메뉴 건너뛰기
Eukaryotic Cell
Volumn 14, Issue 6, 2015, Pages 578-587
Overlapping functions between SWR1 deletion and H3K56 acetylation in Candida albicans
Author keywords

[No Author keywords available]
Indexed keywords

CANDIDA ALBICANS;
EID: 84930395099     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00002-15     Document Type: Article
Times cited : (15)
References (69)
  • 1
    • 37249012276 scopus 로고    scopus 로고
    • Nucleosome destabilization in the epigenetic regulation of gene expression
    • Henikoff S. 2008. Nucleosome destabilization in the epigenetic regulation of gene expression. Nat Rev Genet 9:15-26. http://dx.doi.org/10.1038 /nrg2206.
    • (2008) Nat Rev Genet , vol.9 , pp. 15-26
    • Henikoff, S.1
  • 2
    • 84875149194 scopus 로고    scopus 로고
    • Regulation of nucleosome dynamics by histone modifications
    • Zentner GE, Henikoff S. 2013. Regulation of nucleosome dynamics by histone modifications. Nat Struct Mol Biol 20:259-266. http://dx.doi.org /10.1038/nsmb.2470.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 259-266
    • Zentner, G.E.1    Henikoff, S.2
  • 3
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H, Hawke D, Kobayashi R, Verreault A. 2005. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436:294-298. http://dx.doi.org/10.1038/nature03714.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 4
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replicationcoupled nucleosome assembly
    • Li Q, Zhou H, Wurtele H, Davies B, Horazdovsky B, Verreault A, Zhang Z. 2008. Acetylation of histone H3 lysine 56 regulates replicationcoupled nucleosome assembly. Cell 134:244-255. http://dx.doi.org/10 .1016/j.cell.2008.06.018.
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 5
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen CC, Carson JJ, Feser J, Tamburini B, Zabaronick S, Linger J, Tyler JK. 2008. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 134:231-243. http://dx.doi.org/10.1016/j.cell.2008.06.035.
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 6
    • 48249148195 scopus 로고    scopus 로고
    • Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation
    • Williams SK, Truong D, Tyler JK. 2008. Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc Natl Acad Sci U S A 105:9000-9005. http://dx .doi.org/10.1073/pnas.0800057105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9000-9005
    • Williams, S.K.1    Truong, D.2    Tyler, J.K.3
  • 7
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F, Zhang K, Grunstein M. 2005. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121:375-385. http://dx.doi .org/10.1016/j.cell.2005.03.011.
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 8
    • 34547277498 scopus 로고    scopus 로고
    • Genomewide replication-independent histoneH3exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1
    • Rufiange A, Jacques PE, Bhat W, Robert F, Nourani A. 2007. Genomewide replication-independent histoneH3exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1. Mol Cell 27: 393-405. http://dx.doi.org/10.1016/j.molcel.2007.07.011.
    • (2007) Mol Cell , vol.27 , pp. 393-405
    • Rufiange, A.1    Jacques, P.E.2    Bhat, W.3    Robert, F.4    Nourani, A.5
  • 9
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. 1997. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389:251-260. http://dx.doi.org/10.1038/38444.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 10
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll R, Hudson A, Jackson SP. 2007. Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315:649-652. http://dx.doi.org/10.1126/science.1135862.
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 11
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han J, Zhou H, Horazdovsky B, Zhang K, Xu RM, Zhang Z. 2007. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315:653-655. http://dx.doi.org/10.1126/science.1133234.
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.M.5    Zhang, Z.6
  • 12
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation
    • Celic I, Masumoto H, Griffith WP, Meluh P, Cotter RJ, Boeke JD, Verreault A. 2006. The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr Biol 16:1280-1289. http://dx.doi.org/10.1016/j.cub.2006.06.023.
    • (2006) Curr Biol , vol.16 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6    Verreault, A.7
  • 13
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4
    • Maas NL, Miller KM, DeFazio LG, Toczyski DP. 2006. Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol Cell 23:109-119. http://dx.doi.org/10.1016/j.molcel.2006.06.006.
