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Volumn 24, Issue 13, 2014, Pages 1485-1491

Drosophila lipid droplets buffer the h2av supply to protect early embryonic development

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; DROSOPHILA PROTEIN; FAT DROPLET; HISTONE; JABBA PROTEIN, DROSOPHILA;

EID: 84904055571     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2014.05.022     Document Type: Article
Times cited : (63)

References (43)
  • 1
    • 0024044232 scopus 로고
    • Effects of histone H4 depletion on the cell cycle and transcription of Saccharomyces cerevisiae
    • U.J. Kim, M. Han, P. Kayne, and M. Grunstein Effects of histone H4 depletion on the cell cycle and transcription of Saccharomyces cerevisiae EMBO J. 7 1988 2211 2219
    • (1988) EMBO J. , vol.7 , pp. 2211-2219
    • Kim, U.J.1    Han, M.2    Kayne, P.3    Grunstein, M.4
  • 2
    • 0023666061 scopus 로고
    • Histone H2B repression causes cell-cycle-specific arrest in yeast: Effects on chromosomal segregation, replication, and transcription
    • M. Han, M. Chang, U.J. Kim, and M. Grunstein Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication, and transcription Cell 48 1987 589 597
    • (1987) Cell , vol.48 , pp. 589-597
    • Han, M.1    Chang, M.2    Kim, U.J.3    Grunstein, M.4
  • 3
    • 0344688414 scopus 로고    scopus 로고
    • A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S cerevisiae
    • A. Gunjan, and A. Verreault A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae Cell 115 2003 537 549
    • (2003) Cell , vol.115 , pp. 537-549
    • Gunjan, A.1    Verreault, A.2
  • 4
    • 52049119574 scopus 로고    scopus 로고
    • Altered dosage and mislocalization of histone H3 and Cse4p lead to chromosome loss in Saccharomyces cerevisiae
    • W.C. Au, M.J. Crisp, S.Z. DeLuca, O.J. Rando, and M.A. Basrai Altered dosage and mislocalization of histone H3 and Cse4p lead to chromosome loss in Saccharomyces cerevisiae Genetics 179 2008 263 275
    • (2008) Genetics , vol.179 , pp. 263-275
    • Au, W.C.1    Crisp, M.J.2    Deluca, S.Z.3    Rando, O.J.4    Basrai, M.A.5
  • 5
    • 0022482135 scopus 로고
    • Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission
    • D. Meeks-Wagner, and L.H. Hartwell Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission Cell 44 1986 43 52
    • (1986) Cell , vol.44 , pp. 43-52
    • Meeks-Wagner, D.1    Hartwell, L.H.2
  • 7
    • 0036200147 scopus 로고    scopus 로고
    • Conserved organization of centromeric chromatin in flies and humans
    • M.D. Blower, B.A. Sullivan, and G.H. Karpen Conserved organization of centromeric chromatin in flies and humans Dev. Cell 2 2002 319 330
    • (2002) Dev. Cell , vol.2 , pp. 319-330
    • Blower, M.D.1    Sullivan, B.A.2    Karpen, G.H.3
  • 8
    • 70449769682 scopus 로고    scopus 로고
    • Lipid droplets finally get a little R-E-S-P-E-C-T
    • R.V. Farese Jr.; and T.C. Walther Lipid droplets finally get a little R-E-S-P-E-C-T Cell 139 2009 855 860
    • (2009) Cell , vol.139 , pp. 855-860
    • Farese, Jr.R.V.1    Walther, T.C.2
  • 9
    • 33748598240 scopus 로고    scopus 로고
    • The lipid-droplet proteome reveals that droplets are a protein-storage depot
    • S. Cermelli, Y. Guo, S.P. Gross, and M.A. Welte The lipid-droplet proteome reveals that droplets are a protein-storage depot Curr. Biol. 16 2006 1783 1795
    • (2006) Curr. Biol. , vol.16 , pp. 1783-1795
    • Cermelli, S.1    Guo, Y.2    Gross, S.P.3    Welte, M.A.4
  • 10
    • 0036124889 scopus 로고    scopus 로고
    • Developmental control of histone mRNA and dSLBP synthesis during Drosophila embryogenesis and the role of dSLBP in histone mRNA 3′ end processing in vivo
