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Volumn 4, Issue 6, 2013, Pages

The histone code of Toxoplasma gondii comprises conserved and unique posttranslational modifications

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2A; HISTONE H2B; HISTONE H4; PROTEOME; PROTOZOAL PROTEIN;

EID: 84891615691     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00922-13     Document Type: Article
Times cited : (74)

References (61)
  • 1
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: From genomic organization to genomic regulation
    • Khorasanizadeh S. 2004. The nucleosome: from genomic organization to genomic regulation. Cell 116:259-272.
    • (2004) Cell , vol.116 , pp. 259-272
    • Khorasanizadeh, S.1
  • 3
    • 78650438980 scopus 로고    scopus 로고
    • Epigenetics gets sweeter: O-GlcNAc joins the histone code
    • Hanover JA. 2010. Epigenetics gets sweeter: O-GlcNAc joins the "histone code." Chem. Biol. 17:1272-1274.
    • (2010) Chem. Biol , vol.17 , pp. 1272-1274
    • Hanover, J.A.1
  • 5
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. 2000. The language of covalent histone modifications. Nature 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 6
    • 0031958697 scopus 로고    scopus 로고
    • Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts
    • Dubey JP, Lindsay DS, Speer CA. 1998. Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts. Clin. Microbiol. Rev. 11:267-299.
    • (1998) Clin. Microbiol. Rev , vol.11 , pp. 267-299
    • Dubey, J.P.1    Lindsay, D.S.2    Speer, C.A.3
  • 13
    • 68949196209 scopus 로고    scopus 로고
    • Toxoplasma H2A variants reveal novel insights into nucleo some composition and functions for this histone family
    • Dalmasso MC, Onyango DO, Naguleswaran A, Sullivan WJ, Jr, Angel SO. 2009. Toxoplasma H2A variants reveal novel insights into nucleo some composition and functions for this histone family. J. Mol. Biol. 392:33-47.
    • (2009) J. Mol. Biol , vol.392 , pp. 33-47
    • Dalmasso, M.C.1    Onyango, D.O.2    Naguleswaran, A.3    Sullivan Jr., W.J.4    Angel, S.O.5
  • 14
    • 33644656442 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum histones: Organization, expression, and acetylation
    • Miao J, Fan Q, Cui L, Li J, Li J, Cui L. 2006. The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation. Gene 369:53-65.
    • (2006) Gene , vol.369 , pp. 53-65
    • Miao, J.1    Fan, Q.2    Cui, L.3    Li, J.4    Li, J.5    Cui, L.6
  • 15
    • 67650403817 scopus 로고    scopus 로고
    • Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum
    • Trelle MB, Salcedo-Amaya AM, Cohen AM, Stunnenberg HG, Jensen ON. 2009. Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum. J. Proteome Res. 8:3439-3450.
    • (2009) J. Proteome Res , vol.8 , pp. 3439-3450
    • Trelle, M.B.1    Salcedo-Amaya, A.M.2    Cohen, A.M.3    Stunnenberg, H.G.4    Jensen, O.N.5
  • 16
    • 77956802116 scopus 로고    scopus 로고
    • Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum
    • Cui L, Miao J. 2010. Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum. Eukaryot. Cell 9:1138-1149.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1138-1149
    • Cui, L.1    Miao, J.2
  • 18
    • 34347334624 scopus 로고    scopus 로고
    • Epigenomic modifications predict active promoters and gene structure in Toxoplasma gondii
    • Gissot M, Kelly KA, Ajioka JW, Greally JM, Kim K. 2007. Epigenomic modifications predict active promoters and gene structure in Toxoplasma gondii. PLOS Pathog. 3:e77. doi:10.1371/journal.ppat.0030077.
    • (2007) PLOS Pathog , vol.3
    • Gissot, M.1    Kelly, K.A.2    Ajioka, J.W.3    Greally, J.M.4    Kim, K.5
  • 19
    • 77953807039 scopus 로고    scopus 로고
    • Chromatin modifications: Implications in the regulation of gene expression in Toxo-plasma gondii
    • Bougdour A, Braun L, Cannella D, Hakimi MA. 2010. Chromatin modifications: implications in the regulation of gene expression in Toxo-plasma gondii. Cell. Microbiol. 12:413-423.