    • (2006) Mol Cell , vol.23 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    DeFazio, L.G.3    Toczyski, D.P.4
  • 14
    • 0023958267 scopus 로고
    • Opaque-white phenotype transition: A programmed morphological transition in Candida albicans
    • Rikkerink EH, Magee BB, Magee PT. 1988. Opaque-white phenotype transition: a programmed morphological transition in Candida albicans. J Bacteriol 170:895-899.
    • (1988) J Bacteriol , vol.170 , pp. 895-899
    • Rikkerink, E.H.1    Magee, B.B.2    Magee, P.T.3
  • 15
    • 0023142875 scopus 로고
    • "White-opaque transition": A second high-frequency switching system in Candida albicans
    • Slutsky B, Staebell M, Anderson J, Risen L, Pfaller M, Soll DR. 1987. "White-opaque transition": a second high-frequency switching system in Candida albicans. J Bacteriol 169:189-197.
    • (1987) J Bacteriol , vol.169 , pp. 189-197
    • Slutsky, B.1    Staebell, M.2    Anderson, J.3    Risen, L.4    Pfaller, M.5    Soll, D.R.6
  • 16
    • 0032722557 scopus 로고    scopus 로고
    • Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white phase of Candida albicans confers increased virulence in a mouse model of cutaneous infection
    • Kvaal C, Lachke SA, Srikantha T, Daniels K, McCoy J, Soll DR. 1999. Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white phase of Candida albicans confers increased virulence in a mouse model of cutaneous infection. Infect Immun 67:6652-6662.
    • (1999) Infect Immun , vol.67 , pp. 6652-6662
    • Kvaal, C.1    Lachke, S.A.2    Srikantha, T.3    Daniels, K.4    McCoy, J.5    Soll, D.R.6
  • 17
    • 0041823472 scopus 로고    scopus 로고
    • Skin facilitates Candida albicans mating
    • Lachke SA, Lockhart SR, Daniels KJ, Soll DR. 2003. Skin facilitates Candida albicans mating. Infect Immun 71:4970-4976. http://dx.doi.org /10.1128/IAI.71.9.4970-4976.2003.
    • (2003) Infect Immun , vol.71 , pp. 4970-4976
    • Lachke, S.A.1    Lockhart, S.R.2    Daniels, K.J.3    Soll, D.R.4
  • 18
    • 44849141076 scopus 로고    scopus 로고
    • Differential phagocytosis of white versus opaque Candida albicans by Drosophila and mouse phagocytes
    • Lohse MB, Johnson AD. 2008. Differential phagocytosis of white versus opaque Candida albicans by Drosophila and mouse phagocytes. PLoS One 3:e1473. http://dx.doi.org/10.1371/journal.pone.0001473.
    • (2008) PLoS One , vol.3
    • Lohse, M.B.1    Johnson, A.D.2
  • 20
    • 76549103447 scopus 로고    scopus 로고
    • Histone acetyltransferase Rtt109 is required for Candida albicans pathogenesis
    • Lopes da Rosa J, Boyartchuk VL, Zhu LJ, Kaufman PD. 2010. Histone acetyltransferase Rtt109 is required for Candida albicans pathogenesis. Proc Natl Acad Sci U S A 107:1594-1599. http://dx.doi.org/10.1073/pnas .0912427107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1594-1599
    • da Rosa Lopes, J.1    Boyartchuk, V.L.2    Zhu, L.J.3    Kaufman, P.D.4
  • 22
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA. 2002. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277:45099-45107. http://dx.doi.org/10.1074/jbc.M205670200.
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 23
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD+-dependent deacetylation reactions
    • Sauve AA, Celic I, Avalos J, Deng H, Boeke JD, Schramm VL. 2001. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40:15456-15463. http://dx.doi.org /10.1021/bi011858j.
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 24
    • 80051571474 scopus 로고    scopus 로고
    • Regulation of white and opaque cell-type formation in Candida albicans by Rtt109 and Hst3
    • Stevenson JS, Liu H. 2011. Regulation of white and opaque cell-type formation in Candida albicans by Rtt109 and Hst3. Mol Microbiol 81: 1078-1091. http://dx.doi.org/10.1111/j.1365-2958.2011.07754.x.
