and Karl, D. (1982) Inorganic phosphate assay with malachite green: an improvement and evaluation. J. Biochem. Biophys. Methods 7, 7-13
    • (1982) J. Biochem. Biophys. Methods , vol.7 , pp. 7-13
    • Carter, S.1    Karl, D.2
  • 30
    • 41949126822 scopus 로고    scopus 로고
    • Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, A 3′-5′ helicase partner of the nuclear exosome
    • Bernstein, J., Patterson, D., Wilson, J., and Toth, E. (2008) Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, A 3′-5′ helicase partner of the nuclear exosome. J. Biol. Chem. 283, 4930-4942
    • (2008) J. Biol. Chem. , vol.283 , pp. 4930-4942
    • Bernstein, J.1    Patterson, D.2    Wilson, J.3    Toth, E.4
  • 33
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak, K. J., and Schmittgen, T. D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25, 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 34
    • 0019320639 scopus 로고
    • Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas
    • LeBel, D., Poirier, G. G., Phaneuf, S., St. Jean, P., Laliberte, J. F., and Beaudoin, A. R. (1980) Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas. J. Biol. Chem. 255, 1227-1233
    • (1980) J. Biol. Chem. , vol.255 , pp. 1227-1233
    • LeBel, D.1    Poirier, G.G.2    Phaneuf, S.3    St Jean, P.4    Laliberte, J.F.5    Beaudoin, A.R.6
  • 35
    • 49649098390 scopus 로고    scopus 로고
    • Adenosine receptors control a new pathway of Fas-associated death domain protein expression regulation by secretion
    • Tourneur. L., Mistou, S., Schmitt, A., and Chiocchia, G. (2008) Adenosine receptors control a new pathway of Fas-associated death domain protein expression regulation by secretion. J. Biol. Chem. 283, 17929-17938
    • (2008) J. Biol. Chem. , vol.283 , pp. 17929-17938
    • Tourneur, L.1    Mistou, S.2    Schmitt, A.3    Chiocchia, G.4
  • 37
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 38
    • 0035477839 scopus 로고    scopus 로고
    • Structure and function of the N-terminal 40-kDa fragment of human PMS2: A monomeric GHL ATPase
    • Guarne, A., Junop, M. S., and Yang, W. (2001) Structure and function of the N-terminal 40-kDa fragment of human PMS2: a monomeric GHL ATPase. EMBO J. 20, 5521-5531
    • (2001) EMBO J. , vol.20 , pp. 5521-5531
    • Guarne, A.1    Junop, M.S.2    Yang, W.3
  • 39
    • 0036718795 scopus 로고    scopus 로고
    • ATPase as drug targets: Learning from their structure
    • Chene, P. (2002) ATPase as drug targets: learning from their structure. Nat. Rev. Drug Discov. 9, 665-673
    • (2002) Nat. Rev. Drug Discov. , vol.9 , pp. 665-673
    • Chene, P.1
  • 40
    • 0346497938 scopus 로고
    • ATP-binding site of adenylate kinase: Mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotidebinding proteins
    • Fry, D. C., Kuby, S. A., and Mildvan, A. S. (1986) ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotidebinding proteins. Proc. Natl. Acad. Sci. U. S. A. 83, 907-911
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 907-911
    • Fry, D.C.1    Kuby, S.A.2    Mildvan, A.S.3
  • 41
    • 0024603237 scopus 로고
    • A specific 31-nucleotide domain of U1 RNA directly interacts with the 70K small nuclear ribonucleoprotein component
    • Query, C. C., Bentley. R. C., and Keene, J. D. (1989) A specific 31-nucleotide domain of U1 RNA directly interacts with the 70K small nuclear ribonucleoprotein component. Cell 57, 89-101
    • (1989) Cell , vol.57 , pp. 89-101
    • Query, C.C.1    Bentley, R.C.2    Keene, J.D.3
  • 42
    • 0024655246 scopus 로고
    • RNA binding proteins as developmental regulators
    • Bandziulis, R. J., Swanson, M. S., and Dreyfuss, G. (1989) RNA binding proteins as developmental regulators. Genes Dev. 3, 431-437
    • (1989) Genes Dev. , vol.3 , pp. 431-437
    • Bandziulis, R.J.1    Swanson, M.S.2    Dreyfuss, G.3
  • 43
    • 34547211817 scopus 로고    scopus 로고
    • The long unwinding road of RNA helicases
    • Bleichert, F., and Baserga, S. (2007) The long unwinding road of RNA helicases. Mol. Cell 27, 339-352
    • (2007) Mol. Cell , vol.27 , pp. 339-352
    • Bleichert, F.1    Baserga, S.2
  • 44
    • 0037188887 scopus 로고    scopus 로고
    • RNA chaperones exist and DEAD box proteins get a life
    • Lorsch, J. (2002) RNA chaperones exist and DEAD box proteins get a life. Cell 109, 797-800
    • (2002) Cell , vol.109 , pp. 797-800
    • Lorsch, J.1
  • 45
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: A family affair - Active and passive players in RNP-remodeling
    • Linder, P. (2006) Dead-box proteins: a family affair - active and passive players in RNP-remodeling. Nucleic Acids Res. 34, 4168-4180
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4168-4180
    • Linder, P.1
  • 47
    • 34547931108 scopus 로고    scopus 로고
    • Biochemical characterization of the ATPase and helicase activity of UAP56, an essential pre-mRNA splicing and mRNA export factor
    • Sheng. J., Zhang. L., and Zhao. R. (2007) Biochemical characterization of the ATPase and helicase activity of UAP56, an essential pre-mRNA splicing and mRNA export factor. J. Biochem. Chem. 282, 22544-22550
    • (2007) J. Biochem. Chem. , vol.282 , pp. 22544-22550
    • Sheng, J.1    Zhang, L.2    Zhao, R.3
  • 48
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H and eIF4F
    • Rogers, G. W., Richter, N. J., Lima, W. F., and Merrick, W. C. (2001) Modulation of the helicase activity of eIF4A by eIF4B, eIF4H and eIF4F. J. Biol. Chem. 276, 30914-30922
    • (2001) J. Biol. Chem. , vol.276 , pp. 30914-30922
    • Rogers, G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 49
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich, C. S., Erzberger, J. P., Flick, J. S., Berger, J. M., Thorner, I., and Weis, W. (2006) Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat. Cell Biol. 8, 668-676
    • (2006) Nat. Cell Biol. , vol.8 , pp. 668-676
    • Weirich, C.S.1    Erzberger, J.P.2    Flick, J.S.3    Berger, J.M.4    Thorner, I.5    Weis, W.6
  • 50
    • 33745406566 scopus 로고    scopus 로고
    • The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis
    • Granneman, S., Lin, C. Y., Champion, E. A., Nandineni, M. R., Zorca, C., and Baserga, S. J. (2006) The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis. Nucleic Acids Res. 34, 3189-3199
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3189-3199
    • Granneman, S.1    Lin, C.Y.2    Champion, E.A.3    Nandineni, M.R.4    Zorca, C.5    Baserga, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.