    • D.J. Lanzotti, H. Kaygun, X. Yang, R.J. Duronio, and W.F. Marzluff Developmental control of histone mRNA and dSLBP synthesis during Drosophila embryogenesis and the role of dSLBP in histone mRNA 3′ end processing in vivo Mol. Cell. Biol. 22 2002 2267 2282
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2267-2282
    • Lanzotti, D.J.1    Kaygun, H.2    Yang, X.3    Duronio, R.J.4    Marzluff, W.F.5
  • 11
    • 84869489094 scopus 로고    scopus 로고
    • Lipid droplets control the maternal histone supply of Drosophila embryos
    • Z. Li, K. Thiel, P.J. Thul, M. Beller, R.P. Kühnlein, and M.A. Welte Lipid droplets control the maternal histone supply of Drosophila embryos Curr. Biol. 22 2012 2104 2113
    • (2012) Curr. Biol. , vol.22 , pp. 2104-2113
    • Li, Z.1    Thiel, K.2    Thul, P.J.3    Beller, M.4    Kühnlein, R.P.5    Welte, M.A.6
  • 12
    • 84869484668 scopus 로고    scopus 로고
    • Histones: Sequestered by Jabba in fatty storehouse
    • W.F. Marzluff, and D.C. Tatomer Histones: sequestered by Jabba in fatty storehouse Curr. Biol. 22 2012 R951 R953
    • (2012) Curr. Biol. , vol.22
    • Marzluff, W.F.1    Tatomer, D.C.2
  • 13
    • 0003455528 scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • M. Ashburner Drosophila: A Laboratory Handbook 1989 Cold Spring Harbor Laboratory Press Cold Spring Harbor 181
    • (1989) Drosophila: A Laboratory Handbook , pp. 181
    • Ashburner, M.1
  • 14
    • 0025039420 scopus 로고
    • Daughterless-abo-like, a Drosophila maternal-effect mutation that exhibits abnormal centrosome separation during the late blastoderm divisions
    • W. Sullivan, J.S. Minden, and B.M. Alberts daughterless-abo-like, a Drosophila maternal-effect mutation that exhibits abnormal centrosome separation during the late blastoderm divisions Development 110 1990 311 323
    • (1990) Development , vol.110 , pp. 311-323
    • Sullivan, W.1    Minden, J.S.2    Alberts, B.M.3
  • 16
    • 0034725587 scopus 로고    scopus 로고
    • Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster
    • T.J. Leach, M. Mazzeo, H.L. Chotkowski, J.P. Madigan, M.G. Wotring, and R.L. Glaser Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster J. Biol. Chem. 275 2000 23267 23272
    • (2000) J. Biol. Chem. , vol.275 , pp. 23267-23272
    • Leach, T.J.1    Mazzeo, M.2    Chotkowski, H.L.3    Madigan, J.P.4    Wotring, M.G.5    Glaser, R.L.6
  • 17
    • 84880775985 scopus 로고    scopus 로고
    • The variant histone H2A.V of Drosophila - Three roles, two guises
    • S. Baldi, and P.B. Becker The variant histone H2A.V of Drosophila - three roles, two guises Chromosoma 122 2013 245 258
    • (2013) Chromosoma , vol.122 , pp. 245-258
    • Baldi, S.1    Becker, P.B.2
  • 18
    • 80055119973 scopus 로고    scopus 로고
    • In-vivo centrifugation of Drosophila embryos
    • S.L. Tran, and M.A. Welte In-vivo centrifugation of Drosophila embryos J. Vis. Exp. 40 2010 2005
    • (2010) J. Vis. Exp. , vol.40 , pp. 2005
    • Tran, S.L.1    Welte, M.A.2
  • 19
    • 79955012081 scopus 로고    scopus 로고
    • Drosophila histone H2A variant (H2Av) controls poly(ADP-ribose) polymerase 1 (PARP1) activation in chromatin
    • E. Kotova, N. Lodhi, M. Jarnik, A.D. Pinnola, Y. Ji, and A.V. Tulin Drosophila histone H2A variant (H2Av) controls poly(ADP-ribose) polymerase 1 (PARP1) activation in chromatin Proc. Natl. Acad. Sci. USA 108 2011 6205 6210
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 6205-6210
    • Kotova, E.1    Lodhi, N.2    Jarnik, M.3    Pinnola, A.D.4    Ji, Y.5    Tulin, A.V.6
  • 21
    • 0033012289 scopus 로고    scopus 로고
    • A His2AvDGFP fusion gene complements a lethal His2AvD mutant allele and provides an in vivo marker for Drosophila chromosome behavior
