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. 1979 Sep 1;181(3):585–591. doi: 10.1042/bj1810585

Studies on the high-mobility-group non-histone proteins from hen oviduct.

C S Teng, G K Andrews, C T Teng
PMCID: PMC1161198  PMID: 518542

Abstract

Nuclear high-mobility-group (HMG) proteins were isolated from hen oviduct. These were proteins HMG-1, -2, -3, -14 and -17, which are equivalent to the classification of calf thymus HMG proteins. Hen oviduct proteins HMG-1 and -2 were individually isolated by HCIO4.extraction and CM-Sephadex chromatographic separation. Their mol.wts. were determined as 28 000 and 27 000, respectively. The proteins have a high content of acidic and basic amino acids. The association of proteins HMG-1 and -2 with the genome of hen oviduct nuclei was probed by a limited digestion with nucleases. Hen oviduct nuclei were incubated with deoxyribonuclease I or micrococcal nuclease until 10% of the DNA was digested. The nuclear suspension was centrifuged and the contents of proteins HMG-1 and -2 in the supernatant and sediment fractions were analysed by polyacrylamide-gel electrophoresis. HMG proteins were found to be preferentially released by micrococcal-nuclease digestion rather than by deoxyribonuclease I.

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Selected References

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  1. Axel R., Cedar H., Felsenfield G. The structure of the globin genes in chromatin. Biochemistry. 1975 Jun 3;14(11):2489–2495. doi: 10.1021/bi00682a031. [DOI] [PubMed] [Google Scholar]
  2. Bloom K. S., Anderson J. N. Fractionation of hen oviduct chromatin into transcriptionally active and inactive regions after selective micrococcal nuclease digestion. Cell. 1978 Sep;15(1):141–150. doi: 10.1016/0092-8674(78)90090-9. [DOI] [PubMed] [Google Scholar]
  3. Burgoyne L. A., Mobbs J. D., Marshall A. J. Chromatin structure: a property of the higher structures of chromatin and in the time course of its formation during chromatin replication. Nucleic Acids Res. 1976 Dec;3(12):3293–3304. doi: 10.1093/nar/3.12.3293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bustin M., Hopkins R. B., Isenberg I. Immunological relatedness of high mobility group chromosomal proteins from calf thymus. J Biol Chem. 1978 Mar 10;253(5):1694–1699. [PubMed] [Google Scholar]
  5. Garel A., Axel R. Selective digestion of transcriptionally active ovalbumin genes from oviduct nuclei. Proc Natl Acad Sci U S A. 1976 Nov;73(11):3966–3970. doi: 10.1073/pnas.73.11.3966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Garel A., Zolan M., Axel R. Genes transcribed at diverse rates have a similar conformation in chromatin. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4867–4871. doi: 10.1073/pnas.74.11.4867. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Goodwin G. H., Johns E. W. Are the high mobility group non-histone chromosomal proteins associated with 'active' chromatin? Biochim Biophys Acta. 1978 Jun 22;519(1):279–284. doi: 10.1016/0005-2787(78)90081-3. [DOI] [PubMed] [Google Scholar]
  8. Goodwin G. H., Johns E. W. Isolation and characterisation of two calf-thymus chromatin non-histone proteins with high contents of acidic and basic amino acids. Eur J Biochem. 1973 Dec 3;40(1):215–219. doi: 10.1111/j.1432-1033.1973.tb03188.x. [DOI] [PubMed] [Google Scholar]
  9. Goodwin G. H., Nicolas R. H., Johns E. W. An improved large scale fractionation of high mobility group non-histone chromatin proteins. Biochim Biophys Acta. 1975 Oct 20;405(2):280–291. doi: 10.1016/0005-2795(75)90094-x. [DOI] [PubMed] [Google Scholar]
  10. Goodwin G. H., Sanders C., Johns E. W. A new group of chromatin-associated proteins with a high content of acidic and basic amino acids. Eur J Biochem. 1973 Sep 21;38(1):14–19. doi: 10.1111/j.1432-1033.1973.tb03026.x. [DOI] [PubMed] [Google Scholar]
  11. Goodwin G. H., Walker J. M., Johns E. W. Studies on the degradation of high mobility group non-histone chromosomal proteins. Biochim Biophys Acta. 1978 Jun 22;519(1):233–242. doi: 10.1016/0005-2787(78)90076-x. [DOI] [PubMed] [Google Scholar]
  12. Goodwin G. H., Woodhead L., Johns E. W. The presence of high mobility group non-histone chromatin proteins in isolated nucleosomes. FEBS Lett. 1977 Jan 15;73(1):85–88. [PubMed] [Google Scholar]
  13. Hewish D. R., Burgoyne L. A. The calcium dependent endonuclease activity of isolated nuclear preparations. Relationships between its occurrence and the occurrence of other classes of enzymes found in nuclear preparations. Biochem Biophys Res Commun. 1973 May 15;52(2):475–481. doi: 10.1016/0006-291x(73)90736-5. [DOI] [PubMed] [Google Scholar]
