메뉴 건너뛰기




Volumn 464, Issue , 2008, Pages 285-302

Purification and analysis of variant and modified histones using 2D PAGE

Author keywords

Acetylation; Electroelution; Histone modification; Histone variants; Phosphorylation; SDS PAGE; Triton X 100; Two dimensional polyacrylamidegelelectrophoresis; Ubiquitylation; Western analysis

Indexed keywords


EID: 60349130646     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60327-461-6_16     Document Type: Article
Times cited : (11)

References (49)
  • 1
    • 33947524604 scopus 로고    scopus 로고
    • Histone variants - the structure behind the function
    • Ausio, J. (2006). Histone variants - the structure behind the function. Brief. Funct. Genomics Proteomics 5, 228-243.
    • (2006) Brief. Funct. Genomics Proteomics , vol.5 , pp. 228-243
    • Ausio, J.1
  • 2
    • 33646239638 scopus 로고    scopus 로고
    • Hake, S.B. and C.D. Allis (2006). Histone H3 variants and their potential role in indexing mammalian genomes: The H3 barcode hypothesis. Proc. Natl. Acad. Sci. USA 103, 6428-6435.
    • Hake, S.B. and C.D. Allis (2006). Histone H3 variants and their potential role in indexing mammalian genomes: The "H3 barcode hypothesis." Proc. Natl. Acad. Sci. USA 103, 6428-6435.
  • 3
    • 13244255650 scopus 로고    scopus 로고
    • Histone variants: Deviants?
    • Kamakaka, R.T. and S. Biggins (2005). Histone variants: Deviants? Genes Dev. 19, 295-316.
    • (2005) Genes Dev , vol.19 , pp. 295-316
    • Kamakaka, R.T.1    Biggins, S.2
  • 4
    • 27144504752 scopus 로고    scopus 로고
    • Histones in functional diversification: Core histone variants
    • Pusarla, R.H. and P. Bhargava (2005). Histones in functional diversification: Core histone variants. FEBS J. 272, 5149-5168.
    • (2005) FEBS J , vol.272 , pp. 5149-5168
    • Pusarla, R.H.1    Bhargava, P.2
  • 5
    • 1642575958 scopus 로고    scopus 로고
    • Purification and analyses of histone H1 variants and H1 posttranslational modifications
    • Mizzen, C.A. (2004). Purification and analyses of histone H1 variants and H1 posttranslational modifications. Methods Enzymol. 375, 278-297.
    • (2004) Methods Enzymol , vol.375 , pp. 278-297
    • Mizzen, C.A.1
  • 6
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007). Chromatin modifications and their function. Cell 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 7
    • 33646900510 scopus 로고    scopus 로고
    • The tale beyond the tail: Histone core domain modifications and the regulation of chromatin structure
    • Mersfelder, E.L. and M.R. Parthun (2006). The tale beyond the tail: Histone core domain modifications and the regulation of chromatin structure. Nucleic Acids Res. 34, 2653-2662.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2653-2662
    • Mersfelder, E.L.1    Parthun, M.R.2
  • 8
    • 17244370475 scopus 로고    scopus 로고
    • Histone modifications: Combinatorial complexity or cumulative simplicity?
    • Henikoff, S. (2005). Histone modifications: Combinatorial complexity or cumulative simplicity? Proc. Natl. Acad. Sci. USA 102, 5308-5309.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5308-5309
    • Henikoff, S.1
  • 9
    • 0034885838 scopus 로고    scopus 로고
    • Phosphorylation of histone variant regions in chromatin: Unlocking the linker?
    • Green, G.R. (2001). Phosphorylation of histone variant regions in chromatin: Unlocking the linker? Biochem. Cell Biol. 79, 275-287.
    • (2001) Biochem. Cell Biol , vol.79 , pp. 275-287
    • Green, G.R.1
  • 10
    • 0017795309 scopus 로고
    • Resolution of histones by polyacrylamide gel electrophoresis in presence of nonionic detergents
    • Zweidler, A. (1978). Resolution of histones by polyacrylamide gel electrophoresis in presence of nonionic detergents. Methods Cell Biol. 17, 223-333.
    • (1978) Methods Cell Biol , vol.17 , pp. 223-333
    • Zweidler, A.1
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0015240498 scopus 로고
    • The molecular weights of vertebrate histones exploiting a modified sodium dodecyl sulfate electrophoretic method
    • Panyim, S. and R. Chalkley (1971). The molecular weights of vertebrate histones exploiting a modified sodium dodecyl sulfate electrophoretic method. J. Biol. Chem. 246, 7557-7560.
    • (1971) J. Biol. Chem , vol.246 , pp. 7557-7560
    • Panyim, S.1    Chalkley, R.2
  • 13
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfeld, R.A., U.J. Lewis, and D.E. Williams (1962). Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195, 281-283.
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 14
    • 0014478325 scopus 로고
    • High resolution acrylamide gel electrophoresis of histones
    • Panyim, S. and R. Chalkley (1969). High resolution acrylamide gel electrophoresis of histones. Arch. Biochem. Biophys. 130, 337-346.
    • (1969) Arch. Biochem. Biophys , vol.130 , pp. 337-346
    • Panyim, S.1    Chalkley, R.2
  • 15
    • 0018114028 scopus 로고
    • Separation of histones from contaminating ribosomal proteins by two-dimensional gel electrophoresis
    • Savic, A. and D. Poccia (1978). Separation of histones from contaminating ribosomal proteins by two-dimensional gel electrophoresis. Anal. Biochem. 88, 573-579.
    • (1978) Anal. Biochem , vol.88 , pp. 573-579
    • Savic, A.1    Poccia, D.2
  • 16
    • 0019435602 scopus 로고
    • Transitions in histone variants of the male pronucleus following fertilization and evidence for a maternal store of cleavage-stage histones in the sea urchin egg
    • Poccia, D., J. Salik, and G. Krystal (1981). Transitions in histone variants of the male pronucleus following fertilization and evidence for a maternal store of cleavage-stage histones in the sea urchin egg. Dev. Biol. 82, 287-296.
    • (1981) Dev. Biol , vol.82 , pp. 287-296
    • Poccia, D.1    Salik, J.2    Krystal, G.3
  • 17
    • 0019417164 scopus 로고
    • Electrophoretic analysis of the stored histone pool in unfertilized sea urchin eggs: Quantification and identification by antibody binding
    • Salik, J., L. Herlands, H.P. Hoffmann, and D. Poccia (1981). Electrophoretic analysis of the stored histone pool in unfertilized sea urchin eggs: Quantification and identification by antibody binding. J. Cell Biol. 90, 385-395.
    • (1981) J. Cell Biol , vol.90 , pp. 385-395
    • Salik, J.1    Herlands, L.2    Hoffmann, H.P.3    Poccia, D.4
  • 18
    • 0021160721 scopus 로고
    • Remodeling of sperm chromatin following fertilization: Nucleosome repeat length and histone variant transitions in the absence of DNA synthesis
    • Poccia, D., T. Greenough, G.R. Green, E. Nash, J. Erickson, and M. Gibbs (1984). Remodeling of sperm chromatin following fertilization: Nucleosome repeat length and histone variant transitions in the absence of DNA synthesis. Dev. Biol. 104, 274-286.
    • (1984) Dev. Biol , vol.104 , pp. 274-286
    • Poccia, D.1    Greenough, T.2    Green, G.R.3    Nash, E.4    Erickson, J.5    Gibbs, M.6
  • 19
    • 0021954151 scopus 로고
    • Phosphorylation of sea urchin sperm H1 and H2B histones precedes chromatin decondensation and H1 exchange during pronuclear formation
    • Green, G.R. and D.L. Poccia (1985). Phosphorylation of sea urchin sperm H1 and H2B histones precedes chromatin decondensation and H1 exchange during pronuclear formation. Dev. Biol. 108, 235-245.
    • (1985) Dev. Biol , vol.108 , pp. 235-245
    • Green, G.R.1    Poccia, D.L.2
  • 20
    • 0023266321 scopus 로고
    • Transitions in histone variants during sea urchin spermatogenesis
    • Poccia, D.L, M.V. Simpson, and G.R. Green (1987). Transitions in histone variants during sea urchin spermatogenesis. Dev. Biol. 121, 445-453.
    • (1987) Dev. Biol , vol.121 , pp. 445-453
    • Poccia, D.L.1    Simpson, M.V.2    Green, G.R.3
  • 21
    • 0024297520 scopus 로고
    • Interaction of sperm histone variants and linker DNA during spermiogenesis in the sea urchin
    • Green, G.R. and D.L. Poccia (1988). Interaction of sperm histone variants and linker DNA during spermiogenesis in the sea urchin. Biochemistry 27, 619-625.
    • (1988) Biochemistry , vol.27 , pp. 619-625
    • Green, G.R.1    Poccia, D.L.2
  • 22
    • 0024346026 scopus 로고
    • Phosphorylation of sea urchin histone CS H2A
    • Green, G.R. and D.L. Poccia (1989). Phosphorylation of sea urchin histone CS H2A. Dev. Biol. 134, 413-419.
    • (1989) Dev. Biol , vol.134 , pp. 413-419
    • Green, G.R.1    Poccia, D.L.2
  • 23
    • 0025250419 scopus 로고
    • Sperm histones and chromatin structure of the "primitive" sea urchin Eucidaris tribuloides
    • Vodicka, M., G.R. Green, and D.L. Poccia (1990). Sperm histones and chromatin structure of the "primitive" sea urchin Eucidaris tribuloides. J. Exp. Zool. 256, 179-188.