    • M. Clarkson, and R. Saint A His2AvDGFP fusion gene complements a lethal His2AvD mutant allele and provides an in vivo marker for Drosophila chromosome behavior DNA Cell Biol. 18 1999 457 462
    • (1999) DNA Cell Biol. , vol.18 , pp. 457-462
    • Clarkson, M.1    Saint, R.2
  • 22
    • 11844295965 scopus 로고    scopus 로고
    • The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin
    • J. Swaminathan, E.M. Baxter, and V.G. Corces The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin Genes Dev. 19 2005 65 76
    • (2005) Genes Dev. , vol.19 , pp. 65-76
    • Swaminathan, J.1    Baxter, E.M.2    Corces, V.G.3
  • 23
    • 54149091257 scopus 로고    scopus 로고
    • Metabolism and regulation of canonical histone mRNAs: Life without a poly(A) tail
    • W.F. Marzluff, E.J. Wagner, and R.J. Duronio Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail Nat. Rev. Genet. 9 2008 843 854
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 843-854
    • Marzluff, W.F.1    Wagner, E.J.2    Duronio, R.J.3
  • 24
    • 36249011467 scopus 로고    scopus 로고
    • Transcription of histone gene cluster by differential core-promoter factors
    • Y. Isogai, S. Keles, M. Prestel, A. Hochheimer, and R. Tjian Transcription of histone gene cluster by differential core-promoter factors Genes Dev. 21 2007 2936 2949
    • (2007) Genes Dev. , vol.21 , pp. 2936-2949
    • Isogai, Y.1    Keles, S.2    Prestel, M.3    Hochheimer, A.4    Tjian, R.5
  • 26
    • 36248931620 scopus 로고    scopus 로고
    • A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone pre-mRNA processing
    • E.J. Wagner, B.D. Burch, A.C. Godfrey, H.R. Salzler, R.J. Duronio, and W.F. Marzluff A genome-wide RNA interference screen reveals that variant histones are necessary for replication-dependent histone pre-mRNA processing Mol. Cell 28 2007 692 699
    • (2007) Mol. Cell , vol.28 , pp. 692-699
    • Wagner, E.J.1    Burch, B.D.2    Godfrey, A.C.3    Salzler, H.R.4    Duronio, R.J.5    Marzluff, W.F.6
  • 28
    • 34548514866 scopus 로고    scopus 로고
    • Proteins under new management: Lipid droplets deliver
    • M.A. Welte Proteins under new management: lipid droplets deliver Trends Cell Biol. 17 2007 363 369
    • (2007) Trends Cell Biol. , vol.17 , pp. 363-369
    • Welte, M.A.1
  • 29
    • 19344366158 scopus 로고    scopus 로고
    • Metazoan replication-dependent histone mRNAs: A distinct set of RNA polymerase II transcripts
    • W.F. Marzluff Metazoan replication-dependent histone mRNAs: a distinct set of RNA polymerase II transcripts Curr. Opin. Cell Biol. 17 2005 274 280
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 274-280
    • Marzluff, W.F.1
  • 32
    • 68249094946 scopus 로고    scopus 로고
    • Histone levels are regulated by phosphorylation and ubiquitylation- dependent proteolysis
    • R.K. Singh, M.H. Kabbaj, J. Paik, and A. Gunjan Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis Nat. Cell Biol. 11 2009 925 933
    • (2009) Nat. Cell Biol. , vol.11 , pp. 925-933
    • Singh, R.K.1    Kabbaj, M.H.2    Paik, J.3    Gunjan, A.4
  • 33
    • 0020531221 scopus 로고
    • Studies of nuclear and cytoplasmic behaviour during the five mitotic cycles that precede gastrulation in Drosophila embryogenesis
    • V.E. Foe, and B.M. Alberts Studies of nuclear and cytoplasmic behaviour during the five mitotic cycles that precede gastrulation in Drosophila embryogenesis J. Cell Sci. 61 1983 31 70
    • (1983) J. Cell Sci. , vol.61 , pp. 31-70
    • Foe, V.E.1    Alberts, B.M.2
  • 35
    • 78649884849 scopus 로고    scopus 로고
    • H2A.Z nucleosomes enriched over active genes are homotypic
    • C.M. Weber, J.G. Henikoff, and S. Henikoff H2A.Z nucleosomes enriched over active genes are homotypic Nat. Struct. Mol. Biol. 17 2010 1500 1507
