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Volumn 16, Issue 10, 2005, Pages 1641-1653

Peptide mass mapping of acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with histone deacetylase (HDACs) inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETYLATION; CELLS; ELECTROPHORESIS; ENZYME INHIBITION; GELS; LIQUID CHROMATOGRAPHY; MATRIX ALGEBRA; POLYPEPTIDES;

EID: 25144460509     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2005.06.001     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • K. Luger, A.W. Mader, R.K. Richmond, D.F. Sargent, T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 Å resolution Nature 389 1997 251 260
    • (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
  • 3
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B.D. Strahl, C.D. Allis The language of covalent histone modifications Nature 403 2000 41 45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 5
    • 0033592999 scopus 로고    scopus 로고
    • Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in tetrahymena
    • B.D. Strahl, R. Ohba, R.G. Cook, C.D. Allis Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in tetrahymena Proc. Natl. Acad. Sci. U.S.A. 96 1999 14967 14972
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14967-14972
    • Strahl, B.D.1    Ohba, R.2    Cook, R.G.3    Allis, C.D.4
  • 6
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T. Jenuwein, C.D. Allis Translating the histone code Science 293 2001 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 7
    • 6344286164 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling complexes: Enzymes tailored to deal with chromatin
    • S. Sif ATP-dependent nucleosome remodeling complexes Enzymes tailored to deal with chromatin J. Cell. Biochem. 91 2004 1087 1098
    • (2004) J. Cell. Biochem. , vol.91 , pp. 1087-1098
    • Sif, S.1
  • 8
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Y. Zhang, D. Reinberg Transcription regulation by histone methylation Interplay between different covalent modifications of the core histone tails Genes Dev. 15 2001 2343 2360
    • (2001) Genes Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 9
    • 0242474622 scopus 로고    scopus 로고
    • Acetylation and methylation in nuclear receptor gene activation
    • W. Xu, H. Cho, R.M. Evans Acetylation and methylation in nuclear receptor gene activation Methods Enzymol. 364 2003 205 223
    • (2003) Methods Enzymol. , vol.364 , pp. 205-223
    • Xu, W.1    Cho, H.2    Evans, R.M.3
  • 11
    • 0037188911 scopus 로고    scopus 로고
    • Histone methylation: Dynamic or static?
    • A.J. Bannister, R. Schneider, T. Kouzarides Histone methylation Dynamic or static? Cell 109 2002 801 806
    • (2002) Cell , vol.109 , pp. 801-806
    • Bannister, A.J.1    Schneider, R.2    Kouzarides, T.3
  • 15
    • 2942737394 scopus 로고    scopus 로고
    • Phosphorylation and acetylation of histone H3 at inducible genes: Two controversies revisited
    • L.C. Mahadevan, A.L. Clayton, C.A. Hazzalin, S. Thomson Phosphorylation and acetylation of histone H3 at inducible genes Two controversies revisited Novartis Foundation Symp. 259 2004 102/11 111/4; Discussion; 163-169
    • (2004) Novartis Foundation Symp. , vol.259
    • Mahadevan, L.C.1    Clayton, A.L.2    Hazzalin, C.A.3    Thomson, S.4
  • 16
    • 0031149505 scopus 로고    scopus 로고
    • Chromosomal mapping of core histone acetylation by immunoselection
    • C. Crane-Robinson, T.R. Hebbes, A.L. Clayton, A.W. Thorne Chromosomal mapping of core histone acetylation by immunoselection Methods 12 1997 48 56
    • (1997) Methods , vol.12 , pp. 48-56
    • Crane-Robinson, C.1    Hebbes, T.R.2    Clayton, A.L.3    Thorne, A.W.4
  • 17
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • N. Suka, Y. Suka, A.A. Carmen, J. Wu, M. Grunstein Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin Mol. Cell 8 2001 473 479
    • (2001) Mol. Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 18
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • J.B. Fenn, M. Mann, C.K. Meng, S.F. Wong, C.M. Whitehouse Electrospray ionization for mass spectrometry of large biomolecules Science 246 1989 64 71
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 21
    • 0013431655 scopus 로고
    • UV laser matrix desorption/ionization mass spectrometry of proteins in the 100,000 Da range
    • M. Karas, U. Bahr, F. Hillenkamp UV laser matrix desorption/ionization mass spectrometry of proteins in the 100,000 Da range Int. J. Mass Spectrom. Ion Processes 92 1989 231 242
    • (1989) Int. J. Mass Spectrom. Ion Processes , vol.92 , pp. 231-242
    • Karas, M.1    Bahr, U.2    Hillenkamp, F.3
  • 22
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100,000 by laser ionization time-of-flight mass spectrometry
