메뉴 건너뛰기




Volumn 92, Issue 4, 2004, Pages 691-700

Application of mass spectrometry to the identification and quantification of histone post-translational modifications

Author keywords

Chromatin; Histone; Mass spectrometry; Post translational modification

Indexed keywords

HISTONE; PEPTIDE FRAGMENT;

EID: 7544229161     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.20106     Document Type: Article
Times cited : (118)

References (49)
  • 1
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger SL. 2002. Histone modifications in transcriptional regulation. Curr Opin Genet Dev 12:142-148.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 3
    • 0041382914 scopus 로고    scopus 로고
    • Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry
    • Cocklin RR, Wang M. 2003. Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry. J Protein Chem 22:327-334.
    • (2003) J Protein Chem , vol.22 , pp. 327-334
    • Cocklin, R.R.1    Wang, M.2
  • 4
    • 0014430329 scopus 로고
    • Calf and pea histone IV. I. Amino acid compositions and the identical COOH-terminal 19-residue sequence
    • DeLange RJ, Fambrough DM, Smith EL, Bonner J. 1968. Calf and pea histone IV. I. Amino acid compositions and the identical COOH-terminal 19-residue sequence. J Biol Chem 243:5906-5913.
    • (1968) J Biol Chem , vol.243 , pp. 5906-5913
    • Delange, R.J.1    Fambrough, D.M.2    Smith, E.L.3    Bonner, J.4
  • 6
  • 7
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. 1989. Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71.
    • (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
  • 9
    • 0014409959 scopus 로고
    • Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone
    • Gershey EL, Vidali G, Allfrey VG. 1968. Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. J Biol Chem 243:5018-5022.
    • (1968) J Biol Chem , vol.243 , pp. 5018-5022
    • Gershey, E.L.1    Vidali, G.2    Allfrey, V.G.3
  • 11
    • 0037099468 scopus 로고    scopus 로고
    • Histone modification and replacement in chromatin activation
    • Goll MG, Bestor TH. 2002. Histone modification and replacement in chromatin activation. Genes Dev 16: 1739-1742.
    • (2002) Genes Dev , vol.16 , pp. 1739-1742
    • Goll, M.G.1    Bestor, T.H.2
  • 12
    • 0036176357 scopus 로고    scopus 로고
    • The SIN domain of the histone octamer is essential for intramolecular folding of nucleosomal arrays
    • Horn PJ, Crowley KA, Carruthers LM, Hansen JC, Peterson CL. 2002. The SIN domain of the histone octamer is essential for intramolecular folding of nucleosomal arrays. Nat Struct Biol 9:167-171.
    • (2002) Nat Struct Biol , vol.9 , pp. 167-171
    • Horn, P.J.1    Crowley, K.A.2    Carruthers, L.M.3    Hansen, J.C.4    Peterson, C.L.5
  • 13
    • 0017327721 scopus 로고
    • Amino-terminal sequence identity of ubiquitin and the nonhistone component of nuclear protein A24
    • Hunt LT, Dayhoff MO. 1977. Amino-terminal sequence identity of ubiquitin and the nonhistone component of nuclear protein A24. Biochem Biophys Res Commun 74: 650-655.
    • (1977) Biochem Biophys Res Commun , vol.74 , pp. 650-655
    • Hunt, L.T.1    Dayhoff, M.O.2
  • 14
    • 0037382605 scopus 로고    scopus 로고
    • Functional consequences of histone modifications
    • Iizuka M, Smith MM. 2003. Functional consequences of histone modifications. Curr Opin Genet Dev 13:154-160.
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 154-160
    • Iizuka, M.1    Smith, M.M.2
  • 15
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F. 1988. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 60:2299-3001.
    • (1988) Anal Chem , vol.60 , pp. 2299-3001
    • Karas, M.1    Hillenkamp, F.2
  • 16
    • 0013431655 scopus 로고
    • UV Laser Matrix Desorption/Ionization Mass Spectrometry of Proteins in the 100,000 Dalton Range
    • Karas M, Bahr U, Hillenkamp F. 1989. UV Laser Matrix Desorption/ Ionization Mass Spectrometry of Proteins in the 100,000 Dalton Range. Int J Mass Spectrom Ion Proc 92:231-242.
