Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1982 Aug 25;10(16):5059–5072. doi: 10.1093/nar/10.16.5059

Influence of nonhistone chromatin protein HMG-1 on the enzymatic digestion of purified DNA.

K Shastri, P J Isackson, J L Fishback, M D Land, G R Reeck
PMCID: PMC320851  PMID: 6291002

Abstract

The effect of chicken erythrocyte High Mobility Group protein 1 (HMG-1) on the enzymatic hydrolysis of purified double-stranded and single-stranded bacteriophage lambda DNA was studied. HMG-1 was found to inhibit the digestion of single- and double-stranded DNA by S1 nuclease and DNase I, respectively. HMG-I increased the rate of hydrolysis of double-stranded DNA by micrococcal nuclease, particularly at low HMG-1/DNA ratios, and had little effect on the hydrolysis of single-stranded DNA by micrococcal nucleases, even at high HMG-1 DNA ratios. We also present a semi-quantitative estimate that HMG-1 and HMG-2 occur in chromatin from rapidly dividing, cultured rat hepatoma cells at about 8 times the level that they occur in adult rat liver chromatin.

Full text

PDF
5059

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alberts B. M., Frey L. T4 bacteriophage gene 32: a structural protein in the replication and recombination of DNA. Nature. 1970 Sep 26;227(5265):1313–1318. doi: 10.1038/2271313a0. [DOI] [PubMed] [Google Scholar]
  2. Ando T. A nuclease specific for heat-denatured DNA in isolated from a product of Aspergillus oryzae. Biochim Biophys Acta. 1966 Jan 18;114(1):158–168. doi: 10.1016/0005-2787(66)90263-2. [DOI] [PubMed] [Google Scholar]
  3. Bidney D. L., Reeck G. R. Analysis of the effectiveness of sodium chloride in dissociating non-histone chromatin proteins of cultured hepatoma cells. Biochim Biophys Acta. 1978 Dec 21;521(2):753–761. doi: 10.1016/0005-2787(78)90314-3. [DOI] [PubMed] [Google Scholar]
  4. Bidney D. L., Reeck G. R. Purification from cultured hepatoma cells of two nonhistone chromatin proteins with preferential affinity for single-stranded DNA: apparent analogy with calf thymus HMG proteins. Biochem Biophys Res Commun. 1978 Dec 14;85(3):1211–1218. doi: 10.1016/0006-291x(78)90671-x. [DOI] [PubMed] [Google Scholar]
  5. Blobel G., Potter V. R. Nuclei from rat liver: isolation method that combines purity with high yield. Science. 1966 Dec 30;154(3757):1662–1665. doi: 10.1126/science.154.3757.1662. [DOI] [PubMed] [Google Scholar]
  6. Bustin M., Neihart N. K. Antibodies against chromosomal HMG proteins stain the cytoplasm of mammalian cells. Cell. 1979 Jan;16(1):181–189. doi: 10.1016/0092-8674(79)90199-5. [DOI] [PubMed] [Google Scholar]
  7. Christiansen C., Baldwin R. L. Catalysis of DNA reassociation by the Escherichia coli DNA binding protein: A polyamine-dependent reaction. J Mol Biol. 1977 Sep 25;115(3):441–454. doi: 10.1016/0022-2836(77)90164-4. [DOI] [PubMed] [Google Scholar]
  8. Gold L., O'Farrell P. Z., Russel M. Regulation of gene 32 expression during bacteriophage T4 infection of Escherichia coli. J Biol Chem. 1976 Nov 25;251(22):7251–7262. [PubMed] [Google Scholar]
  9. 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]
  10. Gordon J. S., Bruno J., Lucas J. J. Heterogeneous binding of high mobility group chromosomal proteins to nuclei. J Cell Biol. 1981 Feb;88(2):373–379. doi: 10.1083/jcb.88.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hell A., Birnie G. D., Slimming T. K., Paul J. Controlled fragmentation of DNA by DNase I. Anal Biochem. 1972 Aug;48(2):369–377. doi: 10.1016/0003-2697(72)90089-9. [DOI] [PubMed] [Google Scholar]
  12. Huang W. M., Lehman I. R. On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. J Biol Chem. 1972 May 25;247(10):3139–3146. [PubMed] [Google Scholar]
  13. Isackson P. J., Bidney D. L., Reeck G. R., Neihart N. K., Bustin M. High mobility group chromosomal proteins isolated from muclei and cytosol of cultured hepatoma cells are similar. Biochemistry. 1980 Sep 16;19(19):4466–4471. doi: 10.1021/bi00560a013. [DOI] [PubMed] [Google Scholar]
  14. Isackson P. J., Clow L. G., Reeck G. R. Comparison of the salt dissociations of high molecular weight HMG non-histone chromatin proteins from double-stranded DNA and from chromatin. FEBS Lett. 1981 Mar 9;125(1):30–34. doi: 10.1016/0014-5793(81)80989-1. [DOI] [PubMed] [Google Scholar]
  15. Isackson P. J., Debold W. A., Reeck G. R. Isolation and separation of chicken erythrocyte high mobility group non-histone chromatin proteins by chromatography on phosphocellulose. FEBS Lett. 1980 Oct 6;119(2):337–342. doi: 10.1016/0014-5793(80)80284-5. [DOI] [PubMed] [Google Scholar]
  16. Isackson P. J., Fishback J. L., Bidney D. L., Reeck G. R. Preferential affinity of high molecular weight high mobility group non-histone chromatin proteins for single-stranded DNA. J Biol Chem. 1979 Jul 10;254(13):5569–5572. [PubMed] [Google Scholar]
  17. Jackson J. B., Pollock J. M., Jr, Rill R. L. Chromatin fractionation procedure that yields nucleosomes containing near-stoichiometric amounts of high mobility group nonhistone chromosomal proteins. Biochemistry. 1979 Aug 21;18(17):3739–3748. doi: 10.1021/bi00584a015. [DOI] [PubMed] [Google Scholar]
  18. Javaherian K., Sadeghi M., Liu L. F. Nonhistone proteins HMG1 and HMG2 unwind DNA double helix. Nucleic Acids Res. 1979 Aug 10;6(11):3569–3580. doi: 10.1093/nar/6.11.3569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Levy B. W., Connor W., Dixon G. H. A subset of trout testis nucleosomes enriched in transcribed DNA sequences contains high mobility group proteins as major structural components. J Biol Chem. 1979 Feb 10;254(3):609–620. [PubMed] [Google Scholar]
  20. STUDIER F. W. SEDIMENTATION STUDIES OF THE SIZE AND SHAPE OF DNA. J Mol Biol. 1965 Feb;11:373–390. doi: 10.1016/s0022-2836(65)80064-x. [DOI] [PubMed] [Google Scholar]
  21. Seyedin S. M., Kistler W. S. Levels of chromosomal protein high mobility group 2 parallel the proliferative activity of testis, skeletal muscle, and other organs. J Biol Chem. 1979 Nov 25;254(22):11264–11271. [PubMed] [Google Scholar]
  22. 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]
  23. Vogt V. M. Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae. Eur J Biochem. 1973 Feb 15;33(1):192–200. doi: 10.1111/j.1432-1033.1973.tb02669.x. [DOI] [PubMed] [Google Scholar]
  24. 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]
  25. Wu J. R., Yeh Y. C. Requirement of a functional gene 32 product of bacteriophage T4 in UV, repair. J Virol. 1973 Oct;12(4):758–765. doi: 10.1128/jvi.12.4.758-765.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES