Abstract
In a recent publication the isolation and some characteristics of an anti-histone 3 monoclonal antibody, 1GB3 were described (Muller et al. FEBS Lett. 182: 459–464, 1985). We now report that the epitope recognized is phylogenetically conserved and located in the N-terminal part of H3, most likely between residues 40 and 50. Using the ELISA technique we found this region to be accessible in chromatin to the monoclonal antibody. The effect of non-ionic detergents on the adsorbtion of chromatin on microtiter plates was studied in this context.
Immunological analysis of the reaction of the monoclonal antibody with chromatin by immunoinhibition and immunosedimentation shows that the H3 epitope is accessible in both folded and unfolded chromatin fibre as well as in high- and low-molecular weight oligonucleosomes.
Similar content being viewed by others
Abbreviations
- BSA:
-
Bovine srum albumin
- mab:
-
Monoclonal antibody
- PBS:
-
Phosphate buffered saline
- PMSF:
-
Phenylmethyl sulfonyl fluoride
References
Bustin M (1979) Current topics in Microbiology and Immunology 88: 105–142
Benezra R, Blankstein LA, Stollar BD & Levy SB (1981) J. Biol. Chem. 256: 6837–6841
Takahashi K & Tashiro Y (1979) Eur. J. Biochem. 97: 353–360
Mazen A, DeMurcia G, Bernard S, Pouget J & Champagne M (1982) Eur. J. Biochem. 127: 168–176
Dimitrov SI, Russanova VR & Pashev IG (1987) The EMBO J. 6: 2387–2392
Muller S, Eraid M, Burggraf E, Couppez M, Sautiere P, Champagne M & VanRegenmortel MHV (1982) The EMBO J. 1: 939–944
Muller S, Mazen A, Martinage A & VanRegenmortel MHV (1984) The EMBO J. 3: 2431–2436
Turner BM (1982) Chromosoma (Berl.) 87: 345–357
Mendelson E & Bustin M (1984) Biochemistry 23: 3459–3466
Mendelson E, Smith BJ & Bustin M (1984) Biochemistry 23: 3466–3471
Laskov R, Muller S, Hochberg M, Giloh H, VanRegenmortel MHV & Eilat D (1984) Eur. J. Immunol. 14: 74–81
Muller S, Jockers-Wretou E, Sekeris CE, VanRegenmortel MHV & Bautz FA (1985) FEBS Lett. 182: 459–464
Shindo H, Mc Ghee JD & Cohen JS (1980) Biopolymers 19: 523–538
Blobel G & Potter VR (1966) Science 154: 1662–1665
Johns EW (1977) Meth. Cell Biol. 14: 183–203
Johns EW (1967) Biochem. J. 105: 611–614
Ivanova VS (1984) Prep Biochem. 14: 405–416
Lekanidou R, Tsitilou SG & Kafatos FC (1980) Insect. Biochem. 10: 367–374
Johns EW, Forrester S & Riches PL (1972) Arch. Biochem. Biophys. 132: 287–296
Weintraub H, Patter K & VanLente F (1975) Cell 6: 85–110
Panyim S & Chalkley R (1969) Arch. Biochem. Biophys. 130: 337–346
Burch JBE & Martinson HG (1981) Nucleic Acids Res., 9: 4367–4385
Hartley BS (1970) Biochem. J. 119: 805–822
Bustin M, Simpson RT, Sperling R & Goldblatt D (1977) Biochemistry 16: 5381–5385
Weber K, Bibring T & Osborn M (1975) Exp. Cell Res. 95: 111–120
Russanova VR, Venkov CD & Tsanev RG (1980) Cell Differentiation 9: 339–350
Symington J, Green M & Krackmann K (1981) Proc. Natl. Acad. Sci. USA 78: 178–181
Towbin H, Staehelin T & Gordin J (1979) Proc. Natl. Acad. Sci. USA 76: 4350–4354
Goldblatt D & Bustin M (1980) Biochem. Biophys. Acta 606: 304–315
Bradford M (1976) Anal. Biochem. 72: 254–284
VonHolt C, Strickland N, Brandt WF & Strickland MS (1979) FEBS Lett. 100: 201–218
Franklin SG & Zweidler A (1977) Nature 266: 273–275
Zweidler A (1984) In: Stein GS, Stein JC & Marzluff WF (Eds) Histone Genes and Histone Gene Expression (pp. 339–371)
Tsanev RG (1983) Molec. Biol. Rep. 9: 9–17
Absolom D & VanRegenmortel MHV (1977) FEBS Lett. 81: 419–422
Chipev CC (1983) Int. J. Biol. Macromol. 5: 10–16
Zweidler A (1978) Methods in Cell Biol. 17: 223–233
Gardas A & Lewartowska A (1988) J. Immunol. Methods 106: 251–255
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Jockers-Wretou, E., Russanova, V. & Venkov, C. Accessibility of an epitope common to all histone H3 variants in folded and unfolded chromatin as studied by a monoclonal antibody. Molecular Biology Reports 13, 123–131 (1988). https://doi.org/10.1007/BF00444307
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00444307