    • (1990) J. Exp. Zool , vol.256 , pp. 179-188
    • Vodicka, M.1    Green, G.R.2    Poccia, D.L.3
  • 24
    • 0025296295 scopus 로고
    • 6DMAP inhibits chromatin decondensation but not sperm histone kinase in sea urchin male pronuclei
    • Poccia, D., W. Pavan, and G.R. Green (1990). 6DMAP inhibits chromatin decondensation but not sperm histone kinase in sea urchin male pronuclei. Exp. Cell Res. 188, 226-234.
    • (1990) Exp. Cell Res , vol.188 , pp. 226-234
    • Poccia, D.1    Pavan, W.2    Green, G.R.3
  • 25
    • 0001763471 scopus 로고
    • Phosphorylation of plant H2A histones
    • Green, G.R., L.C. Gustavsen, and D.L. Poccia (1990). Phosphorylation of plant H2A histones. Plant Phys. 93, 1241-1245.
    • (1990) Plant Phys , vol.93 , pp. 1241-1245
    • Green, G.R.1    Gustavsen, L.C.2    Poccia, D.L.3
  • 26
    • 0025913042 scopus 로고
    • A complex pattern of H2A phosphorylation in the mouse testis
    • Green, G.R., J.C. Patel, N.B. Hecht, and D.L. Poccia (1991). A complex pattern of H2A phosphorylation in the mouse testis. Exp. Cell Res. 195, 8-12.
    • (1991) Exp. Cell Res , vol.195 , pp. 8-12
    • Green, G.R.1    Patel, J.C.2    Hecht, N.B.3    Poccia, D.L.4
  • 28
    • 0038531105 scopus 로고    scopus 로고
    • Multiple roles for Saccharomyces cerevisiae histone H2A in telomere position effect, Spt phenotypes and double-strand-break repair
    • Wyatt, H.R., H. Liaw, G.R. Green, and A.J. Lustig (2003). Multiple roles for Saccharomyces cerevisiae histone H2A in telomere position effect, Spt phenotypes and double-strand-break repair. Genetics 164, 47-64.
    • (2003) Genetics , vol.164 , pp. 47-64
    • Wyatt, H.R.1    Liaw, H.2    Green, G.R.3    Lustig, A.J.4
  • 29
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D.W., S. G. Fischer, M. W. Kirschner, and U. K. Laemmli (1977). Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102-1106.
    • (1977) J. Biol. Chem , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 30
    • 0020149539 scopus 로고
    • A multisample device for electroelution, concentration, and dialysis of proteins from fixed and stained gel slices
    • Green, G.R., D. Poccia, and L. Herlands (1982). A multisample device for electroelution, concentration, and dialysis of proteins from fixed and stained gel slices. Anal. Biochem. 123, 66-73.
    • (1982) Anal. Biochem , vol.123 , pp. 66-73
    • Green, G.R.1    Poccia, D.2    Herlands, L.3
  • 31
    • 0021017817 scopus 로고
    • Histone-like protein in the archaebacterium Sulfolobus acidocaldarius
    • Green, G.R., D.G. Searcy, and R.J. DeLange (1983). Histone-like protein in the archaebacterium Sulfolobus acidocaldarius. Biochim. Biophys. Acta 741, 251-257.
    • (1983) Biochim. Biophys. Acta , vol.741 , pp. 251-257
    • Green, G.R.1    Searcy, D.G.2    DeLange, R.J.3
  • 32
    • 0023192441 scopus 로고
    • Western blotting of histones from acid-urea-Triton and sodium dodecyl sulfate-polyacrylamide gels
    • Waterborg, J.H. and R.E. Harrington (1987). Western blotting of histones from acid-urea-Triton and sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 162, 430-434.
    • (1987) Anal. Biochem , vol.162 , pp. 430-434
    • Waterborg, J.H.1    Harrington, R.E.2
  • 33
    • 0026557178 scopus 로고
    • Western blotting and immunochemical detection of histones electrophoretically resolved on acid-urea-triton and sodium dodecyl sulfate-polyacrylamide gels
    • Delcuve, G.P. and J.R. Davie (1992). Western blotting and immunochemical detection of histones electrophoretically resolved on acid-urea-triton and sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 200, 339-341.
    • (1992) Anal. Biochem , vol.200 , pp. 339-341
    • Delcuve, G.P.1    Davie, J.R.2
  • 34
    • 0028951895 scopus 로고
    • Rapid and effective Western blotting of histones from acid-urea-Triton and sodium dodecyl sulfate polyacrylamide gels: Two different approaches depending on the subsequent qualitative or quantitative analysis
    • Thiriet, C. and P. Albert (1995). Rapid and effective Western blotting of histones from acid-urea-Triton and sodium dodecyl sulfate polyacrylamide gels: Two different approaches depending on the subsequent qualitative or quantitative analysis. Electrophoresis 16, 357-361.
    • (1995) Electrophoresis , vol.16 , pp. 357-361
    • Thiriet, C.1    Albert, P.2