    • (2011) Mol Microbiol , vol.81 , pp. 1078-1091
    • Stevenson, J.S.1    Liu, H.2
  • 25
    • 84875516407 scopus 로고    scopus 로고
    • Nucleosome assembly factors CAF-1 and HIR modulate epigenetic switching frequencies in an H3K56 acetylationassociated manner in Candida albicans
    • Stevenson JS, Liu H. 2013. Nucleosome assembly factors CAF-1 and HIR modulate epigenetic switching frequencies in an H3K56 acetylationassociated manner in Candida albicans. Eukaryot Cell 12:591-603. http: //dx.doi.org/10.1128/EC.00334-12.
    • (2013) Eukaryot Cell , vol.12 , pp. 591-603
    • Stevenson, J.S.1    Liu, H.2
  • 26
    • 84876313606 scopus 로고    scopus 로고
    • A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme
    • Watanabe S, Radman-Livaja M, Rando OJ, Peterson CL. 2013. A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme. Science 340:195-199. http://dx.doi.org/10.1126/science.1229758.
    • (2013) Science , vol.340 , pp. 195-199
    • Watanabe, S.1    Radman-Livaja, M.2    Rando, O.J.3    Peterson, C.L.4
  • 28
    • 84870390011 scopus 로고    scopus 로고
    • Epigenetic regulation of condensin-mediated genome organization during the cell cycle and upon DNA damage through histone H3 lysine 56 acetylation
    • Tanaka A, Tanizawa H, Sriswasdi S, Iwasaki O, Chatterjee AG, Speicher DW, Levin HL, Noguchi E, Noma K. 2012. Epigenetic regulation of condensin-mediated genome organization during the cell cycle and upon DNA damage through histone H3 lysine 56 acetylation. Mol Cell 48:532-546. http://dx.doi.org/10.1016/j.molcel.2012.09.011.
    • (2012) Mol Cell , vol.48 , pp. 532-546
    • Tanaka, A.1    Tanizawa, H.2    Sriswasdi, S.3    Iwasaki, O.4    Chatterjee, A.G.5    Speicher, D.W.6    Levin, H.L.7    Noguchi, E.8    Noma, K.9
  • 29
    • 0034307468 scopus 로고    scopus 로고
    • Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
    • Jackson JD, Gorovsky MA. 2000. Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic Acids Res 28:3811-3816. http://dx.doi.org/10.1093/nar/28.19.3811.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3811-3816
    • Jackson, J.D.1    Gorovsky, M.A.2
  • 30
    • 0029954395 scopus 로고    scopus 로고
    • Essential and nonessential histone H2A variants in Tetrahymena thermophila
    • Liu X, Li B, Gorovsky MA. 1996. Essential and nonessential histone H2A variants in Tetrahymena thermophila. Mol Cell Biol 16:4305-4311.
    • (1996) Mol Cell Biol , vol.16 , pp. 4305-4311
    • Liu, X.1    Li, B.2    Gorovsky, M.A.3
  • 31
    • 0027058961 scopus 로고
    • A histone variant, H2AvD, is essential in Drosophila melanogaster
    • van Daal A, Elgin SC. 1992. A histone variant, H2AvD, is essential in Drosophila melanogaster. Mol Biol Cell 3:593-602. http://dx.doi.org/10 .1091/mbc.3.6.593.
    • (1992) Mol Biol Cell , vol.3 , pp. 593-602
    • van Daal, A.1    Elgin, S.C.2
  • 33
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini MD, Wu M, Madhani HD. 2003. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell 112:725-736. http://dx.doi.org/10.1016/S0092-8674(03) 00123-5.
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 34
    • 29144531244 scopus 로고    scopus 로고
    • Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning
    • Guillemette B, Bataille AR, Gevry N, Adam M, Blanchette M, Robert F, Gaudreau L. 2005. Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning. PLoS Biol 3:e384. http://dx.doi.org/10.1371/journal.pbio.0030384.
    • (2005) PLoS Biol , vol.3
    • Guillemette, B.1    Bataille, A.R.2    Gevry, N.3    Adam, M.4    Blanchette, M.5    Robert, F.6    Gaudreau, L.7
  • 35
    • 34047111213 scopus 로고    scopus 로고
    • Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome
    • Albert I, Mavrich TN, Tomsho LP, Qi J, Zanton SJ, Schuster SC, Pugh BF. 2007. Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome. Nature 446:572-576. http: //dx.doi.org/10.1038/nature05632.