    • (1989) Int J Mass Spectrom Ion Proc , vol.92 , pp. 231-242
    • Karas, M.1    Bahr, U.2    Hillenkamp, F.3
  • 17
    • 0032467640 scopus 로고    scopus 로고
    • Tip60 acetylates six lysines of a specific class in core histones in vitro
    • Kimura A, Horikoshi M. 1998. Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells 3:789-800.
    • (1998) Genes Cells , vol.3 , pp. 789-800
    • Kimura, A.1    Horikoshi, M.2
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 20
    • 0028801404 scopus 로고
    • Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription
    • Kruger W, Peterson CL, Sil A, Coburn C, Arents G, Moudrianakis EN, Herskowitz I. 1995. Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription. Genes Dev 9:2770-2779.
    • (1995) Genes Dev , vol.9 , pp. 2770-2779
    • Kruger, W.1    Peterson, C.L.2    Sil, A.3    Coburn, C.4    Arents, G.5    Moudrianakis, E.N.6    Herskowitz, I.7
  • 21
    • 0030699092 scopus 로고    scopus 로고
    • Sin mutations of histone H3: Influence on nucleosome core structure and function
    • Kurumizaka H, Wolffe AP. 1997. Sin mutations of histone H3: Influence on nucleosome core structure and function. Mol Cell Biol 17:6953-6969.
    • (1997) Mol Cell Biol , vol.17 , pp. 6953-6969
    • Kurumizaka, H.1    Wolffe, A.P.2
  • 22
    • 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 [see comments]. Nature 389: 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
  • 23
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EAaB, David J. 1997. Raster3D: Photorealistic Molecular Graphics. Methods Enzymology 277:505-524.
    • (1997) Methods Enzymology , vol.277 , pp. 505-524
    • Merritt, E.Aa.B.1    David, J.2
  • 24
    • 33947482638 scopus 로고
    • The occurrence of Epsilon-N-Methyl lysine in histones
    • Murray K. 1964. The occurrence of Epsilon-N-Methyl lysine in histones. Biochemistry 127:10-15.
    • (1964) Biochemistry , vol.127 , pp. 10-15
    • Murray, K.1
  • 25
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng HH, Feng Q, Wang H, Erdjument-Bromage H, Tempst P, Zhang Y, Struhl K. 2002. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev 16:1518-1527.
    • (2002) Genes Dev , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 26
    • 0014056415 scopus 로고
    • Phosphate and thiol groups in histone f3 from rat liver and thymus nuclei
    • Ord MG, Stocken LA. 1967. Phosphate and thiol groups in histone f3 from rat liver and thymus nuclei. Biochem J 102:631-636.
    • (1967) Biochem J , vol.102 , pp. 631-636
    • Ord, M.G.1    Stocken, L.A.2
  • 29
    • 0034599529 scopus 로고    scopus 로고
    • Histone H2A is required for normal centromere function in Saccharomyces cerevisiae
    • Pinto I, Winston F. 2000. Histone H2A is required for normal centromere function in Saccharomyces cerevisiae. Embo J 19:1598-1612.
    • (2000) Embo J , vol.19 , pp. 1598-1612
    • Pinto, I.1    Winston, F.2
  • 30
    • 0030999604 scopus 로고    scopus 로고
    • Histone octamer function in vivo: Mutations in the dimer-tetramer interfaces disrupt both gene activation and repression
    • Santisteban MS, Arents G, Moudrianakis EN, Smith MM. 1997. Histone octamer function in vivo: Mutations in the dimer-tetramer interfaces disrupt both gene activation and repression. Embo J 16:2493-2506.
    • (1997) Embo J , vol.16 , pp. 2493-2506
    • Santisteban, M.S.1    Arents, G.2    Moudrianakis, E.N.3    Smith, M.M.4
  • 32
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio Y, Eisenman RN. 2003. Histone sumoylation is associated with transcriptional repression. Proc Natl Acad Sci USA 100:13225-13230.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13225-13230
    • Shiio, Y.1    Eisenman, R.N.2
  • 34
    • 0037402422 scopus 로고    scopus 로고
    • Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4
