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H4  -  histone H4

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Disease relevance of H4

  • A histone H4 cDNA variant (H4-v.1) was cloned from a bovine adrenal medullary phage library using PCR as a method of detection [1].
  • The H4 phosphotransferase (Masaracchia, R. A., Kemp, B., and Walsh, D. A. (1977) J. Biol. Chem. 252, 7109-7117) from lymphosarcoma cells was isolated in a nonactive form [2].
  • Moreover, treatment of BLV-infected cells with TSA increased H4 acetylation at the viral promoter, showing a close correlation between the level of histone acetylation and transcriptional activation of the BLV LTR [3].
  • These data suggest that H4 interacts with the insulin, rather than the hypoxia/contraction, pathway for activation of glucose transport in muscle tissue, and that H4 acts either directly or indirectly to increase the number of insulin receptors at the surface of the muscle cell [4].
  • Here we examine Escherichia coli protein H-NS and calf thymus histones, H1, H2A, H2B, H3, and H4, for the presence of cPHB [5].
 

High impact information on H4

  • Lysine 14 of H3 and lysines 8 and 16 of H4 are highly preferred acetylation sites for Gcn5p [6].
  • Core particles were also reconstituted with calf thymus non-acetylated H3, H2A, and H2B with either mono-, di-, or tri-acetylated H4 isolated from cuttle -fish testes [7].
  • We also show that substitutions at histone H4 K91, K59, S47, and R92 and histone H3 K56 and K115 lead to hypersensitivity to DNA-damaging agents, linking the significance of the chemical identity of these modifiable residues to DNA metabolism [8].
  • A novel lipid hydroperoxide-derived cyclic covalent modification to histone H4 [9].
  • We have discovered that synthetic 4-oxo-nonenal or 4-oxo-2-nonenal-generated from 13(S)-hydroperoxyoctadecadienoic acid recognizes the specific amino acid motifs of His75, Ala76, and Lys77 in bovine histone H4 [9].
 

Biological context of H4

  • Thus, bovine histone H4-v.1 mRNA represents the first example of a histone H4 transcript that contains both 3'UTR characteristics of cell-cycle dependent and cell-cycle independent histone mRNAs [1].
  • The other sites of phosphorylation in H2B nd H4 are completely masked when the histones are complexed with DNA [10].
  • The first 3 residues in the amino acid sequence of Neurospora H3 histone are identical to the first 3 residues in calf and pea H3; Neurospora H1, H2A, and H4 histones have blocked NH2 termini, like their mammalian counterparts [11].
  • When a mixture of DNA-free core histones (H) from calf thymus is phosphorylated by the catalytic subunit of cAMP-dependent protein kinase, phosphate is incorporated primarily into H2B and, to a lesser extent, into H3 and H4 [10].
  • The finding of recognizable H1, H2A, H2B, H3, and H4 histones in Neurospora extends the range of eukaryotes now shown to contain a full complement of these strongly conserved chromosomal proteins, and supports the view that histones became involved in chromosome structure at a very early point in the evolution of eukaryotes [11].
 

Anatomical context of H4

  • Poly A-containing histone H4 mRNA variant (H4-v. 1): isolation and sequence determination from bovine adrenal medulla [1].
  • Despite many similarities to a protease-activated Ca2+/phospholipid-dependent enzyme isolated from lymphocytes (Ogawa, Y., Takai, Y., Kawahara, Y., Kimura, S., and Nishizuka, Y. (1981) J. Immunol. 127, 1369-1374), the H4 phosphotransferase was not activated by Ca2+, phospholipids, or any combination thereof [2].
  • Deacetylation towards the unacetylated and monoacetylated H4 population in fibroblasts began at the late 2-cell to 4-cell stage [12].
  • Chicken erythrocyte core histones H2A, H2B, H3, and H4 and lambdaDNA in 2 M NaCl were allowed to interact by stepwise decrease in the salt concentration [13].
  • The purified protamine kinase exhibited about 5% activity with casein, 8% with histone H2B, and less than 0.1% with histone H1, histone H4, glycogen synthase a from rabbit skeletal muscle, ovalbumin, bovine serum albumin, and phosvitin [14].
 