    • (2007) Nature , vol.446 , pp. 572-576
    • Albert, I.1    Mavrich, T.N.2    Tomsho, L.P.3    Qi, J.4    Zanton, S.J.5    Schuster, S.C.6    Pugh, B.F.7
  • 36
    • 33947137710 scopus 로고    scopus 로고
    • Dynamics of replication-independent histone turnover in budding yeast
    • Dion MF, Kaplan T, Kim M, Buratowski S, Friedman N, Rando OJ. 2007. Dynamics of replication-independent histone turnover in budding yeast. Science 315:1405-1408. http://dx.doi.org/10.1126/science.1134053.
    • (2007) Science , vol.315 , pp. 1405-1408
    • Dion, M.F.1    Kaplan, T.2    Kim, M.3    Buratowski, S.4    Friedman, N.5    Rando, O.J.6
  • 37
    • 2642515598 scopus 로고    scopus 로고
    • A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome
    • Park YJ, Dyer PN, Tremethick DJ, Luger K. 2004. A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome. J Biol Chem 279:24274-24282. http://dx.doi.org/10.1074/jbc.M313152200.
    • (2004) J Biol Chem , vol.279 , pp. 24274-24282
    • Park, Y.J.1    Dyer, P.N.2    Tremethick, D.J.3    Luger, K.4
  • 38
    • 68149158205 scopus 로고    scopus 로고
    • Labile H3.3+H2A.Z nucleosomes mark 'nucleosomefree regions'
    • Henikoff S. 2009. Labile H3.3+H2A.Z nucleosomes mark 'nucleosomefree regions'. Nat Genet 41:865-866. http://dx.doi.org/10.1038/ng0809 -865.
    • (2009) Nat Genet , vol.41 , pp. 865-866
    • Henikoff, S.1
  • 39
  • 40
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • Kobor MS, Venkatasubrahmanyam S, Meneghini MD, Gin JW, Jennings JL, Link AJ, Madhani HD, Rine J. 2004. A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol 2:E131. http://dx.doi.org /10.1371/journal.pbio.0020131.
    • (2004) PLoS Biol , vol.2
    • Kobor, M.S.1    Venkatasubrahmanyam, S.2    Meneghini, M.D.3    Gin, J.W.4    Jennings, J.L.5    Link, A.J.6    Madhani, H.D.7    Rine, J.8
  • 41
    • 0348184963 scopus 로고    scopus 로고
    • ATPdriven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G, Shen X, Landry J, Wu WH, Sen S, Wu C. 2004. ATPdriven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303:343-348. http://dx.doi.org/10.1126 /science.1090701.
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 42
    • 77957889181 scopus 로고    scopus 로고
    • The SWR1 histone replacement complex causes genetic instability and genome- wide transcription misregulation in the absence of H2A.Z
    • Morillo-Huesca M, Clemente-Ruiz M, Andujar E, Prado F. 2010. The SWR1 histone replacement complex causes genetic instability and genome- wide transcription misregulation in the absence of H2A.Z. PLoS One 5:e12143. http://dx.doi.org/10.1371/journal.pone.0012143.
    • (2010) PLoS One , vol.5
    • Morillo-Huesca, M.1    Clemente-Ruiz, M.2    Andujar, E.3    Prado, F.4
  • 44
    • 6344279816 scopus 로고    scopus 로고
    • The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres
    • Zhang H, Richardson DO, Roberts DN, Utley R, Erdjument-Bromage H, Tempst P, Cote J, Cairns BR. 2004. The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres. Mol Cell Biol 24:9424-9436. http://dx.doi.org/10.1128/MCB.24.21.9424-9436.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 9424-9436
    • Zhang, H.1    Richardson, D.O.2    Roberts, D.N.3    Utley, R.4    Erdjument-Bromage, H.5    Tempst, P.6    Cote, J.7    Cairns, B.R.8
  • 45
    • 41149115039 scopus 로고    scopus 로고
    • Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histoneH2Avariants
    • Auger A, Galarneau L, Altaf M, Nourani A, Doyon Y, Utley RT, Cronier D, Allard S, Cote J. 2008. Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histoneH2Avariants. Mol Cell Biol 28:2257-2270. http://dx.doi.org/10.1128/MCB.01755-07.