    • Smith CM, Gafken PR, Zhang Z, Gottschling DE, Smith JB, Smith DL. 2003. Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4. Anal Biochem 316:23-33.
    • (2003) Anal Biochem , vol.316 , pp. 23-33
    • Smith, C.M.1    Gafken, P.R.2    Zhang, Z.3    Gottschling, D.E.4    Smith, J.B.5    Smith, D.L.6
  • 35
    • 0023666071 scopus 로고
    • Activation of the yeast HO gene by release from multiple negative controls
    • Sternberg PW, Stern MJ, Clark I, Herskowitz I. 1987. Activation of the yeast HO gene by release from multiple negative controls. Cell 48:567-577.
    • (1987) Cell , vol.48 , pp. 567-577
    • Sternberg, P.W.1    Stern, M.J.2    Clark, I.3    Herskowitz, I.4
  • 37
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • Suka N, Suka Y, Carmen AA, Wu J, Grunstein M. 2001. Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol Cell 8:473-479.
    • (2001) Mol Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 38
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100,000 by laser ionization time-of-flight mass spectrometry
    • Tanaka K, Waki H, Ido Y, Akita S, Yoshida Y, Yoshida T. 1988. Protein and Polymer Analyses up to m/z 100,000 by Laser Ionization Time-of-Flight Mass Spectrometry. Rapid Commun Mass Spectrom 2:151-153.
    • (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
  • 39
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner BM. 2002. Cellular memory and the histone code. Cell 111:285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 41
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F, Gafken PR, Gottschling DE. 2002. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109:745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 42
    • 0014430407 scopus 로고
    • Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones
    • Vidali G, Gershey EL, Allfrey VG. 1968. Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones. J Biol Chem 243: 6361-6366.
    • (1968) J Biol Chem , vol.243 , pp. 6361-6366
    • Vidali, G.1    Gershey, E.L.2    Allfrey, V.G.3
  • 43
    • 0030893061 scopus 로고    scopus 로고
    • Effects of Sin- Versions of histone H4 on yeast chromatin structure and function
    • Wechser MA, Kladde MP, Alfieri JA, Peterson CL. 1997. Effects of Sin- versions of histone H4 on yeast chromatin structure and function. Embo J 16:2086-2095.
    • (1997) Embo J , vol.16 , pp. 2086-2095
    • Wechser, M.A.1    Kladde, M.P.2    Alfieri, J.A.3    Peterson, C.L.4
  • 44
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White CL, Suto RK, Luger K. 2001. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. Embo J 20: 5207-5218.
    • (2001) Embo J , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 45
    • 0022029557 scopus 로고
    • Electrospray interface for liquid chromatographs and mass spectrometers
    • Whitehouse CM, Dreyer RN, Yamashita M, Fenn JB. 1985. Electrospray interface for liquid chromatographs and mass spectrometers. Anal Chem 57:675-679.
    • (1985) Anal Chem , vol.57 , pp. 675-679
    • Whitehouse, C.M.1    Dreyer, R.N.2    Yamashita, M.3    Fenn, J.B.4
  • 46
    • 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
    • Zhang K, Tang H, Huang L, Blankenship JW, Jones PR, Xiang F, Yau PM, Burlingame AL. 2002a. 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 306:259-269.
    • (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
  • 48
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • Zhang L, Eugeni EE, Parthun MR, Freitas MA. 2003. Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 112:77-86.
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 49
    • 0347123341 scopus 로고    scopus 로고
    • Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry
    • Zhang L, Freitas MA, Wickman J, Parthun MR, Klisovic MI, Marcucci G, Byrd JC. 2004. Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry. J Am Soc Mass Spectrom 15:77-86.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.