Abstract
Proteins extracted from chicken erythrocyte chromatin with 0.35 M NaCl were subjected to sequential chromatography on columns containing immobilized double-stranded and single-stranded DNA's. Two-dimensional electrophoresis of protein fractions revealed that HMG-14 and HMG-17 are among the proteins that are retained by the single-stranded DNA column in 0.2 M NaCl/l mM Tris-Cl (pH 7.5) after having failed to be retained by the double-stranded column under the same conditions. That suggests that those two proteins possess preferential affinity for single-stranded DNA. Further evidence for that was provided by chromatography of purified HMG-14 and of purified HMG-17 on single-stranded and double-stranded DNA columns. We discuss the possible relevance of our results to suggested functions of HMG-14 and HMG-17.
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- Abercrombie B. D., Kneale G. G., Crane-Robinson C., Bradbury E. M., Goodwin G. H., Walker J. M., Johns E. W. Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA. Eur J Biochem. 1978 Mar;84(1):173–177. doi: 10.1111/j.1432-1033.1978.tb12154.x. [DOI] [PubMed] [Google Scholar]
- Baker C., Isenberg I., Goodwin G. H., Johns E. W. Physical studies of the nonhistone chromosomal proteins HMG-U and HMG-2. Biochemistry. 1976 Apr 20;15(8):1645–1649. doi: 10.1021/bi00653a009. [DOI] [PubMed] [Google Scholar]
- Bidney D. L., Reeck G. R. Association products and conformations of salt-dissociated and acid-extracted histones. A two-phase procedure for isolating salt-dissociated histones. Biochemistry. 1977 May 3;16(9):1844–1849. doi: 10.1021/bi00628a013. [DOI] [PubMed] [Google Scholar]
- 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]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Cary P. D., Crane-Robinson C., Bradbury E. M., Javaherian K., Goodwin G. H., Johns E. W. Conformational studies of two non-histone chromosomal proteins and their interactions with DNA. Eur J Biochem. 1976 Mar 1;62(3):583–590. doi: 10.1111/j.1432-1033.1976.tb10193.x. [DOI] [PubMed] [Google Scholar]
- Gazit B., Panet A., Cedar H. Reconstitution of a deoxyribonuclease I-sensitive structure on active genes. Proc Natl Acad Sci U S A. 1980 Apr;77(4):1787–1790. doi: 10.1073/pnas.77.4.1787. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Germond J. E., Hirt B., Oudet P., Gross-Bellark M., Chambon P. Folding of the DNA double helix in chromatin-like structures from simian virus 40. Proc Natl Acad Sci U S A. 1975 May;72(5):1843–1847. doi: 10.1073/pnas.72.5.1843. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Hosoda J., Moise H. Purification and physicochemical properties of limited proteolysis products of T4 helix destabilizing protein (gene 32 protein). J Biol Chem. 1978 Oct 25;253(20):7547–7558. [PubMed] [Google Scholar]
- 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]
- 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]
- 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]
- Javaherian K., Amini S. Conformational study of calf thymus HMG14 nonhistone protein. Biochem Biophys Res Commun. 1978 Dec 29;85(4):1385–1391. doi: 10.1016/0006-291x(78)91157-9. [DOI] [PubMed] [Google Scholar]
- Jensen D. E., Kelly R. C., von Hippel P. H. DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures. J Biol Chem. 1976 Nov 25;251(22):7215–7228. [PubMed] [Google Scholar]
- 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]
- Litman R. M. A deoxyribonucleic acid polymerase from Micrococcus luteus (Micrococcus lysodeikticus) isolated on deoxyribonucleic acid-cellulose. J Biol Chem. 1968 Dec 10;243(23):6222–6233. [PubMed] [Google Scholar]
- O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
- O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
- 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]
- Peters E. H., Levy-Wilson B., Dixon G. H. Evidence for the location of high mobility group protein T in the internucleosomal linker regions of trout testis chromatin. J Biol Chem. 1979 May 10;254(9):3358–3361. [PubMed] [Google Scholar]
- Sandeen G., Wood W. I., Felsenfeld G. The interaction of high mobility proteins HMG14 and 17 with nucleosomes. Nucleic Acids Res. 1980 Sep 11;8(17):3757–3778. doi: 10.1093/nar/8.17.3757. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Walker J. M., Gooderham K., Hastings J. R., Mayes E., Johns E. W. The primary structures of non-histone chromosomal proteins HMG 1 and 2. FEBS Lett. 1980 Dec 29;122(2):264–270. doi: 10.1016/0014-5793(80)80453-4. [DOI] [PubMed] [Google Scholar]
- Walker J. M., Goodwin G. H., Johns E. W. The primary structure of the nucleosome-associated chromosomal protein HMG 14. FEBS Lett. 1979 Apr 15;100(2):394–398. doi: 10.1016/0014-5793(79)80378-6. [DOI] [PubMed] [Google Scholar]
- Walker J. M., Hastings J. R., Johns E. W. The primary structure of a non-histone chromosomal protein. Eur J Biochem. 1977 Jun 15;76(2):461–468. doi: 10.1111/j.1432-1033.1977.tb11616.x. [DOI] [PubMed] [Google Scholar]
- Weisbrod S., Groudine M., Weintraub H. Interaction of HMG 14 and 17 with actively transcribed genes. Cell. 1980 Jan;19(1):289–301. doi: 10.1016/0092-8674(80)90410-9. [DOI] [PubMed] [Google Scholar]
- Weisbrod S., Weintraub H. Isolation of a subclass of nuclear proteins responsible for conferring a DNase I-sensitive structure on globin chromatin. Proc Natl Acad Sci U S A. 1979 Feb;76(2):630–634. doi: 10.1073/pnas.76.2.630. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weisbrod S., Weintraub H. Isolation of actively transcribed nucleosomes using immobilized HMG 14 and 17 and an analysis of alpha-globin chromatin. Cell. 1981 Feb;23(2):391–400. doi: 10.1016/0092-8674(81)90134-3. [DOI] [PubMed] [Google Scholar]