    • K. Tanaka, H. Waki, Y. Ido, S. Akita, Y. Yoshida, T. Yoshida Protein and polymer analyses up to m/z 100,000 by laser ionization time-of-flight mass spectrometry Rapid Commun. Mass Spectrom. 2 1988 151 153
    • (1988) Rapid Commun. Mass Spectrom. , vol.2 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 23
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • F. Hillenkamp, M. Karas, R.C. Beavis, B.T. Chait Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers Anal. Chem. 63 1991 1193A 1203A
    • (1991) Anal. Chem. , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 25
    • 0037099664 scopus 로고    scopus 로고
    • Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization- postsource decay, and nanoelectrospray ionization tandem mass spectrometry
    • K. Zhang, H. Tang, L. Huang, J.W. Blankenship, P.R. Jones, F. Xiang, P.M. Yau, A.L. Burlingame Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization-postsource decay, and nanoelectrospray ionization tandem mass spectrometry Anal. Biochem. 306 2002 259 269
    • (2002) Anal. Biochem. , vol.306 , pp. 259-269
    • Zhang, K.1    Tang, H.2    Huang, L.3    Blankenship, J.W.4    Jones, P.R.5    Xiang, F.6    Yau, P.M.7    Burlingame, A.L.8
  • 26
    • 0037419508 scopus 로고    scopus 로고
    • Analysis of core histones by liquid chromatography-mass spectrometry and peptide mapping
    • K. Zhang, H. Tang Analysis of core histones by liquid chromatography-mass spectrometry and peptide mapping J. Chromatogr. B 783 2003 173 179
    • (2003) J. Chromatogr. B , vol.783 , pp. 173-179
    • Zhang, K.1    Tang, H.2
  • 27
    • 0347123341 scopus 로고    scopus 로고
    • Differential expression of histone posttranslational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry
    • L. Zhang, M.A. Freitas, J. Wickman, M.R. Parthun, M.I. Klisovic, G. Marcucci, J.C. Byrd Differential expression of histone posttranslational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry J. Am. Soc. Mass Spectrom. 15 2004 77 86
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 77-86
    • Zhang, L.1    Freitas, M.A.2    Wickman, J.3    Parthun, M.R.4    Klisovic, M.I.5    Marcucci, G.6    Byrd, J.C.7
  • 28
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone posttranslational modifications by peptide mass fingerprinting
    • L. Zhang, E.E. Eugeni, M.R. Parthun, M.A. Freitas Identification of novel histone posttranslational modifications by peptide mass fingerprinting Chromosoma 112 2003 77 86
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 29
    • 0942276237 scopus 로고    scopus 로고
    • Differentiation between peptides containing acetylated or trimethylated lysines by mass spectrometry: An application for determining lysine 9 acetylation and methylation of histone H3
    • K. Zhang, P.M. Yau, B. Chandrasekhar, R. New, R. Kondrat, B.S. Imai, M.E. Bradbury Differentiation between peptides containing acetylated or trimethylated lysines by mass spectrometry An application for determining lysine 9 acetylation and methylation of histone H3 Proteomics 4 2004 1 10
    • (2004) Proteomics , vol.4 , pp. 1-10
    • Zhang, K.1    Yau, P.M.2    Chandrasekhar, B.3    New, R.4    Kondrat, R.5    Imai, B.S.6    Bradbury, M.E.7
  • 31
    • 7544229161 scopus 로고    scopus 로고
    • Application of mass spectrometry to the identification and quantification of histone posttranslational modifications
    • M.A. Freitas, A.R. Sklenar, M.R. Parthun Application of mass spectrometry to the identification and quantification of histone posttranslational modifications J. Cell. Biochem. 92 2004 691 700
    • (2004) J. Cell. Biochem. , vol.92 , pp. 691-700
    • Freitas, M.A.1    Sklenar, A.R.2    Parthun, M.R.3
  • 32
  • 34
    • 0030606909 scopus 로고    scopus 로고
    • Separation of acetylated core histones by hydrophilic-interaction liquid chromatography
    • H. Lindner, B. Sarg, C. Meraner, W. Helliger Separation of acetylated core histones by hydrophilic-interaction liquid chromatography J. Chromatogr. A 743 1996 137 144
    • (1996) J. Chromatogr. a , vol.743 , pp. 137-144
    • Lindner, H.1    Sarg, B.2    Meraner, C.3    Helliger, W.4
  • 35
    • 0030859617 scopus 로고    scopus 로고
    • Application of hydrophilic-interaction liquid chromatography to the separation of phosphorylated H1 histones
    • H. Lindner, B. Sarg, W. Helliger Application of hydrophilic-interaction liquid chromatography to the separation of phosphorylated H1 histones J. Chromatogr. A 782 1997 55 62
    • (1997) J. Chromatogr. a , vol.782 , pp. 55-62
    • Lindner, H.1    Sarg, B.2    Helliger, W.3
  • 37
    • 0037986377 scopus 로고    scopus 로고
    • An integrated approach to identifying chemically induced posttranslational modifications using comparative MALDI-MS and targeted HPLC-ESI-MS/MS
    • M.D. Person, T.J. Monks, S.S. Lau An integrated approach to identifying chemically induced posttranslational modifications using comparative MALDI-MS and targeted HPLC-ESI-MS/MS Chem. Res. Toxicol. 16 2003 598 608