Associations of H4 with chemical compounds

  • Iodination of H4 tyrosine 72 is without effect on histone octamer stability [15].
  • Their electrophoretic mobilities in polyacrylamide gels and their amino acid compositions indicate that they are histones homologous, although not identical, to the H1, H2A, H2B, H3, and H4 histones of mammals [11].
  • The binding to DNA-cellulose of histones H2A, H2B, H3, and H4, which have had the first 20 to 30 amino acid residues removed from their NH2 termini, is indistinguishable from the binding to DNA-cellulose of the same intact histones, as judged by their salt elution profile [16].
  • Interaction of cGMP-dependent protein kinase with histones H2A, H2B, H3, and H4, or poly(L-arginine) resulted in changes in enzyme conformation such that inactivation of cGMP binding and activation of basal catalytic activity (assayed without cGMP) occurred [17].
  • A method is presented which enables the conformational status of H4 in nucleosomes to be determined by simply electrophoresing the histones on a Triton gel after probing nucleosomes with labeled iodine [18].
 

Other interactions of H4

  • A nucleosome-like structure containing DNA and the arginine-rich histones H3 and H4 [19].
  • Using a highly stringent binding assay in combination with DNA sequencing gels, we found that ADP-ribose polymers bind noncovalently to a specific group of chromatin proteins, i.e., histones H1, H2A, H2B, H3, and H4 and protamine [20].
  • Histones H2a, H2b, H3, and H4 associated with DNA are relatively resistant to acrosin [21].
  • MEP degraded oligopeptides, including bradykinin, alpha-neoendorphin, bovine adrenal medulla dodecapeptide, substance P, bombesin, neurotensin, and alpha-endorphin, but not polypeptides such as reduced lysozyme and histone H4, hence, MEP probably belongs to the family of endo-oligopeptidases [22].
 

Analytical, diagnostic and therapeutic context of H4

  • Conformational changes in the H3 . H4 histone complex. Serological and circular dichroism studies [23].
  • In each acetylated H4 subfraction, the acetylated tryptic peptides were identified by peptide mapping and amino acid analysis with reference to the peptide map of nonacetylated H4 [24].
  • N-terminal sequencing and immunoblotting with anti-histone antibodies confirmed the presence of both intact and proteolytically cleaved somatic histones H3, H2B, H2A, and H4 [25].
  • Bovine serum was analysed in the same manner on serial DNA-cellulose columns, and H4 and partially degraded H2A were detected by Western-blot analysis [26].
  • Two-dimensional peptide mapping of the chymotryptic and tryptic digest of [methyl-14C]histone H4 and analysis of the chymotryptic digest on HPLC have shown that only a single peptide is radiolabeled [27].