    • (2010) Cell. Microbiol , vol.12 , pp. 413-423
    • Bougdour, A.1    Braun, L.2    Cannella, D.3    Hakimi, M.A.4
  • 20
    • 84864577566 scopus 로고    scopus 로고
    • Separation of variant methylated histone tails by differential ion mobility
    • Shvartsburg AA, Zheng Y, Smith RD, Kelleher NL. 2012. Separation of variant methylated histone tails by differential ion mobility. Anal. Chem. 84:6317-6320.
    • (2012) Anal. Chem , vol.84 , pp. 6317-6320
    • Shvartsburg, A.A.1    Zheng, Y.2    Smith, R.D.3    Kelleher, N.L.4
  • 21
    • 77951833317 scopus 로고    scopus 로고
    • High resolution electron transfer dissociation studies of unfractionated intact histones from murine embryonic stem cells using on-line capillary LC separation: Determination of abundant histone isoforms and translational modifications
    • Eliuk SM, Maltby D, Panning B, Burlingame AL. 2010. High resolution electron transfer dissociation studies of unfractionated intact histones from murine embryonic stem cells using on-line capillary LC separation: determination of abundant histone isoforms and translational modifications. Mol. Cell. Proteomics 9:824-837.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 824-837
    • Eliuk, S.M.1    Maltby, D.2    Panning, B.3    Burlingame, A.L.4
  • 22
  • 24
    • 33846809241 scopus 로고    scopus 로고
    • Characterization of histones and their post-translational modifications by mass spectrometry
    • Garcia BA, Shabanowitz J, Hunt DF. 2007. Characterization of histones and their post-translational modifications by mass spectrometry. Curr. Opin. Chem. Biol. 11:66-73.
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 66-73
    • Garcia, B.A.1    Shabanowitz, J.2    Hunt, D.F.3
  • 26
    • 77951794785 scopus 로고    scopus 로고
    • Mass spectrometric analysis of histone variants and post-translational modifications
    • (Schol. Ed.)
    • Garcia BA. 2009. Mass spectrometric analysis of histone variants and post-translational modifications. Front. Biosci. (Schol. Ed.) 1:142-153.
    • (2009) Front. Biosci , vol.1 , pp. 142-153
    • Garcia, B.A.1
  • 27
    • 84860294536 scopus 로고    scopus 로고
    • Proteomics in chromatin biology and epigenetics: Elucidation of post-translational modifications of histone proteins by mass spectrometry
    • Sidoli S, Cheng L, Jensen ON. 2012. Proteomics in chromatin biology and epigenetics: Elucidation of post-translational modifications of histone proteins by mass spectrometry. J. Proteomics. 75:3419-3433.
    • (2012) J. Proteomics , vol.75 , pp. 3419-3433
    • Sidoli, S.1    Cheng, L.2    Jensen, O.N.3
  • 30
    • 84863837647 scopus 로고    scopus 로고
    • New marks on the block: Set5 methylates H4 lysines 5, 8 and 12
    • Green EM, Morrison AJ, Gozani O. 2012. New marks on the block: Set5 methylates H4 lysines 5, 8 and 12. Nucleus 3:335-339.
    • (2012) Nucleus , vol.3 , pp. 335-339
    • Green, E.M.1    Morrison, A.J.2    Gozani, O.3
  • 33
    • 84861689430 scopus 로고    scopus 로고
    • Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii
    • Jeffers V, Sullivan WJ, Jr. 2012. Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii. Eukaryot. Cell 11:735-742.
    • (2012) Eukaryot. Cell , vol.11 , pp. 735-742
    • Jeffers, V.1    Sullivan Jr., W.J.2
  • 34
    • 37349107849 scopus 로고    scopus 로고
    • Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin
    • Altaf M, Utley RT, Lacoste N, Tan S, Briggs SD, Côté J. 2007. Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin. Mol. Cell 28:1002-1014.