    • (2008) Mol Cell Biol , vol.28 , pp. 2257-2270
    • Auger, A.1    Galarneau, L.2    Altaf, M.3    Nourani, A.4    Doyon, Y.5    Utley, R.T.6    Cronier, D.7    Allard, S.8    Cote, J.9
  • 46
    • 84884214357 scopus 로고    scopus 로고
    • Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement
    • Ranjan A, Mizuguchi G, FitzGerald PC, Wei D, Wang F, Huang Y, Luk E, Woodcock CL, Wu C. 2013. Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement. Cell 154:1232-1245. http://dx.doi.org/10.1016/j.cell.2013.08.005.
    • (2013) Cell , vol.154 , pp. 1232-1245
    • Ranjan, A.1    Mizuguchi, G.2    FitzGerald, P.C.3    Wei, D.4    Wang, F.5    Huang, Y.6    Luk, E.7    Woodcock, C.L.8    Wu, C.9
  • 47
    • 33748077784 scopus 로고    scopus 로고
    • Bistable expression of WOR1, a master regulator of white-opaque switching in Candida albicans
    • Huang G, Wang H, Chou S, Nie X, Chen J, Liu H. 2006. Bistable expression of WOR1, a master regulator of white-opaque switching in Candida albicans. Proc Natl Acad Sci U S A 103:12813-12818. http://dx .doi.org/10.1073/pnas.0605270103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 12813-12818
    • Huang, G.1    Wang, H.2    Chou, S.3    Nie, X.4    Chen, J.5    Liu, H.6
  • 49
    • 33748030763 scopus 로고    scopus 로고
    • Epigenetic properties of white-opaque switching in Candida albicans are based on a self-sustaining transcriptional feedback loop
    • Zordan RE, Galgoczy DJ, Johnson AD. 2006. Epigenetic properties of white-opaque switching in Candida albicans are based on a self-sustaining transcriptional feedback loop. Proc Natl Acad SciUSA103:12807-12812. http://dx.doi.org/10.1073/pnas.0605138103.
    • (2006) Proc Natl Acad SciUSA , vol.103 , pp. 12807-12812
    • Zordan, R.E.1    Galgoczy, D.J.2    Johnson, A.D.3
  • 50
    • 13844316993 scopus 로고    scopus 로고
    • Strains and strategies for large-scale gene deletion studies of the diploid human fungal pathogen Candida albicans
    • Noble SM, Johnson AD. 2005. Strains and strategies for large-scale gene deletion studies of the diploid human fungal pathogen Candida albicans. Eukaryot Cell 4:298-309. http://dx.doi.org/10.1128/EC.4.2.298-309.2005.
    • (2005) Eukaryot Cell , vol.4 , pp. 298-309
    • Noble, S.M.1    Johnson, A.D.2
  • 51
    • 57349156700 scopus 로고    scopus 로고
    • Efg1-mediated recruitment of NuA4 to promoters is required for hypha-specific Swi/Snf binding and activation in Candida albicans
    • Lu Y, Su C, Mao X, Raniga PP, Liu H, Chen J. 2008. Efg1-mediated recruitment of NuA4 to promoters is required for hypha-specific Swi/Snf binding and activation in Candida albicans. Mol Biol Cell 19:4260-4272. http://dx.doi.org/10.1091/mbc.E08-02-0173.
    • (2008) Mol Biol Cell , vol.19 , pp. 4260-4272
    • Lu, Y.1    Su, C.2    Mao, X.3    Raniga, P.P.4    Liu, H.5    Chen, J.6
  • 52
    • 84887860497 scopus 로고    scopus 로고
    • Synergistic regulation of hyphal elongation by hypoxia, CO(2), and nutrient conditions controls the virulence of Candida albicans
    • Lu Y, Su C, Solis NV, Filler SG, Liu H. 2013. Synergistic regulation of hyphal elongation by hypoxia, CO(2), and nutrient conditions controls the virulence of Candida albicans. Cell Host Microbe 14:499-509. http: //dx.doi.org/10.1016/j.chom.2013.10.008.
