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. 1976 Mar 1;68(3):430–439. doi: 10.1083/jcb.68.3.430

Presence of histones in Aspergillus nidulans

PMCID: PMC2109667  PMID: 799641

Abstract

Five major histone proteins have been extracted from chromatin isolated from purified nuclei of the fungus, Aspergillus nidulans. These proteins had chromatographic properties which were similar to reference calf thymus histones and were purified to electrophoretic homegeneity by gel chromatography of Bio-Gel P10, Bio-Gel P60, and Sephadex G-100. Electrophoresis of these proteins in three different systems (urea- starch, urea-acetic acid polyacrylamide, and discontinuous SDS polyacrylamide) showed that the A. nidulans histones H3 and H4 were nearly identical to calf thymus H3 and H4 with respect to net charge and molecular weight criteria, whereas the fungal histones H1, H2a and H2b were similar but not identical to the corresponding calf thymus histones. Amino acid analysis of A. nidulans histones H2a, H2b, and H4 showed them to be closely related to the homologous calf thymus histones. The mobility patterns of A. nidulans ribosomal basic proteins in three different electrophoretic systems were distinctly different from those of the fungal histones.

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Selected References

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  1. BURTON K. A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem J. 1956 Feb;62(2):315–323. doi: 10.1042/bj0620315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Berg R. A., Prockop D. J. Purification of (14C) protocollagen and its hydroxylation by prolyl-hydroxylase. Biochemistry. 1973 Aug 28;12(18):3395–3401. doi: 10.1021/bi00742a005. [DOI] [PubMed] [Google Scholar]
  3. Bradbury E. M., Carpenter B. G., Rattle H. W. Magnetic resonance studies of deoxyribonucleoprotein. Nature. 1973 Jan 12;241(5385):123–126. doi: 10.1038/241123a0. [DOI] [PubMed] [Google Scholar]
  4. Bradley D. M., Goldin H. H., Claybrook J. R. Histone analysis in Volvox. FEBS Lett. 1974 May 1;41(2):219–222. doi: 10.1016/0014-5793(74)81216-0. [DOI] [PubMed] [Google Scholar]
  5. Böhm E. L., Strickland W. N., Strickland M., Thwaits B. H., van der Westhuizen D. R., von Holt C. Purification of the five main calf thymus histone fractions by gel exclusion chromatography. FEBS Lett. 1973 Aug 15;34(2):217–221. doi: 10.1016/0014-5793(73)80797-5. [DOI] [PubMed] [Google Scholar]
  6. Charlesworth M. C., Parish R. W. The isolation of nuclei and basic nucleoproteins from the cellular slime mold Dictyostelium discoideum. Eur J Biochem. 1975 May;54(1):307–316. doi: 10.1111/j.1432-1033.1975.tb04141.x. [DOI] [PubMed] [Google Scholar]
  7. DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. 3. Complete amino acid sequence of pea seedling histone IV; comparison with the homologous calf thymus histone. J Biol Chem. 1969 Oct 25;244(20):5669–5679. [PubMed] [Google Scholar]
  8. Dwivedi R. S., Dutta S. K., Bloch D. P. Isolation and characterization of chromatin from Neurospora crassa. J Cell Biol. 1969 Oct;43(1):51–58. doi: 10.1083/jcb.43.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Elgin S. C., Weintraub H. Chromosomal proteins and chromatin structure. Annu Rev Biochem. 1975;44:725–774. doi: 10.1146/annurev.bi.44.070175.003453. [DOI] [PubMed] [Google Scholar]
  10. Fambrough D. M., Bonner J. On the similarity of plant and animal histones. Biochemistry. 1966 Aug;5(8):2563–2570. doi: 10.1021/bi00872a012. [DOI] [PubMed] [Google Scholar]
  11. Franco L., Johns E. W., Navlet J. M. Histones from baker's yeast. Isolation and fractionation. Eur J Biochem. 1974 Jun 1;45(1):83–89. doi: 10.1111/j.1432-1033.1974.tb03532.x. [DOI] [PubMed] [Google Scholar]