    • (2007) Mol. Cell , vol.28 , pp. 1002-1014
    • Altaf, M.1    Utley, R.T.2    Lacoste, N.3    Tan, S.4    Briggs, S.D.5    Côté, J.6
  • 35
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W, Kim J, Roeder RG. 2004. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117: 735-748.
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 36
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian MD, Grunstein M. 2007. Functions of site-specific histone acetylation and deacetylation. Annu. Rev. Biochem. 76:75-100.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 38
    • 84862496145 scopus 로고    scopus 로고
    • A role for CARM1-mediated histone H3 arginine methylation in protecting histone acetylation by releasing corepressors from chromatin
    • doi:10.1371/ journal.pone.0034692
    • Wu J, Cui N, Wang R, Li J, Wong J. 2012. A role for CARM1-mediated histone H3 arginine methylation in protecting histone acetylation by releasing corepressors from chromatin. PLoS One 7:e34692. doi:10.1371/ journal.pone.0034692.
    • (2012) PLoS One , vol.7
    • Wu, J.1    Cui, N.2    Wang, R.3    Li, J.4    Wong, J.5
  • 39
    • 0035816682 scopus 로고    scopus 로고
    • Set domain containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
    • Tachibana M, Sugimoto K, Fukushima T, Shinkai Y. 2001. Set domain containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J. Biol. Chem. 276:25309-25317.
    • (2001) J. Biol. Chem , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 41
    • 79957564427 scopus 로고    scopus 로고
    • Nucleosomes in the neighborhood: New roles for chromatin modifications in replication origin control
    • Dorn ES, Cook JG. 2011. Nucleosomes in the neighborhood: new roles for chromatin modifications in replication origin control. Epigenetics 6:552-559.
    • (2011) Epigenetics , vol.6 , pp. 552-559
    • Dorn, E.S.1    Cook, J.G.2
  • 42
    • 70349694389 scopus 로고    scopus 로고
    • 298:H3-H4 phosphorylation: Dual role in mitosis and interphase
    • Perez-Cadahia B, Drobic B, Davie JR. 2010. 298:H3-H4 phosphorylation: dual role in mitosis and interphase. Biochem. Cell Biol. 87:695-709.
    • (2010) Biochem. Cell Biol , vol.87 , pp. 695-709
    • Perez-Cadahia, B.1    Drobic, B.2    Davie, J.R.3
  • 44
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou EP, Pilch DR, Orr AH, Ivanova VS, Bonner WM. 1998. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273:5858-5868.
    • (1998) J. Biol. Chem , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 45
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants-ancient wrap artists of the epigenome
    • Talbert PB, Henikoff S. 2010. Histone variants-ancient wrap artists of the epigenome. Nat. Rev. Mol. Cell Biol. 11:264-275.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 46
    • 0033556404 scopus 로고    scopus 로고
    • Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates
    • Schiltz RL, Mizzen CA, Vassilev A, Cook RG, Allis CD, Nakatani Y. 1999. Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J. Biol. Chem. 274:1189-1192.
    • (1999) J. Biol. Chem , vol.274 , pp. 1189-1192
    • Schiltz, R.L.1    Mizzen, C.A.2    Vassilev, A.3    Cook, R.G.4    Allis, C.D.5    Nakatani, Y.6
  • 47
    • 33846113751 scopus 로고    scopus 로고
    • N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage
    • Jiang T, Zhou X, Taghizadeh K, Dong M, Dedon PC. 2007. N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage. Proc. Natl. Acad. Sci. U. S. A. 104:60-65.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 60-65
    • Jiang, T.1    Zhou, X.2    Taghizadeh, K.3    Dong, M.4    Dedon, P.C.5
  • 50
    • 51449116748 scopus 로고    scopus 로고
    • Identification of a novel post-translational modification in Plasmodium falciparum: Protein su moylation in different cellular compartments
    • Issar N, Roux E, Mattei D, Scherf A. 2008. Identification of a novel post-translational modification in Plasmodium falciparum: protein su moylation in different cellular compartments. Cell. Microbiol. 10: 1999-2011.