  14. Javaherian K., Liu J. F., Wang J. C. Nonhistone proteins HMG1 and HMG2 change the DNA helical structure. Science. 1978 Mar 24;199(4335):1345–1346. doi: 10.1126/science.628842. [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. LeStourgeon W. M., Rusch H. P. Localization of nucleolar and chromatin residual acidic protein changes during differentiation in Physarum polycephalum. Arch Biochem Biophys. 1973 Mar;155(1):144–158. doi: 10.1016/s0003-9861(73)80017-7. [DOI] [PubMed] [Google Scholar]
  18. Levy W B., Wong N. C., Dixon G. H. Selective association of the trout-specific H6 protein with chromatin regions susceptible to DNase I and DNase II: possible location of HMG-T in the spacer region between core nucleosomes. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2810–2814. doi: 10.1073/pnas.74.7.2810. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Levy B. W., Dixon G. H. Changes in the sequence diversity of polyadenylated cytoplasmic RNA during testis differentiation in rainbow trout (Salmo gairdnerii). Eur J Biochem. 1977 Mar 15;74(1):61–67. doi: 10.1111/j.1432-1033.1977.tb11366.x. [DOI] [PubMed] [Google Scholar]
  20. Levy W. B., Dixon G. H. A study of the localization of high mobility group proteins in chromatin. Can J Biochem. 1978 Jun;56(6):480–491. doi: 10.1139/o78-075. [DOI] [PubMed] [Google Scholar]
  21. Noll M. Subunit structure of chromatin. Nature. 1974 Sep 20;251(5472):249–251. doi: 10.1038/251249a0. [DOI] [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. Rabbani A., Goodwin G. H., Johns E. W. High mobility group non-histone chromosomal proteins from chicken erythrocytes. Biochem Biophys Res Commun. 1978 Mar 30;81(2):351–358. doi: 10.1016/0006-291x(78)91540-1. [DOI] [PubMed] [Google Scholar]
  24. Rabbani A., Goodwin G. H., Johns E. W. Studies on the tissue specificity of the high-mobility-group non-histone chromosomal proteins from calf. Biochem J. 1978 Aug 1;173(2):497–505. doi: 10.1042/bj1730497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ruiz-Carrillo A., Allfrey V. G. A method for the purification of histone fraction F3 by affinity chromatography. Arch Biochem Biophys. 1973 Jan;154(1):185–191. doi: 10.1016/0003-9861(73)90047-7. [DOI] [PubMed] [Google Scholar]
  26. Schaller H., Nüsslein C., Bonhoeffer F. J., Kurz C., Nietzschmann I. Affinity chromatography of DNA-binding enzymes on single-stranded DNA-agarose columns. Eur J Biochem. 1972 Apr 24;26(4):474–481. doi: 10.1111/j.1432-1033.1972.tb01789.x. [DOI] [PubMed] [Google Scholar]
  27. Shooter K. V., Goodwin G. H., Johns E. W. Interactions of a purified non-histone chromosomal protein with DNA and histone. Eur J Biochem. 1974 Sep 1;47(2):263–270. doi: 10.1111/j.1432-1033.1974.tb03690.x. [DOI] [PubMed] [Google Scholar]
  28. Spiker S., Mardian J. K., Isenberg I. Chomosomal HMG proteins occur in three eukaryotic kingdoms. Biochem Biophys Res Commun. 1978 May 15;82(1):129–135. doi: 10.1016/0006-291x(78)90586-7. [DOI] [PubMed] [Google Scholar]
  29. Sterner R., Boffa L. C., Vidali G. Comparative structural analysis of high mobility group proteins from a variety of sources. Evidence for a high mobility group protein unique to avian erythrocyte nuclei. J Biol Chem. 1978 Jun 10;253(11):3830–3836. [PubMed] [Google Scholar]
  30. Teng C. S., Gallagher K., Teng C. T. Isolation of a high-molecular-weight high-mobility-group-type non-histone protein from hen oviduct. Biochem J. 1978 Dec 15;176(3):1003–1006. doi: 10.1042/bj1761003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Vidali G., Boffa L. C., Allfrey V. G. Selective release of chromosomal proteins during limited DNAase 1 digestion of avian erythrocyte chromatin. Cell. 1977 Oct;12(2):409–415. doi: 10.1016/0092-8674(77)90117-9. [DOI] [PubMed] [Google Scholar]
  32. Walker J. M., Goodwin G. H., Johns E. W. The similarity between the primary structures of two non-histone chromosomal proteins. Eur J Biochem. 1976 Mar 1;62(3):461–469. doi: 10.1111/j.1432-1033.1976.tb10179.x. [DOI] [PubMed] [Google Scholar]
  33. Watson D. C., Peters E. H., Dixon G. H. The purification, characterization and partial sequence determination of a trout testis non-histone protein, HMG-T. Eur J Biochem. 1977 Mar 15;74(1):53–60. doi: 10.1111/j.1432-1033.1977.tb11365.x. [DOI] [PubMed] [Google Scholar]
  34. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  35. Weintraub H., Groudine M. Chromosomal subunits in active genes have an altered conformation. Science. 1976 Sep 3;193(4256):848–856. doi: 10.1126/science.948749. [DOI] [PubMed] [Google Scholar]

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