메뉴 건너뛰기




Volumn 27, Issue 5, 2017, Pages 651-660

Structure-Function Studies Link Class II Viral Fusogens with the Ancestral Gamete Fusion Protein HAP2

Author keywords

conjugation; evolution of sex; GCS1; HAP2; membrane fusion; structure homology modeling; Tetrahymena; virus fusogen

Indexed keywords

MEMBRANE PROTEIN; PROTOZOAL PROTEIN;

EID: 85013645762     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2017.01.049     Document Type: Article
Times cited : (71)

References (43)
  • 2
    • 30344459431 scopus 로고    scopus 로고
    • GENERATIVE CELL SPECIFIC 1 is essential for angiosperm fertilization
    • 2 Mori, T., Kuroiwa, H., Higashiyama, T., Kuroiwa, T., GENERATIVE CELL SPECIFIC 1 is essential for angiosperm fertilization. Nat. Cell Biol. 8 (2006), 64–71.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 64-71
    • Mori, T.1    Kuroiwa, H.2    Higashiyama, T.3    Kuroiwa, T.4
  • 3
    • 77249172226 scopus 로고    scopus 로고
    • Is HAP2-GCS1 an ancestral gamete fusogen?
    • 3 Wong, J.L., Johnson, M.A., Is HAP2-GCS1 an ancestral gamete fusogen?. Trends Cell Biol. 20 (2010), 134–141.
    • (2010) Trends Cell Biol. , vol.20 , pp. 134-141
    • Wong, J.L.1    Johnson, M.A.2
  • 5
    • 33846094853 scopus 로고    scopus 로고
    • Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization
    • 5 von Besser, K., Frank, A.C., Johnson, M.A., Preuss, D., Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization. Development 133 (2006), 4761–4769.
    • (2006) Development , vol.133 , pp. 4761-4769
    • von Besser, K.1    Frank, A.C.2    Johnson, M.A.3    Preuss, D.4
  • 8
    • 79251477550 scopus 로고    scopus 로고
    • The functional domain of GCS1-based gamete fusion resides in the amino terminus in plant and parasite species
    • 8 Mori, T., Hirai, M., Kuroiwa, T., Miyagishima, S.Y., The functional domain of GCS1-based gamete fusion resides in the amino terminus in plant and parasite species. PLoS ONE, 5, 2010, e15957.
    • (2010) PLoS ONE , vol.5 , pp. e15957
    • Mori, T.1    Hirai, M.2    Kuroiwa, T.3    Miyagishima, S.Y.4
  • 9
    • 77950400019 scopus 로고    scopus 로고
    • HAP2(GCS1)-dependent gamete fusion requires a positively charged carboxy-terminal domain
    • 9 Wong, J.L., Leydon, A.R., Johnson, M.A., HAP2(GCS1)-dependent gamete fusion requires a positively charged carboxy-terminal domain. PLoS Genet., 6, 2010, e1000882.
    • (2010) PLoS Genet. , vol.6 , pp. e1000882
    • Wong, J.L.1    Leydon, A.R.2    Johnson, M.A.3
  • 10
    • 84923287323 scopus 로고    scopus 로고
    • The cytoplasmic domain of the gamete membrane fusion protein HAP2 targets the protein to the fusion site in Chlamydomonas and regulates the fusion reaction
    • 10 Liu, Y., Pei, J., Grishin, N., Snell, W.J., The cytoplasmic domain of the gamete membrane fusion protein HAP2 targets the protein to the fusion site in Chlamydomonas and regulates the fusion reaction. Development 142 (2015), 962–971.
    • (2015) Development , vol.142 , pp. 962-971
    • Liu, Y.1    Pei, J.2    Grishin, N.3    Snell, W.J.4
  • 12
    • 66749150463 scopus 로고    scopus 로고
    • The tetrahymena conjugation junction
    • F. Baluska D. Volkmann P.W. Barlow Springer
    • 12 Cole, E.S., The tetrahymena conjugation junction. Baluska, F., Volkmann, D., Barlow, P.W., (eds.) Cell-Cell Channels, 2006, Springer, 39–62.
    • (2006) Cell-Cell Channels , pp. 39-62