    • (2008) Cell. Microbiol , vol.10 , pp. 1999-2011
    • Issar, N.1    Roux, E.2    Mattei, D.3    Scherf, A.4
  • 52
    • 70349530494 scopus 로고    scopus 로고
    • Long-term evolution of histone families: Old notions and new insights into their mechanisms of diversification across eukaryotes
    • In Pontarotti P (ed), Springer Verlag, Berlin, Germany
    • Eirín-López JM, Dryhurst D, Méndez J, Jusio J. 2009. Long-term evolution of histone families: old notions and new insights into their mechanisms of diversification across eukaryotes, p 139-162. In Pontarotti P (ed), Evolutionary biology: concept, modeling, and application. Springer Verlag, Berlin, Germany.
    • (2009) Evolutionary Biology: Concept, Modeling, and Application , pp. 139-162
    • Eirín-López, J.M.1    Dryhurst, D.2    Méndez, J.3    Jusio, J.4
  • 53
    • 30944448223 scopus 로고    scopus 로고
    • Pair of unusual GCN5 histone acetyltransferases and ADA2 homologues in the protozoan parasite Toxoplasma gondii
    • Bhatti MM, Livingston M, Mullapudi N, Sullivan WJ, Jr. 2006. Pair of unusual GCN5 histone acetyltransferases and ADA2 homologues in the protozoan parasite Toxoplasma gondii. Eukaryot. Cell 5:62-76.
    • (2006) Eukaryot. Cell , vol.5 , pp. 62-76
    • Bhatti, M.M.1    Livingston, M.2    Mullapudi, N.3    Sullivan Jr., W.J.4
  • 57
    • 60649095351 scopus 로고    scopus 로고
    • Genome-wide analysis of heterochromatin associates clonally variant gene regulation with peri nuclear repressive centers in malaria parasites
    • Lopez-Rubio JJ, Mancio-Silva L, Scherf A. 2009. Genome-wide analysis of heterochromatin associates clonally variant gene regulation with peri nuclear repressive centers in malaria parasites. Cell Host Microbe 5:179-190.
    • (2009) Cell Host Microbe , vol.5 , pp. 179-190
    • Lopez-Rubio, J.J.1    Mancio-Silva, L.2    Scherf, A.3
  • 58
    • 0029895115 scopus 로고    scopus 로고
    • Insertional tagging,cloning, and expression of the Toxoplasma gondii hypoxanthine-xanthine-guanine phosphoribosyltransferase gene. Use as a selectable marker for stable transformation
    • Donald RG, Carter D, Ullman B, Roos DS. 1996. Insertional tagging,cloning, and expression of the Toxoplasma gondii hypoxanthine-xanthine-guanine phosphoribosyltransferase gene. Use as a selectable marker for stable transformation. J. Biol. Chem. 271:14010-14019.
    • (1996) J. Biol. Chem , vol.271 , pp. 14010-14019
    • Donald, R.G.1    Carter, D.2    Ullman, B.3    Roos, D.S.4
  • 59
    • 0025300686 scopus 로고
    • Trypanosoma cruzi histones. Further characterization and comparison with higher eukaryotes
    • Toro GC, Galanti N. 1990. Trypanosoma cruzi histones. Further characterization and comparison with higher eukaryotes. Biochem. Int. 21: 481-490.
    • (1990) Biochem. Int , vol.21 , pp. 481-490
    • Toro, G.C.1    Galanti, N.2
  • 61
    • 84862156464 scopus 로고    scopus 로고
    • HIstome-a relational knowledgebase of human histone proteins and histone modifying enzymes
    • Khare SP, Habib F, Sharma R, Gadewal N, Gupta S, Galande S. 2012.HIstome-a relational knowledgebase of human histone proteins and histone modifying enzymes. Nucleic Acids Res. 40:D337-D342.
    • (2012) Nucleic Acids Res , vol.40
    • Khare, S.P.1    Habib, F.2    Sharma, R.3    Gadewal, N.4    Gupta, S.5    Galande, S.6


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