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 598-608
    • Person, M.D.1    Monks, T.J.2    Lau, S.S.3
  • 38
    • 0033523885 scopus 로고    scopus 로고
    • Silencing of metallothionein-I gene in mouse lymphosarcoma cells by methylation
    • S. Majumder, K. Ghoshal, Z. Li, Y. Bo, S.T. Jacob Silencing of metallothionein-I gene in mouse lymphosarcoma cells by methylation Oncogene 18 1999 6287 6295
    • (1999) Oncogene , vol.18 , pp. 6287-6295
    • Majumder, S.1    Ghoshal, K.2    Li, Z.3    Bo, Y.4    Jacob, S.T.5
  • 39
    • 0036889153 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase and DNA methyltransferase synergistically activate the methylated metallothionein I promoter by activating the transcription factor MTF-1 and forming an open chromatin structure
    • K. Ghoshal, J. Datta, S. Majumder, S. Bai, X. Dong, M. Parthun, S.T. Jacob Inhibitors of histone deacetylase and DNA methyltransferase synergistically activate the methylated metallothionein I promoter by activating the transcription factor MTF-1 and forming an open chromatin structure Mol. Cell. Biol. 22 2002 8302 8319
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8302-8319
    • Ghoshal, K.1    Datta, J.2    Majumder, S.3    Bai, S.4    Dong, X.5    Parthun, M.6    Jacob, S.T.7
  • 40
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • D.N. Perkins, D.J. Pappin, D.M. Creasy, J.S. Cottrell Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 20 1999 3551 3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 41
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • K.R. Clauser, P. Baker, A.L. Burlingame Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching Anal. Chem. 71 1999 2871 2882
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 43
    • 0031026487 scopus 로고    scopus 로고
    • Histones in transit: Cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells
    • L. Chang, S.S. Loranger, C. Mizzen, S.G. Ernst, C.D. Allis, A.T. Annunziato Histones in transit Cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells Biochemistry 36 1997 469 480
    • (1997) Biochemistry , vol.36 , pp. 469-480
    • Chang, L.1    Loranger, S.S.2    Mizzen, C.3    Ernst, S.G.4    Allis, C.D.5    Annunziato, A.T.6
  • 44
    • 0022650761 scopus 로고
    • Nonrandom utilization of acetylation sites in histones isolated from tetrahymena. Evidence for functionally distinct H4 acetylation sites
    • L.G. Chicoine, I.G. Schulman, R. Richman, R.G. Cook, C.D. Allis Nonrandom utilization of acetylation sites in histones isolated from tetrahymena. Evidence for functionally distinct H4 acetylation sites J. Biol. Chem. 261 1986 1071 1076
    • (1986) J. Biol. Chem. , vol.261 , pp. 1071-1076
    • Chicoine, L.G.1    Schulman, I.G.2    Richman, R.3    Cook, R.G.4    Allis, C.D.5
  • 45
    • 0023664032 scopus 로고
    • Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4
    • M. Couppez, A. Martin-Ponthieu, P. Sautiere Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4 J. Biol. Chem. 262 1987 2854 2860
    • (1987) J. Biol. Chem. , vol.262 , pp. 2854-2860
    • Couppez, M.1    Martin-Ponthieu, A.2    Sautiere, P.3
  • 47
    • 0024396097 scopus 로고
    • Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies
    • B.M. Turner, L.P. O'Neill, I.M. Allan Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies FEBS Lett. 253 1989 141 145
    • (1989) FEBS Lett. , vol.253 , pp. 141-145
    • Turner, B.M.1    O'Neill, L.P.2    Allan, I.M.3
  • 48
    • 11144226936 scopus 로고    scopus 로고
    • Histone H4 hyperacetylation precludes histone H4 lysine 20 trimethylation
    • B. Sarg, W. Helliger, H. Talasz, E. Koutzamani, H.H. Lindner Histone H4 hyperacetylation precludes histone H4 lysine 20 trimethylation J. Biol. Chem. 279 2004 53458 53464
    • (2004) J. Biol. Chem. , vol.279 , pp. 53458-53464
    • Sarg, B.1    Helliger, W.2    Talasz, H.3    Koutzamani, E.4    Lindner, H.H.5
  • 49
    • 0036311564 scopus 로고    scopus 로고
    • Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor
    • J. Li, Q. Lin, H.G. Yoon, Z.Q. Huang, B.D. Strahl, C.D. Allis, J. Wong Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor Mol. Cell. Biol. 22 2002 5688 5697
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5688-5697
    • Li, J.1    Lin, Q.2    Yoon, H.G.3    Huang, Z.Q.4    Strahl, B.D.5    Allis, C.D.6    Wong, J.7
  • 51
    • 2942752412 scopus 로고    scopus 로고
    • Regulation of NF-κB action by reversible acetylation
    • W.C. Greene, L.F. Chen Regulation of NF-κB action by reversible acetylation Novartis Foundation Symp. 259 2004 208/17 Discussion; 218-225
    • (2004) Novartis Foundation Symp. , vol.259
    • Greene, W.C.1    Chen, L.F.2


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