  • 35
    • 0032528407 scopus 로고    scopus 로고
    • Efficient antibody generation using histone H1 subfractions purified from Western blots
    • Albert, P. and C. Redon (1998). Efficient antibody generation using histone H1 subfractions purified from Western blots. Anal. Biochem. 261, 87-92.
    • (1998) Anal. Biochem , vol.261 , pp. 87-92
    • Albert, P.1    Redon, C.2
  • 36
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg, A., W. Weiss, and M.J. Dunn (2004). Current two-dimensional electrophoresis technology for proteomics. Proteomics 4, 3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 37
    • 33645566839 scopus 로고    scopus 로고
    • Characterizing phosphoproteins and phosphoproteomes using mass spectrometry
    • Goshe, M. B. (2006). Characterizing phosphoproteins and phosphoproteomes using mass spectrometry. Brief. Funct. Genomics Proteomics 4, 363-376.
    • (2006) Brief. Funct. Genomics Proteomics , vol.4 , pp. 363-376
    • Goshe, M.B.1
  • 38
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B. and R. Aebersold (2006). Mass spectrometry and protein analysis. Science 312, 212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 39
    • 33748571491 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry
    • Wittmann-Liebold, B., H.R. Graack, and T. Pohl (2006). Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry. Proteomics 6, 4688-4703.
    • (2006) Proteomics , vol.6 , pp. 4688-4703
    • Wittmann-Liebold, B.1    Graack, H.R.2    Pohl, T.3
  • 40
    • 33846809241 scopus 로고    scopus 로고
    • Characterization of histones and their post-translational modifications by mass spectrometry
    • Garcia, B.A., J. Shabanowitz, and D.F. Hunt (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
  • 42
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • Wisniewski, J.R., A. Zougman, S. Krüger, and M. Mann (2007). Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol. Cell. Proteomics 6, 72-87.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Krüger, S.3    Mann, M.4
  • 43
    • 33645471026 scopus 로고    scopus 로고
    • Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry
    • Bonenfant, D., M. Coulot, H. Towbin, P. Schindler, and J. Oostrum (2006). Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry. Mol. Cell. Proteomics 5, 541-552.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 541-552
    • Bonenfant, D.1    Coulot, M.2    Towbin, H.3    Schindler, P.4    Oostrum, J.5
  • 45
    • 32344452605 scopus 로고    scopus 로고
    • Precise characterization of human histones in the H2A gene family by top down mass spectrometry
    • Boyne, M.T., J.J. Pesavento, C.A. Mizzen, and N.L. Kelleher (2006). Precise characterization of human histones in the H2A gene family by top down mass spectrometry. Proteome Res. 5, 248-253.
    • (2006) Proteome Res , vol.5 , pp. 248-253
    • Boyne, M.T.1    Pesavento, J.J.2    Mizzen, C.A.3    Kelleher, N.L.4
  • 46
    • 23944472674 scopus 로고    scopus 로고
    • Mass spectrometric analysis of histone posttranslational modifications
    • Burlingame, A.L., X. Zhang, and R.J. Chalkley (2005). Mass spectrometric analysis of histone posttranslational modifications. Methods 36, 383-394.
    • (2005) Methods , vol.36 , pp. 383-394
    • Burlingame, A.L.1    Zhang, X.2    Chalkley, R.J.3
  • 47
    • 0022585279 scopus 로고
    • Nuclei and chromosomal proteins
    • Poccia, D.L. and G.R. Green (1986). Nuclei and chromosomal proteins. Methods Cell Biol. 27, 153-174.
    • (1986) Methods Cell Biol , vol.27 , pp. 153-174
    • Poccia, D.L.1    Green, G.R.2
  • 48
    • 0018340310 scopus 로고
    • A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction
    • Henderson, L.E., S. Oroszlan, and W. Konigsberg (1979). A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction. Anal. Biochem. 93, 153-157.
    • (1979) Anal. Biochem , vol.93 , pp. 153-157
    • Henderson, L.E.1    Oroszlan, S.2    Konigsberg, W.3
  • 49
    • 0022339214 scopus 로고
    • Genetic control of chromatin structure 5′ to the qa-x and qa-2 genes of Neurospora
    • Baum, J.A. and N.H. Giles (1985). Genetic control of chromatin structure 5′ to the qa-x and qa-2 genes of Neurospora. J. Mol. Biol. 182, 79-89.
    • (1985) J. Mol. Biol , vol.182 , pp. 79-89
    • Baum, J.A.1    Giles, N.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.