Abstract
Chromosomal proteins have been isolated from barley (Hordeum vulgare) and corn (Zea mays) nuclei by extraction with 5% perchloric acid. In each plant, one protein was shown to belong to the HMG proteins. Their molecular weights are very close to that of HMG 14 from chicken erythrocytes, as shown by electrophoretic mobility in SDS polyacrylamide gels. In acetic acid-urea-Triton polyacrylamide gels they migrate between HMG 1,2 and HMG 14, from chicken erythrocytes. Their amino acid compositions are typical of HMG proteins, with equivalent high values of acidic and basic residues.
Extraction of HMG's from purified barley chromatin fractions with 0.35 M NaCl considerably reduces histone H2 contamination and increases the yield of HMG up to 0.7% of the total histones. In this technique a second protein was extracted which is soluble in 2% Trichloroacetic acid and shows electrophoretic mobility analogous to those of HMG 14 and 17 from chicken erythrocytes. Whether or not these proteins are counterparts of the animal HMG's 1–2 or HMG's 14–17 is discussed.
Similar content being viewed by others
References
Allfrey VG: Postsynthetic modifications. In: Johns HW (ed) The HMG Chromosal Proteins. Academic Press, London, 1982, pp 123–148.
Bellard M, Kuo MT, Dretzen G, Chambon P: Differential nuclease sensitivity of the ovalbumin andβ-globin chromatin regions in erythrocytes and oviduct cells of laying hen. Nucleic Acids Res 8:2737–2750, 1980.
Ehresmann B, Imbault P, Weil JH: Spectrophotometric determination of protein concentration in cell extracts containing tRNA's and RNA's. Anal Biochem 54:454–463, 1973.
Gazit B, Panet A, Cedar H: Reconstitution of a deoxyribo nuclease I — sensitive structure on active genes. Proc Natl Acad Sci USA 77:1787–1790, 1980.
Goodwin GH, Mathew CGP: Role in gene structure and function. In: Johns EW (ed) The HMG chromosomal proteins. Academic Press, London, 1982, pp 193–221.
Goodwin GH, Nicolas RH, Johns EW: An improved large scale fractionation of high mobility group non-histone chromatin proteins. Biochim Biophys Acta 405:280–291, 1975.
Goodwin GH, Rabanni A, Nicolas RH, Johns EW: The isolation of the high mobility group non histone chromosal protein HMG 14. FEBS Lett 80:413–416, 1977.
Goodwin GH, Walker JM, Johns EW: The high mobility group (HMG) non histone chromosal proteins. In: Busch H (ed) The cell nucleus VI. Academic Press, New York, 1978, pp 181–219.
Hardison R, Chalkley R: Polyacrylamide gel electrophoretic fractionation of histones. In: Prescott DM (ed) Methods in cell biology. Chromatin and chromosome protein research 17, 1979, pp 235–251.
Laemmli UK: Clevage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685, 1970.
Langenbuch J, Philipps G, Gigot C: Fractionation and characterization of histones from barley (Hordeum vulgare) leaves. Plant Mol Biol 2:207–220, 1983.
Levy-Wilson B, Dixon GH: Renaturation kinetics of cDNA complementary to cytoplasmic polyadenylated RNA from rainbow trout testis. Accessibility of transcribed genes to pancreatic DNAse. Nucleic Acids Res 4:883–898, 1977.
Levy-Wilson B, Kuehl LR, Dixon GH: The release of high mobility group protein H6 and protamine gene sequences upon selective DNAse I degradation of trout testis chromatin. Nucleic Acids Res 8:2859–2869, 1980.
Levy-Wilson B, Wong NCW, Dixon GH: Selective association of the trout-specific H6 protein with chromatin regions susceptible to DNAse I and DNAse II: possible location of HMGT in the spacer region between core nucleosomes. Proc Natl Acad Sci USA 74:2810–2814, 1977.
Mathis D, Oudet P, Chambon P: Structure of transcribing chromatin. Progress in Nucleic Acids Res and Mol Biol 24:1–55, 1980.
Mayes ELV: Species and tissues specificity. In: Johns EW (ed) The HMG ehromosal proteins. Academic Press, London, 1982, pp 9–40.
Muller A, Philipps G, Gigot C: Properties of condensed chromatin in barley nuclei. Planta 149:69–77, 1980.
O'Farrell PH: High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007–4021, 1975.
Paterson R, Knight CA: Protein synthesis in Tobacco protoplasts infected with tobacco mosaic virus. Virology 64:10–22, 1975.
Reeves R, Candido EPM: Partial inhibition of histone deacetylase in active chromatin by HMG 14 and 17. Nucleic Acids Res 8:1947–1960, 1980.
Sanders C, Johns EW: A method for the large scale preparation of two chromatin proteins. Biochem Soc Trans 2:547–550, 1974.
Seyedin SM, Pehrson JR, Cole RD: Loss of chromosomal high mobility group proteins HMG1 and HMG2 when mouse neuroblastoma and Friend erythroleukemia cells become committed to differentiation. Proc Natl Acad Sci USA 78:5988–5992, 1981.
Spiker S, Key JL, Wakim B: Identification and fractionation of plant histones. Arch Biochem Biophys 176:510–518, 1976.
Spiker S, Mardian JKW, Isenberg I: Chromosomal HMG proteins occur in three eukaryotic kingdoms. Biochem Biophys Res Comm 82:129–135, 1978.
Spiker S, Murray MG, Thompson WF: DNase I sensitivity of transcriptionally active genes in intact nuclei and isolated chromatin of plants Proc Natl Acad Sci USA 80:815–819.
Walker JM, Johns EW: The isolation, characterization and partial sequences of the chicken erythrocyte non histone chromosomal proteins HMG 14 and HMG 17. Biochem J 185:383–386, 1980.
Weber K, Osborne M: The reliability of molecular weight determinations by dodecylsulfate polyacrylamide gel electrophoresis. J Biol Chem 244:4406–4412, 1969.
Weisbrod S: Active chromatin. Nature 297:289–295, 1982.
Weisbrod S: Properties of active nucleosomes as revealed by HMG 14 and 17 chromatography. Nucleic Acids Res 10:2017–2041, 1982.
Weisbrod S, Groudine M, Weintraub H: Interaction of HMG 14 and 17 with actively transcribed genes Cell 19:289–301, 1980.
Weisbrod S, Weintraub H: Isolation of subclass of nuclear proteins responsible for conferring a DNAse I — sensitive structure on globin chromatin. Proc Natl Acad Sci USA 76: 1979.