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Gene Review

H3F3C  -  H3 histone, family 3C

Gallus gallus

Synonyms: H3-I, H3-II, H3-III, H3-IV, H3-V, ...
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High impact information on H3F3A


Biological context of H3F3A


Anatomical context of H3F3A

  • The C-terminal hexapeptide of histone H3 of chicken erythrocytes (residues 130-135) corresponding to the sequence Ile-Arg-Gly-Glu-Arg-Ala ( IRGERA ) was prepared by solid-phase peptide synthesis and, after coupling to bovine serum albumin, was used to elicit antibodies in rabbits [9].
  • Targeted disruption of an H3-IV/H3-V gene pair causes increased expression of the remaining H3 genes in the chicken DT40 cell line [10].
  • In the DT40 chicken B cell line, H3-IV and H3-V, which are located in inverted orientation and share a 3'-untranslated region of 531 bp, produce about 24% of the steady-state level of total mRNAs from all the H3 genes [10].
  • The reactivity of chick erythrocyte and calf thymus histone H3 thiol groups toward 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) has been investigated both in the soluble, DNA-free state and in various nucleohistone complexes [11].
  • The competition between histones and low-molecular-weight chelators for Ni(II) in the cell nucleus, histidine and glutathione, is discussed on the basis of the above results, indicating that histone H3 is very likely to bind Ni(II) dissolved intracellularly from phagocytosed particulate nickel compounds [12].

Associations of H3F3A with chemical compounds

  • Small amounts of chymotrypsin rapidly and selectively cleaved at leucine 20 of histone H3 [13].
  • Finally, we find that although the fluorescence emission intensity of acetylethylenediamine-(1,5)-naphthol sulfonate-modified histone H3 is sensitive to octamer structure, SWI-SNF action does not alter fluorescence emission intensity [14].
  • We show here that different photo-cross-links form when these particles are prepared from H3 labeled with photoaffinity reagents on the unique histone H3 cysteine [15].
  • Substitution of Cys 110 of chicken histone H3 with N-iodoacetyl-N1-(5-sulpho-1-naphthyl)ethylenediamine or iodoacetamide prevents octamer formation in 2 M NaCl but does not prevent polyglutamic acid-mediated core particle assembly [16].
  • The intrinsic fluorescence of tryptophan is quenched by the labelled histone H3, but not by iodide, suggesting that non-histone (tryptophan-containing) proteins lie in close proximity to the labelled histone H3 but are not immediately accessible to external solvent [17].

Other interactions of H3F3A


Analytical, diagnostic and therapeutic context of H3F3A

  • Three of the isolated lambda recombinants have been analyzed by restriction enzyme mapping and Southern blotting; one histone H3 gene-encoding recombinant was further analyzed by DNA sequence determination [23].
  • Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers [24].
  • Peptide mapping of the novel H3-H4 and H3-H2B dimers showed that Cys-110 of histone H3 is cross-linked to the 18 amino acid C-terminal end of H4 or to the 66 amino acid C-terminal half of H2B [15].
  • In addition, protein sequence comparison of several vertebrate species revealed that the RT-PCR strategy we have developed for isolating the chicken centromeric histone H3 variant gene should be applicable to the isolation of CENP-A from a wide range of vertebrates [25].