    • Cole, E.S.1
  • 13
    • 0032712574 scopus 로고    scopus 로고
    • Fluorescent dyes for lymphocyte migration and proliferation studies
    • 13 Parish, C.R., Fluorescent dyes for lymphocyte migration and proliferation studies. Immunol. Cell Biol. 77 (1999), 499–508.
    • (1999) Immunol. Cell Biol. , vol.77 , pp. 499-508
    • Parish, C.R.1
  • 14
    • 84922777605 scopus 로고    scopus 로고
    • SUMOylation is developmentally regulated and required for cell pairing during conjugation in Tetrahymena thermophila
    • 14 Nasir, A.M., Yang, Q., Chalker, D.L., Forney, J.D., SUMOylation is developmentally regulated and required for cell pairing during conjugation in Tetrahymena thermophila. Eukaryot. Cell 14 (2015), 170–181.
    • (2015) Eukaryot. Cell , vol.14 , pp. 170-181
    • Nasir, A.M.1    Yang, Q.2    Chalker, D.L.3    Forney, J.D.4
  • 15
    • 84930074657 scopus 로고    scopus 로고
    • The Phyre2 web portal for protein modeling, prediction and analysis
    • 15 Kelley, L.A., Mezulis, S., Yates, C.M., Wass, M.N., Sternberg, M.J., The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10 (2015), 845–858.
    • (2015) Nat. Protoc. , vol.10 , pp. 845-858
    • Kelley, L.A.1    Mezulis, S.2    Yates, C.M.3    Wass, M.N.4    Sternberg, M.J.5
  • 16
    • 84864448769 scopus 로고    scopus 로고
    • Template-based protein structure modeling using the RaptorX web server
    • 16 Källberg, M., Wang, H., Wang, S., Peng, J., Wang, Z., Lu, H., Xu, J., Template-based protein structure modeling using the RaptorX web server. Nat. Protoc. 7 (2012), 1511–1522.
    • (2012) Nat. Protoc. , vol.7 , pp. 1511-1522
    • Källberg, M.1    Wang, H.2    Wang, S.3    Peng, J.4    Wang, Z.5    Lu, H.6    Xu, J.7
  • 17
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • 17 Modis, Y., Ogata, S., Clements, D., Harrison, S.C., Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79 (2005), 1223–1231.
    • (2005) J. Virol. , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 18
    • 84873205968 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein C from Rift Valley fever virus
    • 18 Dessau, M., Modis, Y., Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl. Acad. Sci. USA 110 (2013), 1696–1701.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1696-1701
    • Dessau, M.1    Modis, Y.2
  • 19
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: more than one way to make a hairpin
    • 19 Kielian, M., Rey, F.A., Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 4 (2006), 67–76.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 20
    • 78449257072 scopus 로고    scopus 로고
    • Dengue virus ensures its fusion in late endosomes using compartment-specific lipids
    • 20 Zaitseva, E., Yang, S.T., Melikov, K., Pourmal, S., Chernomordik, L.V., Dengue virus ensures its fusion in late endosomes using compartment-specific lipids. PLoS Pathog., 6, 2010, e1001131.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001131
    • Zaitseva, E.1    Yang, S.T.2    Melikov, K.3    Pourmal, S.4    Chernomordik, L.V.5
  • 21
    • 84872973964 scopus 로고    scopus 로고
    • Functional and evolutionary insight from the crystal structure of rubella virus protein E1
    • 21 DuBois, R.M., Vaney, M.-C., Tortorici, M.A., Kurdi, R.A., Barba-Spaeth, G., Krey, T., Rey, F.A., Functional and evolutionary insight from the crystal structure of rubella virus protein E1. Nature 493 (2013), 552–556.