    • (2013) Cell Host Microbe , vol.14 , pp. 499-509
    • Lu, Y.1    Su, C.2    Solis, N.V.3    Filler, S.G.4    Liu, H.5
  • 53
    • 0032574776 scopus 로고    scopus 로고
    • Monosomy of a specific chromosome determines L-sorbose utilization: A novel regulatory mechanism in Candida albicans
    • Janbon G, Sherman F, Rustchenko E. 1998. Monosomy of a specific chromosome determines L-sorbose utilization: a novel regulatory mechanism in Candida albicans. Proc Natl Acad Sci U S A 95:5150-5155. http: //dx.doi.org/10.1073/pnas.95.9.5150.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5150-5155
    • Janbon, G.1    Sherman, F.2    Rustchenko, E.3
  • 54
    • 0018945880 scopus 로고
    • Strain variation and morphogenesis of yeast- and mycelial-phase Candida albicans in low-sulfate, synthetic medium
    • Manning M, Mitchell TG. 1980. Strain variation and morphogenesis of yeast- and mycelial-phase Candida albicans in low-sulfate, synthetic medium. J Bacteriol 142:714-719.
    • (1980) J Bacteriol , vol.142 , pp. 714-719
    • Manning, M.1    Mitchell, T.G.2
  • 55
    • 0029130739 scopus 로고
    • Chromatin structure snap-shots: Rapid nuclease digestion of chromatin in yeast
    • Kent NA, Mellor J. 1995. Chromatin structure snap-shots: rapid nuclease digestion of chromatin in yeast. Nucleic Acids Res 23:3786-3787. http: //dx.doi.org/10.1093/nar/23.18.3786.
    • (1995) Nucleic Acids Res , vol.23 , pp. 3786-3787
    • Kent, N.A.1    Mellor, J.2
  • 56
    • 77951902484 scopus 로고    scopus 로고
    • Nucleosome-depleted regions in cell-cycle-regulated promoters ensure reliable gene expression in every cell cycle
    • Bai L, Charvin G, Siggia ED, Cross FR. 2010. Nucleosome-depleted regions in cell-cycle-regulated promoters ensure reliable gene expression in every cell cycle. Dev Cell 18:544-555. http://dx.doi.org/10.1016/j .devcel.2010.02.007.
    • (2010) Dev Cell , vol.18 , pp. 544-555
    • Bai, L.1    Charvin, G.2    Siggia, E.D.3    Cross, F.R.4
  • 57
    • 79960921059 scopus 로고    scopus 로고
    • Hyphal development in Candida albicans requires two temporally linked changes in promoter chromatin for initiation and maintenance
    • Lu Y, Su C, Wang A, Liu H. 2011. Hyphal development in Candida albicans requires two temporally linked changes in promoter chromatin for initiation and maintenance. PLoS Biol 9:e1001105. http://dx.doi.org /10.1371/journal.pbio.1001105.
    • (2011) PLoS Biol , vol.9
    • Lu, Y.1    Su, C.2    Wang, A.3    Liu, H.4
  • 59
    • 60349128912 scopus 로고    scopus 로고
    • CO(2) regulates white-to-opaque switching in Candida albicans
    • Huang G, Srikantha T, Sahni N, Yi S, Soll DR. 2009. CO(2) regulates white-to-opaque switching in Candida albicans. Curr Biol 19:330-334. http://dx.doi.org/10.1016/j.cub.2009.01.018.
    • (2009) Curr Biol , vol.19 , pp. 330-334
    • Huang, G.1    Srikantha, T.2    Sahni, N.3    Yi, S.4    Soll, D.R.5
  • 60
    • 77950456763 scopus 로고    scopus 로고
    • N-Acetylglucosamine induces white to opaque switching, a mating prerequisite in Candida albicans
    • Huang G, Yi S, Sahni N, Daniels KJ, Srikantha T, Soll DR. 2010. N-Acetylglucosamine induces white to opaque switching, a mating prerequisite in Candida albicans. PLoS Pathog 6:e1000806. http://dx.doi.org /10.1371/journal.ppat.1000806.
    • (2010) PLoS Pathog , vol.6
    • Huang, G.1    Yi, S.2    Sahni, N.3    Daniels, K.J.4    Srikantha, T.5    Soll, D.R.6
  • 61
    • 84919353031 scopus 로고    scopus 로고
    • Transcribing through the nucleosome
    • Teves SS, Weber CM, Henikoff S. 2014. Transcribing through the nucleosome. Trends Biochem Sci 39:577-586. http://dx.doi.org/10.1016/j .tibs.2014.10.004.