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1500-1507
    • Weber, C.M.1    Henikoff, J.G.2    Henikoff, S.3
  • 36
    • 34547201576 scopus 로고    scopus 로고
    • A genome-wide RNA interference screen identifies putative chromatin regulators essential for E2F repression
    • J. Lu, M.L. Ruhf, N. Perrimon, and P. Leder A genome-wide RNA interference screen identifies putative chromatin regulators essential for E2F repression Proc. Natl. Acad. Sci. USA 104 2007 9381 9386
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9381-9386
    • Lu, J.1    Ruhf, M.L.2    Perrimon, N.3    Leder, P.4
  • 37
    • 0022539155 scopus 로고
    • Parameters controlling transcriptional activation during early Drosophila development
    • B.A. Edgar, and G. Schubiger Parameters controlling transcriptional activation during early Drosophila development Cell 44 1986 871 877
    • (1986) Cell , vol.44 , pp. 871-877
    • Edgar, B.A.1    Schubiger, G.2
  • 38
    • 84884719203 scopus 로고    scopus 로고
    • The embryonic linker histone H1 variant of Drosophila, dBigH1, regulates zygotic genome activation
    • S. Pérez-Montero, A. Carbonell, T. Morán, A. Vaquero, and F. Azorín The embryonic linker histone H1 variant of Drosophila, dBigH1, regulates zygotic genome activation Dev. Cell 26 2013 578 590
    • (2013) Dev. Cell , vol.26 , pp. 578-590
    • Pérez-Montero, S.1    Carbonell, A.2    Morán, T.3    Vaquero, A.4    Azorín, F.5
  • 39
    • 12344321682 scopus 로고    scopus 로고
    • Human Asf1 regulates the flow of S phase histones during replicational stress
    • A. Groth, D. Ray-Gallet, J.P. Quivy, J. Lukas, J. Bartek, and G. Almouzni Human Asf1 regulates the flow of S phase histones during replicational stress Mol. Cell 17 2005 301 311
    • (2005) Mol. Cell , vol.17 , pp. 301-311
    • Groth, A.1    Ray-Gallet, D.2    Quivy, J.P.3    Lukas, J.4    Bartek, J.5    Almouzni, G.6
  • 40
    • 0023663912 scopus 로고
    • Two complexes that contain histones are required for nucleosome assembly in vitro: Role of nucleoplasmin and N1 in Xenopus egg extracts
    • S.M. Dilworth, S.J. Black, and R.A. Laskey Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts Cell 51 1987 1009 1018
    • (1987) Cell , vol.51 , pp. 1009-1018
    • Dilworth, S.M.1    Black, S.J.2    Laskey, R.A.3
  • 41
    • 0034761101 scopus 로고    scopus 로고
    • The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly
    • S. Dutta, I.V. Akey, C. Dingwall, K.L. Hartman, T. Laue, R.T. Nolte, J.F. Head, and C.W. Akey The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly Mol. Cell 8 2001 841 853
    • (2001) Mol. Cell , vol.8 , pp. 841-853
    • Dutta, S.1    Akey, I.V.2    Dingwall, C.3    Hartman, K.L.4    Laue, T.5    Nolte, R.T.6    Head, J.F.7    Akey, C.W.8
  • 42
    • 0027144416 scopus 로고
    • A new method for manipulating transgenes: Engineering heat tolerance in a complex, multicellular organism
    • M.A. Welte, J.M. Tetrault, R.P. Dellavalle, and S.L. Lindquist A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism Curr. Biol. 3 1993 842 853
    • (1993) Curr. Biol. , vol.3 , pp. 842-853
    • Welte, M.A.1    Tetrault, J.M.2    Dellavalle, R.P.3    Lindquist, S.L.4
  • 43
    • 33746018766 scopus 로고
    • Adaptive mechanisms that accelerate embryonic development in Drosophila
    • J.E. Mittenthal, A.B. Baskin, Addison-Wesley Urbana
    • T.L. Karr, and J.E. Mittenthal Adaptive mechanisms that accelerate embryonic development in Drosophila J.E. Mittenthal, A.B. Baskin, Principles of Organization in Organisms 1992 Addison-Wesley Urbana 95 108
    • (1992) Principles of Organization in Organisms , pp. 95-108
    • Karr, T.L.1    Mittenthal, J.E.2


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