    • (2013) Nature , vol.493 , pp. 552-556
    • DuBois, R.M.1    Vaney, M.-C.2    Tortorici, M.A.3    Kurdi, R.A.4    Barba-Spaeth, G.5    Krey, T.6    Rey, F.A.7
  • 23
    • 84893278973 scopus 로고    scopus 로고
    • Relating structure to evolution in class II viral membrane fusion proteins
    • 23 Modis, Y., Relating structure to evolution in class II viral membrane fusion proteins. Curr. Opin. Virol. 5 (2014), 34–41.
    • (2014) Curr. Opin. Virol. , vol.5 , pp. 34-41
    • Modis, Y.1
  • 25
    • 0344981517 scopus 로고    scopus 로고
    • Hydration, structure, and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: an electron spin resonance study
    • 25 Ge, M., Freed, J.H., Hydration, structure, and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: an electron spin resonance study. Biophys. J. 85 (2003), 4023–4040.
    • (2003) Biophys. J. , vol.85 , pp. 4023-4040
    • Ge, M.1    Freed, J.H.2
  • 26
    • 84891846958 scopus 로고    scopus 로고
    • HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion
    • 26 Lai, A.L., Freed, J.H., HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion. Biophys. J. 106 (2014), 172–181.
    • (2014) Biophys. J. , vol.106 , pp. 172-181
    • Lai, A.L.1    Freed, J.H.2
  • 27
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
    • 27 Qiao, H., Armstrong, R.T., Melikyan, G.B., Cohen, F.S., White, J.M., A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol. Biol. Cell 10 (1999), 2759–2769.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 28
    • 69549116106 scopus 로고    scopus 로고
    • Interaction of the Dengue virus fusion peptide with membranes assessed by NMR: The essential role of the envelope protein Trp101 for membrane fusion
    • 28 Melo, M.N., Sousa, F.J.R., Carneiro, F.A., Castanho, M.A.R.B., Valente, A.P., Almeida, F.C.L., Da Poian, A.T., Mohana-Borges, R., Interaction of the Dengue virus fusion peptide with membranes assessed by NMR: The essential role of the envelope protein Trp101 for membrane fusion. J. Mol. Biol. 392 (2009), 736–746.
    • (2009) J. Mol. Biol. , vol.392 , pp. 736-746
    • Melo, M.N.1    Sousa, F.J.R.2    Carneiro, F.A.3    Castanho, M.A.R.B.4    Valente, A.P.5    Almeida, F.C.L.6    Da Poian, A.T.7    Mohana-Borges, R.8
  • 32
    • 0035941478 scopus 로고    scopus 로고
    • New BEL-like LTR-retrotransposons in Fugu rubripes, Caenorhabditis elegans, and Drosophila melanogaster
    • 32 Frame, I.G., Cutfield, J.F., Poulter, R.T., New BEL-like LTR-retrotransposons in Fugu rubripes, Caenorhabditis elegans, and Drosophila melanogaster. Gene 263 (2001), 219–230.
    • (2001) Gene , vol.263 , pp. 219-230
    • Frame, I.G.1    Cutfield, J.F.2    Poulter, R.T.3
  • 33
    • 62549121819 scopus 로고    scopus 로고
    • On the origin of cells and viruses: primordial virus world scenario
    • 33 Koonin, E.V., On the origin of cells and viruses: primordial virus world scenario. Ann. N Y Acad. Sci. 1178 (2009), 47–64.
    • (2009) Ann. N Y Acad. Sci. , vol.1178 , pp. 47-64
    • Koonin, E.V.1
  • 34
    • 84926049825 scopus 로고    scopus 로고
    • Evolution of double-stranded DNA viruses of eukaryotes: from bacteriophages to transposons to giant viruses
    • 34 Koonin, E.V., Krupovic, M., Yutin, N., Evolution of double-stranded DNA viruses of eukaryotes: from bacteriophages to transposons to giant viruses. Ann. N Y Acad. Sci. 1341 (2015), 10–24.