  1. Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Hsu, J.Y., Sun, Z.W., Li, X., Reuben, M., Tatchell, K., Bishop, D.K., Grushcow, J.M., Brame, C.J., Caldwell, J.A., Hunt, D.F., Lin, R., Smith, M.M., Allis, C.D. Cell (2000) [Pubmed]
  2. A chicken histone H3 gene contains intervening sequences. Engel, J.D., Sugarman, B.J., Dodgson, J.B. Nature (1982) [Pubmed]
  3. Correlation between histone lysine methylation and developmental changes at the chicken beta-globin locus. Litt, M.D., Simpson, M., Gaszner, M., Allis, C.D., Felsenfeld, G. Science (2001) [Pubmed]
  4. The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres. Okada, M., Cheeseman, I.M., Hori, T., Okawa, K., McLeod, I.X., Yates, J.R., Desai, A., Fukagawa, T. Nat. Cell Biol. (2006) [Pubmed]
  5. Modulation of histone H3 variant synthesis during the myoblast-myotube transition of chicken myogenesis. Wunsch, A.M., Lough, J. Dev. Biol. (1987) [Pubmed]
  6. Nucleotide sequences of new members (H3-IV and H3-V) of the chicken H3 histone-encoding gene family. Setoguchi, Y., Nakayama, T. Nucleic Acids Res. (1991) [Pubmed]
  7. Nucleotide sequences of two members of the chicken H3 histone-encoding gene family. Nakayama, T. Gene (1991) [Pubmed]
  8. Silencing of transgene transcription precedes methylation of promoter DNA and histone H3 lysine 9. Mutskov, V., Felsenfeld, G. EMBO J. (2004) [Pubmed]
  9. Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits. Muller, S., Himmelspach, K., Van Regenmortel, M.H. EMBO J. (1982) [Pubmed]
  10. Targeted disruption of an H3-IV/H3-V gene pair causes increased expression of the remaining H3 genes in the chicken DT40 cell line. Takami, Y., Takeda, S., Nakayama, T. J. Mol. Biol. (1995) [Pubmed]
  11. Thiol reactivity of histone H3 in soluble and DNA-associated histone complexes: evidence for allosteric and torsional regulation. Feinstein, D.L., Moudrianakis, E.N. Biochemistry (1986) [Pubmed]
  12. Interaction of Nickel(II) with histones: in vitro binding of nickel(II) to the core histone tetramer. Bal, W., Karantza, V., Moudrianakis, E.N., Kasprzak, K.S. Arch. Biochem. Biophys. (1999) [Pubmed]
  13. The action of chymotrypsin on nucleosome cores. Histone products and conformational effects of limited digestion. Rosenberg, N.L., Smith, R.M., Rill, R.L. J. Biol. Chem. (1986) [Pubmed]
  14. Roles of the histone H2A-H2B dimers and the (H3-H4)(2) tetramer in nucleosome remodeling by the SWI-SNF complex. Boyer, L.A., Shao, X., Ebright, R.H., Peterson, C.L. J. Biol. Chem. (2000) [Pubmed]
  15. H3 Cys-110 is in close proximity to the C-terminal regions of H2B and H4 in a nucleosome core with an altered internal arrangement of histones. Kahr, W.H., Lewis, P.N., Pulleyblank, D.E. Biochemistry (1990) [Pubmed]
  16. Fluorescent labelling of histone H3: effect on histone-histone interaction and core particle assembly. Lindsey, G.G., Thompson, P., Pretorius, L., von Holt, C. FEBS Lett. (1985) [Pubmed]
  17. The in situ labeling of histone H3 in chromatin by a fluorescent probe. Mooney, D., Thompson, L.M., Simpkins, H. Biochim. Biophys. Acta (1980) [Pubmed]
  18. Differentiation-dependent alterations in histone methylation and chromatin architecture at the inducible chicken lysozyme gene. Lefevre, P., Lacroix, C., Tagoh, H., Hoogenkamp, M., Melnik, S., Ingram, R., Bonifer, C. J. Biol. Chem. (2005) [Pubmed]
  19. A complex chromatin landscape revealed by patterns of nuclease sensitivity and histone modification within the mouse beta-globin locus. Bulger, M., Schübeler, D., Bender, M.A., Hamilton, J., Farrell, C.M., Hardison, R.C., Groudine, M. Mol. Cell. Biol. (2003) [Pubmed]
  20. A proliferative role for Wnt-3a in chick somites. Galli, L.M., Willert, K., Nusse, R., Yablonka-Reuveni, Z., Nohno, T., Denetclaw, W., Burrus, L.W. Dev. Biol. (2004) [Pubmed]
  21. Binding of non-histone chromosomal protein HMG1 to histone H3 in nucleosomes detected by photochemical cross-linking. Stros, M. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  22. Chicken ovalbumin promoter is demethylated upon expression in the regions specifically involved in estrogen-responsiveness. Morshed, M., Sano, S., Nishimiya, D., Ando, M., Nishijima, K., Iijima, S. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  23. Histone genes are clustered but not tandemly repeated in the chicken genome. Engel, J.D., Dodgson, J.B. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  24. Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers. Leuba, S.H., Bustamante, C., van Holde, K., Zlatanova, J. Biophys. J. (1998) [Pubmed]
  25. Characterization of chicken CENP-A and comparative sequence analysis of vertebrate centromere-specific histone H3-like proteins. Régnier, V., Novelli, J., Fukagawa, T., Vagnarelli, P., Brown, W. Gene (2003) [Pubmed]
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