    • (2014) Trends Biochem Sci , vol.39 , pp. 577-586
    • Teves, S.S.1    Weber, C.M.2    Henikoff, S.3
  • 62
    • 84898883789 scopus 로고    scopus 로고
    • Histone variants: Dynamic punctuation in transcription
    • Weber CM, Henikoff S. 2014. Histone variants: dynamic punctuation in transcription. Genes Dev 28:672-682. http://dx.doi.org/10.1101/gad .238873.114.
    • (2014) Genes Dev , vol.28 , pp. 672-682
    • Weber, C.M.1    Henikoff, S.2
  • 63
    • 33846293581 scopus 로고    scopus 로고
    • H2A.Z contributes to the unique 3D structure of the centromere
    • Greaves IK, Rangasamy D, Ridgway P, Tremethick DJ. 2007. H2A.Z contributes to the unique 3D structure of the centromere. Proc Natl Acad Sci U S A 104:525-530. http://dx.doi.org/10.1073/pnas.0607870104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 525-530
    • Greaves, I.K.1    Rangasamy, D.2    Ridgway, P.3    Tremethick, D.J.4
  • 64
    • 84870904979 scopus 로고    scopus 로고
    • Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair
    • Xu Y, Ayrapetov MK, Xu C, Gursoy-Yuzugullu O, Hu Y, Price BD. 2012. Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair. Mol Cell 48:723-733. http: //dx.doi.org/10.1016/j.molcel.2012.09.026.
    • (2012) Mol Cell , vol.48 , pp. 723-733
    • Xu, Y.1    Ayrapetov, M.K.2    Xu, C.3    Gursoy-Yuzugullu, O.4    Hu, Y.5    Price, B.D.6
  • 65
    • 59649124496 scopus 로고    scopus 로고
    • Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break
    • Kalocsay M, Hiller NJ, Jentsch S. 2009. Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. Mol Cell 33:335-343. http://dx.doi.org/10.1016/j.molcel.2009.01.016.
    • (2009) Mol Cell , vol.33 , pp. 335-343
    • Kalocsay, M.1    Hiller, N.J.2    Jentsch, S.3
  • 66
    • 84884701244 scopus 로고    scopus 로고
    • Structure of the transcriptional network controlling whiteopaque switching in Candida albicans
    • Hernday AD, Lohse MB, Fordyce PM, Nobile CJ, DeRisi JL, Johnson AD. 2013. Structure of the transcriptional network controlling whiteopaque switching in Candida albicans. Mol Microbiol 90:22-35. http://dx .doi.org/10.1111/mmi.12329.
    • (2013) Mol Microbiol , vol.90 , pp. 22-35
    • Hernday, A.D.1    Lohse, M.B.2    Fordyce, P.M.3    Nobile, C.J.4    DeRisi, J.L.5    Johnson, A.D.6
  • 67
    • 70350036600 scopus 로고    scopus 로고
    • Transcriptional loops meet chromatin: A dual-layer network controls white-opaque switching in Candida albicans
    • Hnisz D, Schwarzmuller T, Kuchler K. 2009. Transcriptional loops meet chromatin: a dual-layer network controls white-opaque switching in Candida albicans. Mol Microbiol 74:1-15. http://dx.doi.org/10.1111/j.1365 -2958.2009.06772.x.
    • (2009) Mol Microbiol , vol.74 , pp. 1-15
    • Hnisz, D.1    Schwarzmuller, T.2    Kuchler, K.3
  • 68
    • 0036885807 scopus 로고    scopus 로고
    • A conserved mitogen-activated protein kinase pathway is required for mating in Candida albicans
    • Chen J, Lane S, Liu H. 2002. A conserved mitogen-activated protein kinase pathway is required for mating in Candida albicans. Mol Microbiol 46:1335-1344. http://dx.doi.org/10.1046/j.1365-2958.2002.03249.x.
    • (2002) Mol Microbiol , vol.46 , pp. 1335-1344
    • Chen, J.1    Lane, S.2    Liu, H.3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.