    • (2015) Ann. N Y Acad. Sci. , vol.1341 , pp. 10-24
    • Koonin, E.V.1    Krupovic, M.2    Yutin, N.3
  • 35
    • 85047681854 scopus 로고    scopus 로고
    • Origins of the machinery of recombination and sex
    • 35 Cavalier-Smith, T., Origins of the machinery of recombination and sex. Heredity (Edinb) 88 (2002), 125–141.
    • (2002) Heredity (Edinb) , vol.88 , pp. 125-141
    • Cavalier-Smith, T.1
  • 36
    • 33749147412 scopus 로고    scopus 로고
    • Sex and the eukaryotic cell cycle is consistent with a viral ancestry for the eukaryotic nucleus
    • 36 Bell, P.J.L., Sex and the eukaryotic cell cycle is consistent with a viral ancestry for the eukaryotic nucleus. J. Theor. Biol. 243 (2006), 54–63.
    • (2006) J. Theor. Biol. , vol.243 , pp. 54-63
    • Bell, P.J.L.1
  • 37
    • 78649718268 scopus 로고    scopus 로고
    • Endogenous viral elements in animal genomes
    • 37 Katzourakis, A., Gifford, R.J., Endogenous viral elements in animal genomes. PLoS Genet., 6, 2010, e1001191.
    • (2010) PLoS Genet. , vol.6 , pp. e1001191
    • Katzourakis, A.1    Gifford, R.J.2
  • 38
    • 0034053834 scopus 로고    scopus 로고
    • An envelope glycoprotein of the human endogenous retrovirus HERV-W is expressed in the human placenta and fuses cells expressing the type D mammalian retrovirus receptor
    • 38 Blond, J.-L., Lavillette, D., Cheynet, V., Bouton, O., Oriol, G., Chapel-Fernandes, S., Mandrand, B., Mallet, F., Cosset, F.-L., An envelope glycoprotein of the human endogenous retrovirus HERV-W is expressed in the human placenta and fuses cells expressing the type D mammalian retrovirus receptor. J. Virol. 74 (2000), 3321–3329.
    • (2000) J. Virol. , vol.74 , pp. 3321-3329
    • Blond, J.-L.1    Lavillette, D.2    Cheynet, V.3    Bouton, O.4    Oriol, G.5    Chapel-Fernandes, S.6    Mandrand, B.7    Mallet, F.8    Cosset, F.-L.9
  • 40
    • 84937468655 scopus 로고    scopus 로고
    • Sex is a ubiquitous, ancient, and inherent attribute of eukaryotic life
    • 40 Speijer, D., Lukeš, J., Eliáš, M., Sex is a ubiquitous, ancient, and inherent attribute of eukaryotic life. Proc. Natl. Acad. Sci. USA 112 (2015), 8827–8834.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 8827-8834
    • Speijer, D.1    Lukeš, J.2    Eliáš, M.3
  • 41
    • 45849105215 scopus 로고    scopus 로고
    • Gamete fusion: key protein identified
    • 41 Goodman, C.D., McFadden, G.I., Gamete fusion: key protein identified. Curr. Biol. 18 (2008), R571–R573.
    • (2008) Curr. Biol. , vol.18 , pp. R571-R573
    • Goodman, C.D.1    McFadden, G.I.2
  • 42
    • 0020447816 scopus 로고
    • Selfish DNA: a sexually-transmitted nuclear parasite
    • 42 Hickey, D.A., Selfish DNA: a sexually-transmitted nuclear parasite. Genetics 101 (1982), 519–531.
    • (1982) Genetics , vol.101 , pp. 519-531
    • Hickey, D.A.1
  • 43
    • 0000743310 scopus 로고
    • The role of gene transfer in the evolution of eukaryotic sex
    • R.E. Michod B.R. Levin Sinauer Associates
    • 43 Hickey, D.A., Rose, M.R., The role of gene transfer in the evolution of eukaryotic sex. Michod, R.E., Levin, B.R., (eds.) The Evolution of Sex: An Examination of Current Ideas, 1988, Sinauer Associates, 161–175.
    • (1988) The Evolution of Sex: An Examination of Current Ideas , pp. 161-175
    • Hickey, D.A.1    Rose, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.