  12. Houston L. L. Amino acid analysis of stained bands from polyacrylamide gels. Anal Biochem. 1971 Nov;44(1):81–88. doi: 10.1016/0003-2697(71)90348-4. [DOI] [PubMed] [Google Scholar]
  13. Hsiang M. W., Cole R. D. The isolation of histone from Neurospora crassa. J Biol Chem. 1973 Mar 25;248(6):2007–2013. [PubMed] [Google Scholar]
  14. Iwai K., Shiomi H., Ando T., Mita T. The isolation of histone from Tetrahymena. J Biochem. 1965 Sep;58(3):312–314. doi: 10.1093/oxfordjournals.jbchem.a128206. [DOI] [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Leighton T. J., Dill B. C., Stock J. J., Phillips C. Absence of histones from the chromosomal proteins of fungi. Proc Natl Acad Sci U S A. 1971 Mar;68(3):677–680. doi: 10.1073/pnas.68.3.677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Louie A. J., Dixon G. H. Kinetics of phosphorylation and dephosphorylation of testis histones and their possible role in determining chromosomal structure. Nat New Biol. 1973 Jun 6;243(127):164–168. doi: 10.1038/newbio243164a0. [DOI] [PubMed] [Google Scholar]
  19. Mirsky A. E., Burdick C. J., Davidson E. H., Littau V. C. The role of lysine-rich histone in the maintenance of chromatin structure in metaphase chromosomes. Proc Natl Acad Sci U S A. 1968 Oct;61(2):592–597. doi: 10.1073/pnas.61.2.592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mohberg J., Rusch H. P. Isolation of the nuclear histones from the Myxomycete, Physarum polycephalum. Arch Biochem Biophys. 1969 Nov;134(2):577–589. doi: 10.1016/0003-9861(69)90320-8. [DOI] [PubMed] [Google Scholar]
  21. Panyim S., Bilek D., Chalkley R. An electrophoretic comparison of vertebrate histones. J Biol Chem. 1971 Jul 10;246(13):4206–4215. [PubMed] [Google Scholar]
  22. Panyim S., Chalkley R. High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys. 1969 Mar;130(1):337–346. doi: 10.1016/0003-9861(69)90042-3. [DOI] [PubMed] [Google Scholar]
  23. Panyim S., Chalkley R. The molecular weights of vertebrate histones exploiting a modified sodium dodecyl sulfate electrophoretic method. J Biol Chem. 1971 Dec 25;246(24):7557–7560. [PubMed] [Google Scholar]
  24. Panyim S., Sommer K. R., Chalkley R. Oxidation of the cysteine-containing histone F3. Detection of an evolutionary mutation in a conservative histone. Biochemistry. 1971 Oct 12;10(21):3911–3917. doi: 10.1021/bi00797a018. [DOI] [PubMed] [Google Scholar]
  25. Rizzo P. J., Noodén L. D. Chromosomal proteins in the dinoflagellate alga Gyrodinium cohnii. Science. 1972 May 19;176(4036):796–797. doi: 10.1126/science.176.4036.796. [DOI] [PubMed] [Google Scholar]
  26. Sung M. T., Dixon G. H. Modification of histones during spermiogenesis in trout: a molecular mechanism for altering histone binding to DNA. Proc Natl Acad Sci U S A. 1970 Nov;67(3):1616–1623. doi: 10.1073/pnas.67.3.1616. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Sung M., Smithies O. Differential elution of histones from gel-trapped nuclei. Biopolymers. 1969;7(1):39–58. doi: 10.1002/bip.1969.360070105. [DOI] [PubMed] [Google Scholar]
  28. Tonino G. J., Rozijn T. H. On the occurrence of histones in yeast. Biochim Biophys Acta. 1966 Aug 24;124(2):427–429. doi: 10.1016/0304-4165(66)90215-7. [DOI] [PubMed] [Google Scholar]
  29. Wintersberger U., Smith P., Letnansky K. Yeast chromatin. Preparation from isolated nuclei, histone composition and transcription capacity. Eur J Biochem. 1973 Feb 15;33(1):123–130. doi: 10.1111/j.1432-1033.1973.tb02663.x. [DOI] [PubMed] [Google Scholar]

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