References

  1. Poly A-containing histone H4 mRNA variant (H4-v. 1): isolation and sequence determination from bovine adrenal medulla. Gendron, N., Dumont, M., Gagné, M.F., Lemaire, S. Biochim. Biophys. Acta (1998) [Pubmed]
  2. Activation of a cyclic AMP-independent protein kinase by an endogenous ATP-requiring protease from lymphosarcoma cells. de la Houssaye, B.A., Echols, T.K., Masaracchia, R.A. J. Biol. Chem. (1983) [Pubmed]
  3. Overlapping CRE and E box motifs in the enhancer sequences of the bovine leukemia virus 5' long terminal repeat are critical for basal and acetylation-dependent transcriptional activity of the viral promoter: implications for viral latency. Calomme, C., Dekoninck, A., Nizet, S., Adam, E., Nguyên, T.L., Van Den Broeke, A., Willems, L., Kettmann, R., Burny, A., Van Lint, C. J. Virol. (2004) [Pubmed]
  4. Histone H4 stimulates glucose transport activity in rat skeletal muscle. Louters, L.L., Henriksen, E.J., Tipton, C.M. Biochem. J. (1993) [Pubmed]
  5. Posttranslational modification of E. coli histone-like protein H-NS and bovine histones by short-chain poly-(R)-3-hydroxybutyrate (cPHB). Reusch, R.N., Shabalin, O., Crumbaugh, A., Wagner, R., Schröder, O., Wurm, R. FEBS Lett. (2002) [Pubmed]
  6. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Kuo, M.H., Brownell, J.E., Sobel, R.E., Ranalli, T.A., Cook, R.G., Edmondson, D.G., Roth, S.Y., Allis, C.D. Nature (1996) [Pubmed]
  7. Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation. Muller, S., Erard, M., Burggraf, E., Couppez, M., Sautière, P., Champagne, M., Van Regenmortel, M.H. EMBO J. (1982) [Pubmed]
  8. Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae. Hyland, E.M., Cosgrove, M.S., Molina, H., Wang, D., Pandey, A., Cottee, R.J., Boeke, J.D. Mol. Cell. Biol. (2005) [Pubmed]
  9. A novel lipid hydroperoxide-derived cyclic covalent modification to histone H4. Oe, T., Arora, J.S., Lee, S.H., Blair, I.A. J. Biol. Chem. (2003) [Pubmed]
  10. The in vitro phosphorylation of chromatin by the catalytic subunit of cAMP-dependent protein kinase. Taylor, S.S. J. Biol. Chem. (1982) [Pubmed]
  11. Histones of Neurospora crassa. Goff, C.G. J. Biol. Chem. (1976) [Pubmed]
  12. Changes in histone synthesis and modification at the beginning of mouse development correlate with the establishment of chromatin mediated repression of transcription. Wiekowski, M., Miranda, M., Nothias, J.Y., DePamphilis, M.L. J. Cell. Sci. (1997) [Pubmed]
  13. H3.H4 tetramer directs DNA and core histone octamer assembly in the nucleosome core particle. Jorcano, J.L., Ruiz-Carrillo, A. Biochemistry (1979) [Pubmed]
  14. Purification and properties of a distinct protamine kinase from the cytosol of bovine kidney cortex. Damuni, Z., Amick, G.D., Sneed, T.R. J. Biol. Chem. (1989) [Pubmed]
  15. Role of histone tyrosines in nucleosome formation and histone-histone interaction. Kleinschmidt, A.M., Martinson, H.G. J. Biol. Chem. (1984) [Pubmed]
  16. The use of DNA-cellulose for analyzing histone-DNA interactions. Discovery of nucleosome-like histone binding to single-stranded DNA. Palter, K.B., Alberts, B.M. J. Biol. Chem. (1979) [Pubmed]
  17. Regulation of cyclic nucleotide-dependent protein kinase activity by histones and poly(L-arginine). Walton, G.M., Gill, G.N. J. Biol. Chem. (1981) [Pubmed]
  18. Iodination of nucleosomes at low ionic strength: conformational changes in H4 and stabilization by H1. Burch, J.B., Martinson, H.G. Nucleic Acids Res. (1981) [Pubmed]
  19. A nucleosome-like structure containing DNA and the arginine-rich histones H3 and H4. Moss, T., Stephens, R.M., Crane-Robinson, C., Bradbury, E.M. Nucleic Acids Res. (1977) [Pubmed]
  20. Noncovalent interactions of poly(adenosine diphosphate ribose) with histones. Panzeter, P.L., Realini, C.A., Althaus, F.R. Biochemistry (1992) [Pubmed]
  21. Dispersion of mammalian sperm chromatin during fertilization: an in vitro study. Marushige, Y., Marushige, K. Biochim. Biophys. Acta (1978) [Pubmed]
  22. Substrate specificity of rabbit liver metalloendopeptidase and its new fluorogenic peptide substrates. Kojima, N., Kawabata, S., Makinose, Y., Nishino, N., Iwanaga, S. J. Biochem. (1995) [Pubmed]
  23. Conformational changes in the H3 . H4 histone complex. Serological and circular dichroism studies. Feldman, L., Beaudette, N.V., Stollar, B.D., Fasman, G.D. J. Biol. Chem. (1980) [Pubmed]
  24. Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4. Couppez, M., Martin-Ponthieu, A., Sautière, P. J. Biol. Chem. (1987) [Pubmed]
  25. Somatic histones are components of the perinuclear theca in bovine spermatozoa. Tovich, P.R., Oko, R.J. J. Biol. Chem. (2003) [Pubmed]
  26. Identification and isolation of soluble histones from bovine milk and serum. Waga, S., Tan, E.M., Rubin, R.L. Biochem. J. (1987) [Pubmed]
  27. Site specificity of histone H4 methylation by wheat germ protein-arginine N-methyltransferase. Disa, S.G., Gupta, A., Kim, S., Paik, W.K. Biochemistry (1986) [Pubmed]
 
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